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About USC
USC Today
Located near the heart of Los Angeles, the University of Southern California is one of the nation's top private research universities.
Since its establishment in 1880, USC has conferred degrees on more than a quarter-million students -- leaders who have helped Southern California grow to become a national trendsetter in public policy, economic and business affairs, urban planning and engineering, scientific research, health care and the arts.
Today, USC and its graduates are continuing this tradition of leadership -- developing innovative classroom techniques, exploring new fields of scholarly investigation, and establishing a widening network of service and partnership among the nations of the Pacific Rim.
The traditional function of the university is to teach students -- in the classroom, studio, laboratory, seminar room, on the playing field, and where they live. USC is committed to the principle that this educational mission is most effectively carried out in a context that encourages the creation of new knowledge.
USC places a premium on research and scholarship and on the professional and scholarly credentials of its faculty. Since 1969, the university has been a member of the Association of American Universities, the elective body that unites the 62 premier research universities in the United States and Canada.
USC is accredited by the Western Association of Schools and Colleges, 985 Atlantic Ave., Suite 100, Alameda, CA 94501, (510) 748-9001. Students may review the university's accreditation documents by contacting Jerome Walker, Associate Provost.
The university has traditionally performed a wide variety of roles in service to its communities -- contributing to the welfare of its own members, as well as to Southern California and the nation. In particular, the university's network of affiliated hospitals and its partnerships with business and community organizations enable USC to make its expertise available to the community at large.
Academic ProgramsThe University of Southern California maintains a tradition of academic strength at all levels -- from the earliest explorations of the undergraduate to the advanced scholarly research of the postdoctoral fellow.
USC offers bachelor's degrees in 89 undergraduate majors as well as master's, doctoral and professional degrees in 236 areas of study. Students may select from a variety of major degree combinations in the College of Letters, Arts and Sciences, in the Graduate School and under the direction of the university's 17 professional schools.
The heart of USC's liberal education program is the College of Letters, Arts and Sciences. The largest of USC's academic divisions -- both in student enrollment and faculty -- the college encompasses more than 30 academic departments and programs serving over 5,900 undergraduates and more than 1,500 graduate students. In addition to the undergraduate degrees offered by the college, many of the university's professional schools also offer bachelor's degree programs.
FacultyUSC has more than 3,000 full-time faculty. In addition, approximately 3,180 volunteer faculty members are affiliated with the Keck School of Medicine of USC, and 430 volunteer faculty are affiliated with the USC School of Pharmacy. Research, teaching and service are supported by a staff of 7,900.
USC's faculty includes members of the National Academy of Sciences (10), National Academy of Engineering (25), National Academy of Public Administration (6), and the Institute of Medicine (10). More than 200 faculty members have received prestigious academic and professional awards from organizations as varied as the National Institutes of Health, the National Science Foundation, the Alfred P. Sloan Foundation, the John Simon Guggenheim Foundation and the Academy of Motion Picture Arts and Sciences. In 1994, USC Professor George A. Olah received the Nobel Prize in Chemistry.
StudentsDiversity is the hallmark of the USC student community. USC students come from all 50 states and nearly 150 countries. There are 32,000 students enrolled at the university including 16,500 undergraduate and 15,500 graduate and professional students. In fall 2004, 54 percent of new freshmen were from California. Approximately 32 percent of the university's total enrollment is composed of American minorities; a further 17 percent are international students. USC is consistently near the top among American universities in international enrollment. Among undergraduates, 50 percent are men, 50 percent are women.
The average SAT score of the 2004 enrolled freshman class was 1350. The average GPA was 4.0. In fall 2004, 179 freshmen were National Merit Scholars, 14 were National Achievement Scholars and 33 were National Hispanic Scholars.
USC students consistently earn nationally competitive scholarships and fellowships including Rhodes, Marshall, Fulbright and Truman scholarships.
Research SupportEach year, USC's distinguished faculty and modern facilities attract substantial external funding for educational and scientific research. USC currently ranks in the top 10 among private universities receiving government funding for research and development support and in the top 20 among all universities -- with a 2004 total of nearly $420 million.
LibrariesThe USC libraries house over 4.2 million volumes, more than 3 million photographs, and just over 6 million microforms, and subscribe to nearly 30,000 current journals.
The largest of the USC libraries is the Doheny Memorial Library, which contains the research collections for most of the social sciences and humanities materials. The Doheny Memorial Library also houses the Research Services Center, Cinema-TV Library, the Music Library and Special Collections.
In addition to the Doheny Library, the USC libraries include a number of specialized research libraries that serve the unique research needs of the campus. Most of these are located near the school or department they serve. Three independent campus libraries are devoted to specialized collections for their respective professions: the Asa V. Call Law Library, the Eileen and Kenneth T. Norris Medical Library and the Jennifer Ann Wilson Dental Library and Learning Center.
The Thomas and Dorothy Leavey Library, one of the most technologically sophisticated libraries in the world, features: a core collection of books and journals, two electronic information commons with nearly 200 computer workstations, more than 50 collaborative workspaces, two hands-on learning classrooms, a multimedia auditorium, and more than 1,400 reader seats in a variety of formal and informal arrangements. Designed to support undergraduate learning, Leavey provides faculty and students with tools to accomplish research using both traditional and electronic resources. Within Leavey, the James Irvine Foundation Center for Scholarly Technology provides faculty with assistance in using technology and information resources to develop materials for instruction and scholarly research.
The USC libraries have noteworthy collections in the areas of cinema, international and public affairs, American literature, regional history, marine science, philosophy, Latin American studies, and Korean studies. The Feuchtwanger Memorial Library features an extensive collection of Lion Feuchtwanger's own works along with the rarest books from his library. The USC libraries are also home to the Boeckmann Center for Iberian and Latin American Studies, as well as an extensive collection of photographs chronicling the history of Southern California. A complete list of all USC libraries and updated library hours is available online at www.usc.edu/isd/libraries.
The USC libraries are the administrative hub of the Southern California Electronic Libraries Consortium. USC is a member of the Research Libraries Group, an international association of major universities and research institutions. In addition, USC maintains borrowing agreements with Hebrew Union College, the Los Angeles County Museum of Natural History Library, California State University, Los Angeles, Caltech and UCLA.
USC's digital library resources, available online at www.usc.edu/isd/elecresources, include a collection of article indexes, catalogues, dictionaries, encyclopedias, electronic journals and visual materials. USC's online library catalogue, Homer, provides a list of books, periodicals, government documents and dissertations held in libraries on the University Park campus. The new Scholar's Portal enables simultaneous searching of selected research databases, including Homer and core bibliographic tools in all major subject areas. To access these resources and learn about additional services, visit library.usc.edu.
USC's Ask-A-Librarian service provides professional reference assistance to students, faculty and staff. Patrons receive expert answers -- via phone, email, online "chat" sessions or in person. Ask-A-Librarian is located online at www.usc.edu/isd/askalibrarian.
Computing ResourcesThe Information Services Division (ISD) oversees the university's libraries, computer resources, telecommunications services, licensed database and software collections, and public computing centers and networks.
ISD is responsible for serving the community's technology needs for instruction and research, access to the Internet, email, and print and digital library resources at public computing centers. These centers are equipped with the latest technology to ensure that the USC community has access to the resources it needs.
In order to access computing services and library privileges, new students must obtain a USCard. Students may obtain this identification card at the USCard customer service office located in the Commons lobby. Students must also activate their free USC account at www.usc.edu/isd/firstlogin. Complete information about any of the resources and services provided by ISD is available online at www.usc.edu/isd.
Home ConnectionAll the rooms in USC residence halls, as well as some areas of Leavey Library and the Marshall School of Business, are connected to ResNet, a high-speed computer network. The ResNet connection allows students to bypass their modem and enjoy free, high-speed (10 megabits per second) Internet access.
Students who live off-campus may access the Internet via a computer. USC has more than 1,000 modems that students may dial into for access to the Internet, free of charge. USC's Virtual Private Network (VPN) client is available to access restricted USC resources for students who use another Internet service provider. This application can be downloaded at http://software.usc.edu. Information on connecting to USC can be found at www.usc.edu/isd/it/connect.
USC WirelessMost common areas at USC -- including libraries, auditoriums and eateries -- are configured for wireless technology. New locations are being added continuously. An updated list of the locations where students can connect without plugging in is available at www.usc.edu/isd/it/wireless.
To access the new wireless technology, users need an activated USC account and a wireless card, available at the University Bookstore. For ISD-supported cards, documentation is available at www.usc.edu/isd/it/wireless. The wireless card must then be registered at a public computing center or library and configured with virtual private network (VPN) software, which may be downloaded free-of-charge from http://software.usc.edu. The following computer platforms are currently configured to access the USC wireless network: Windows XP and 2000, and Mac OS 9.0.4 through Mac OS X.
TOTALe (Blackboard)The Trojan Online Teaching and Learning Environment (TOTALe) Web site (http://totale.usc.edu) is the online learning portal used by many USC professors to provide electronic copies of course materials, syllabi, reading materials and handouts. TOTALe, also known as Blackboard, allows students to participate in an online discussion or take a quiz with automatic grading and immediate feedback.
Computing AssistanceISD's Information Technology Services (www.usc.edu/isd/it) offers online computing documentation on a variety of topics. Printed guides are available in public computing centers and the Leavey Library Information Commons.
Software at USCThe university offers a wide range of software available for download, for purchase and for use in ISD's public computing centers. To learn more, visit http://software.usc.edu.
Computer WorkshopsAdventures in Information, an ongoing series of non-credit workshops on computer software and operating systems, is offered throughout the academic year at no cost to students (www.usc.edu/isd/adventures). The hands-on training sessions cover popular topics including Web page creation, image editing and statistics software.
InformationFor more information about computing resources, users may contact the Customer Support Center by calling (213) 740-5555 or emailing firstname.lastname@example.com. Additional assistance also is available at the service desk of any public computing center.
Hospitals and Patient CareThe schools of Medicine, Dentistry and Pharmacy, and the health professions departments of Biokinesiology and Physical Therapy, and Occupational Science and Occupational Therapy train professionals in the health care fields, conduct original research in all aspects of biomedicine and health care and provide high quality patient care to the Southern California community.
Health care facilities on the Health Sciences campus include the USC/Norris Comprehensive Cancer Center and Hospital, the USC University Hospital, the USC Healthcare Consultation Centers I and II and the Doheny Eye Institute. The 293-bed University Hospital is an ultra-modern hospital that offers many specialized services and procedures that are beyond the scope of most community hospitals.
The Keck School of Medicine also provides medical staffing for the nearby Los Angeles County+USC Medical Center, which is one of the nation's largest teaching hospitals. Owned and operated by Los Angeles County, the medical center's specialized facilities include a state-of-the-art burn center, a Level III neo-natal intensive care unit, a Level I trauma service and an HIV/AIDS outpatient center that annually cares for more than 4,000 patients.
Community RelationsUSC is an active partner in efforts to enhance the social, economic, physical and cultural aspects of the neighborhoods adjacent to both the University Park and Health Sciences campuses.
To carry out these efforts, USC Civic and Community Relations (USCCCR) assists USC academic and administrative units to implement the five university community initiatives in partnership with community agencies, leaders and public officials. These initiatives encourage more entrepreneurs to establish businesses in the immediate vicinity of the two campuses; provide special educational, cultural and developmental opportunities for children who live in the immediate neighborhoods; work with neighbors, city and county officials, and the Los Angeles Police Department to provide safer streets in the areas surrounding the two campuses; encourage more USC employees to own and occupy housing in the immediate vicinity of the two campuses; and strive to employ at USC more persons who live in the immediate neighborhoods.
USCCCR provides resources that strengthen the communities around USC's campuses, deepen USC's ties to these diverse communities, and foster positive relations between USC and those people who are most directly affected by USC's presence in these neighborhoods.
More than 265 community service programs administered by USC and affiliated institutions serve more than 430,000 persons and provide volunteer opportunities for more than 40,000 USC students, faculty, staff and alumni and friends each year. These volunteers contribute more than 1.2 million volunteer hours. Areas of activity include arts and culture, athletics and recreation, child care, children and family, business and economic development, communication and media, criminal justice and legal education, employment, environmental, health, housing, human relations, legal, literacy, older adult, public safety, scholarships and awards, technology, volunteer and community service.
Model programs such as the USC Family of Schools, the USC Joint Educational Project, Kid Watch, USC Mission Science, USC After School Sports Connection, and the Neighborhood Academic Initiative are a few of the innovative university-community partnerships that are making a real difference in the lives of the university's neighbors.
Information about these community service programs and data about the USC neighborhoods can be obtained on USCCCR's Web site (www.usc.edu/ext-relations/ccr and www.usc.edu/neighborhoods/community/programs).
From 1994 to 2002 USC employees contributed nearly $4.8 million through the USC Good Neighbors Campaign, which benefited 141 USC-community partnership projects.
USC is committed to working in partnership with its neighbors to build a thriving and safe social and physical environment in Central and East Los Angeles.
Cultural LifeUSC and its graduates play an important role in making Los Angeles one of the world's great centers for the arts. The schools of Music and Theatre produce a regular series of concerts, operas, musicals, plays and other events. There are three major music, drama and cinema theatres on campus. For up-to-date information on cultural events at USC, call the University Ticket Office at (213) 740-7111 or visit the arts Web site (www.usc.edu/info/arts).
AthleticsUSC sponsors nine varsity sports for men and 10 for women, involving more than 500 of the nation's top-ranked athletes. In their pursuit of athletic and academic excellence, USC varsity teams have won more national championships than all but two NCAA member institutions: 20 women's team titles and 85 men's team titles -- including 11 unofficial football titles. USC is one of only three universities in intercollegiate athletic history to win at least five national championships in one year (1962-63 and 1976-77). Fifty USC athletes have been awarded NCAA postgraduate scholarships.
In Olympic competition, USC has fielded more athletes than any other institution. Since 1904, 357 Trojan athletes have participated in the Olympic Games, accumulating a total of 112 gold, 64 silver and 58 bronze medals.
At least one USC athlete has won a gold medal in every summer Olympiad since 1912, making USC the only university in the world with this distinction.
USC Alumni AssociationAll USC graduates are members of the USC Alumni Association, which is dedicated to serving the university's close to 200,000 alumni, lifelong and worldwide. Trojan alumni span all 50 states and virtually every region of the world and are leaders in their chosen fields. Distinguished alumni include former U.S. Secretary of State Warren Christopher, astronaut Neil Armstrong, architect Frank Gehry, opera singer Marilyn Horne, symphony conductor Michael Tilson Thomas, film director George Lucas, baseball legend Mark McGwire and comedian Will Ferrell.
The USC Alumni Association offers a broad portfolio of programs and services to help alumni stay connected to USC and one another. These include: a worldwide network of alumni clubs, career assistance, a searchable online alumni directory, free lifetime email forwarding, organized volunteer opportunities, alumni travel programs and class reunions.
The association was founded in 1923 and is headquartered in Widney Alumni House, the oldest university building in Southern California. For more information, call (213) 740-2300 or visit the USC Alumni Association Web site at http://alumni.usc.edu.
University Park CampusLocated at the same site since USC's establishment in 1880 on eight acres of land in the city of Los Angeles, the University Park campus has grown to its present size of 235 acres. Situated three miles south of the Los Angeles Civic Center, the campus is adjacent to the museums and recreational facilities of Exposition Park and is served by a network of freeways that provides access to most cultural, business and recreational areas of Southern California.
The University Park campus consists of 201 major buildings and residential halls totaling approximately 7.9 million gross square feet. Additional university buildings are located off campus, in the immediate vicinity.
Health Sciences CampusLocated three miles from downtown Los Angeles, the USC Health Sciences campus is a focal point for students, patients and scientists from around the world. Here a blend of clinical, classroom and laboratory resources combines to form a dynamic, interactive environment that is shaping the future of health care.
The 50-acre Health Sciences campus is home to the region's first and oldest medical and pharmacy schools, as well as acclaimed programs in biokinesiology and physical therapy and occupational therapy. In addition to Los Angeles County+USC Medical Center, the primary teaching hospital for the Keck School of Medicine for more than a century, the campus includes several state-of-the-art patient-care facilities, among them USC/Norris Comprehensive Cancer Center and Hospital, USC University Hospital and Doheny Eye Institute. Activities of USC faculty, residents and students also extend beyond the campus -- to affiliated hospitals and health care providers throughout Southern California, and to the USC University Park campus, a collaborative partner in numerous health sciences-related programs.
Other LocationsOther teaching facilities include the Hawaii Center, Orange County Center, Sacramento Center, and the Wrigley Marine Science Center on Santa Catalina Island.
Hawaii Center (808) 423-3123, 900 Hanger Avenue, Building 2060, Hickam Air Force Base, HI 96835-5246, Education.
Orange County Center (949) 437-0000, 2300 Michelson, Irvine, CA 92612, Business, Education, Pharmacy and Social Work.
Sacramento Center (916) 442-6911, 1201 J Street, Sacramento, CA 95814, Policy, Planning, and Development and Education.
Wrigley Marine Science Center at Catalina (310) 510-1364, Wrigley Marine Science Center, P.O. Box 5069, Avalon, CA 90704.


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Hiawatha National Forest
Contact Information
Supervisors Office
820 Rains Drive
Gladstone, MI 49837
Phone: 906-428-5800
Find our Offices
Stay Connected
Contact Us
Monocle Lake Campground has something for everyone. Monocle Lake is a perfect place to use as a home-base while visiting the many recreational opportunities available in the Sault Ste. Marie area, as well as exploring the Whitefish Bay National Scenic Byway all the way to Tahquamenon Falls. Monocle Lake offers a quiet, relaxing place to fish, swim, hike, and just enjoy the out of doors while camped along the shores of a lovely inland lake. Link to Campground Map
From the intersection of M-28 and I-75 drive 15.6 miles west on M-28 to Ranger Road (FH-87). Turn right (north) and drive 6.2 miles on Ranger Road to Lake Shore Drive (forest Highway 42). Turn right (east) on Lake Shore Drive and drive 6.7 miles on FR 3699. Turn right (west) on FR 3699 and drive 1 mile to Monocle Lake Campground.
Map showing recreational areas.
Map Information
Monocle Lake Campground offers 39 campsites in a northern hardwood, aspen, red maple, and white birch setting. All sites have hardened surfaces and tent pads to accommodate accessibility needs. Accessible tables, fire rings, and lantern posts are available at each site. Accessible pressurized water and pit toilets are conveniently spaced throughout the recreation area.
The lake is 172 acres, 40-45 ft. deep, and populated with walleye, small mouth bass, pike, and perch. There are two man-made reefs on the east shore adjacent to the campground. No diving is allowed off the pier. Swimming at or near the pier is discouraged.
Monocle Lake Interpretive Trail 14.5 miles
The picnic/swim area is easily accessible from the spacious 60 vehicle day-use parking area. Tables, grills, and pressurized water are provided as well as accessible toilet facilities. The day-use area can be accessed from the campground by interconnecting pathways.
A boat launch and parking area is located between the campground and the day-use area.
The swim area is easily accessible from the spacious 60 vehicle day-use parking area. Lifeguards are not present. Children should be accompanied in the water by an adult at all times.
Related Information
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subset: commoncrawl


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AISD to Host Hispanic Futures Conference
Workshops and Services for Families Help Ensure Student Success
AUSTIN, Texas—Austin ISD has partnered with the City of Austin, Austin Energy and Con Mi Madre to offer the Hispanic Futures Conference, which provides Hispanic students—and their families—with the tools and resources they need to succeed in college, career and life.
What: This year's theme is "Making the Grade: Tackling Academics and Much More This School Year." The conference will include break-out sessions on topics such as academics, time management and graduation plans. It also includes workshops for students and families about taking advantage of support services and extracurricular activities.
Who: The keynote will be delivered by Hispanic engagement expert Armando Rayo, author of "Austin Breakfast Tacos: The Story of the Most Important Taco of the Day."
When: 8:30 a.m. to 12:30 p.m., Saturday, Sept. 21
Where: Martin Middle School, 1601 Haskell Dr.
Background: AISD works with community partners to provide information, materials and interactive experiences that can help students and families focus their efforts on activities that will pave the way for a successful future.
About 60 percent of AISD students are Hispanic. According to an AISD Department of Research and Evaluation study, 28 percent of Hispanic seniors indicated that parent expectations was the most important factor keeping them in school, compared with 16 percent of non-Hispanic seniors.
The conference is free for AISD families. For more information, please visit www.hispanicfutures.com or contact the AISD Office of Schools at 414-8729.


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Home / Student Life / Health / Nutrition Articles
Health / Nutrition Articles
Top 10 College Towns with the Best Pizza
Did your favorite pizza place make the list?
To-Do List: Starting a New Semester
It's hard to keep track of everything you need to do, so making a list is helpful!
Brain Food: 20 Healthy, Affordable Study Snacks
Many of these snacks are accessible in college meal programs - or anywhere else, for that matter.
10 Things You Should Do Over Holiday Break
While there is some value in getting shuteye, there's only so much rest necessary and, to be fair, you do have other, much more important things to do.
Surviving the Holidays
You may need to embellish just a little with some politically correct answers because you'd never want to offend or disappoint great aunt Gertrude.
Your College Experiences Checklist
Take on new experiences and implement on a "no regrets" policy to ensure you gain the most from your college experience.
How to Become a Morning Person
Once you become a morning person, you'll feel ready to conquer all day, every day.
Study Reveals College Students Perform Better in Later Classes
Falling asleep in class? It's not laziness; it's biology.
Helpful Student Health Tips
Staying healthy can be a challenge but, with a few simple guidelines, is possible.
Student Stress Busters
Stress may be a part of our everyday lives, but that doesn't mean it's unmanageable.
Top 10 Coolest College Dining Halls
Meal plans at these schools are worth he investment.
The Most Underutilized Campus Resources You Should Use
Most students don't realize how many resources are actually available at most colleges campuses across the country. Take advantage of the resources offered by your school - you'll be glad you did!
How to Refresh Your Mind Over Winter Break
Just what is the best way to refresh your brain while also remaining sharp for the spring term?
10 Scientific Reasons to Get a Good Night's Sleep
These scientifically-backed reasons prove that just a little more sleep can have a positive impact on your student life.
Senioritis: Getting Over the Hump & Out of the Slump
Every high school senior experiences it at some point or another: the senioritis slump.
Timeless Advice for College Success
What would some of the greatest minds of all time say to students about to embark on the college journey?
Stress Relief for Students
Discover some recommended methods of simple stress relief for students.
The Problem with Study Drugs
In pursuit of academic excellence, it's become the go-to common-but-highly-illegal practice among college students to abuse prescription stimulant drugs.
What NOT to Do During Finals Week
Avoid these harmful habits, which could negatively impact your studying routine.
Dealing with a College Cold
Getting sick is a part of life, but getting sick in college tends to simply add to our stress.


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4319 Puget Drive, Vancouver MLS®: R2277836
View, View, View! NORTH SHORE MOUNTAIN, CITY AND SOME WATER VIEW! Renovated! Updated kitchen, bathrooms, inside & outside painting. H/W floors, lighting fixtures. Spacious master bedroom with office & rooftop deck on top floor. Bright and spacious contemporary layout. Bonus: Large crawl space for storage. Excellent park like landscaping in front. The home boasts mature garden & wonderful decks to capture the Mountain, City & Water Views. Minutes to Prince of Wales Secondary School and UBC.
Taxes (2017): $9,465.95
- Air Conditioning
- ClthWsh
- Dryr
- Frdg
- Stve
- Garage Door Opener
- Microwave
- Security System
Similar Listings
Listed By: Interlink Realty
Disclaimer: Listing data is based in whole or in part on data generated by the Real Estate Board of Greater Vancouver and Fraser Valley Real Estate Board which assumes no responsibility for its accuracy.


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From FP, follow adoption through several continents and countless families and lives in this accompanying online photo essay. A review of books on EU-rope's constitutionalization. Doing democracy right: Why are other countries so much better at conducting elections than we are? A review of The Trial of Donald Rumsfeld: A Prosecution by Book by Michael Ratner. From IRB, a review of You are Here: Exposing the Vital Link Between What We Do and What That Does to Our Planet by Thomas M. Kostigen; and a review of The Fertility Doctor: John Rock and the Reproductive Revolution by Margaret Marsh and Wanda Ronner. From Adbusters, an essay on industrial childbirth: "Revisiting my son's birth has made me angry". Why do we tax corporations? Wouldn't it be easier just to tax individuals? A review of Solidarity Divided: The Crisis in Organized Labor and a New Path Toward Social Justice by Bill Fletcher and Fernando Gapasin. From Dissent, Harold Meyerson on Labor and Armageddon. From ResetDOC, an interview with John Judis on Barack Obama, a new Roosevelt. Jason Zengerle on how David Axelrod learned to conquer race. John Nichols on why "socialist" is not an epithet. Daniel Kahneman on two big things happening in psychology today. From TNR, a review of Giordano Bruno: Philosopher/Heretic by Ingrid D. Rowland.
From Forbes, a look at how Wall Street robbed you. Sexual Politics: Election 2008 hasn't just been dirty, it's been downright smutty. From Smithsonian, a series of articles on inspiring individuals making a difference in the fields of science, arts, culture and human behavior. From The Atlantic Monthly, a review of Have You Seen? by David Thomson; an article on the forgotten filmmaker who anticipated our modern media madness; and Virginia Postrel on on the politics of the retouched headshot. From Men's News Daily, how did we get from the founder's deep suspicion of majority rule to the deification of democracy? An interview with Paul Bloom on happiness, desire, memory, and the chaotic community that lives inside every human mind. A review of Understanding Privacy by Daniel J. Solove. A new generation of digital tracking technologies can now follow your every move, unleashing a world of personalised adverts; embracing these tools may be the only way to save the media from bankruptcy. Information technology is turning into a global "cloud" accessible from anywhere — what does that mean for the way people conduct business? An interview with Blake Gumprecht, author of The American College Town. Jim Holt on how philosophers have explained our sense of humour. The Mason's Apprentice: Our closest single-celled relatives reveal the origins of the stuff that holds us together.
From The Washington Monthly, Jeffrey Leonard on The Plug-in Revolution: A grand plan for America's energy woes; a review of Turkmeniscam: How Washington Lobbyists Fought to Flack for a Stalinist Dictatorship by Ken Silverstein; a review of War and Taxes by Steven A. Bank, Kirk J. Stark, and Joseph J. Thorndike; and a review of Warrior King: The Triumph and Betrayal of an American Commander in Iraq by Nathan Sassaman. Are al Qa'eda's leaders — fuelled by resentment of Hizbollah's appeal — moving to rebrand themselves a "resistance" group? Ed Husain seems to think that all Islamists eventually become terrorists, but why single them out? What about racists, left wing sympathisers, or even people who care about animals and the environment? An article on "voluntourism": See the world — and help conserve it. A review of The World is Curved: Hidden Dangers to the Global Economy by David M. Smick (and two excerpts). Paolo Virno's latest, Multitude, contends that the question of human nature — good or evil? — is suddenly topical, thanks to "immaterial labour"; but, if true, how useful is this insight? From TED, Alison Jackson on a surprising look at celebrity; Alisa Miller on why we know less than ever about the world; Amy Tan digs deep into the creative process; and Al Seckel says our brains are mis-wired — enjoy it!
From LPBR, a review of The Founding Fathers, Popular Culture and Constitutional Law: Who's Your Daddy? by Susan Burgess; and a review of The Founders' Second Amendment: Origins of the Right to Bear Arms by Stephen P. Halbrook. A review of Give Me Liberty: A Handbook for American Revolutionaries by Naomi Wolf. A review of Left Turn: Forging a New Political Future by Stanley Aronowitz. The Misunderstood Professor: When he suggested in a 1920 treatise that rockets could reach the moon, Robert Goddard sparked a public frenzy. Two excerpts from The Closing of the American Border: Terrorism, Immigration and Security Since 9/11 by Edward Alden. A review of Elisabeth Young-Bruehl's Why Arendt Matters. A review of I Was Wrong: The Meanings of Apologies by Nick Smith. Why do people have paranormal experiences? A team of researchers has been trying to find out. Tim Harford on why it's so hard to get away with blackmail. From Editor & Publisher, yes, newspaper endorsements matter — here is proof; and newspapers weigh alternatives to AP — but do they add up? "There's a seismic shift happening": An interview with Spike Lee on why history is on his side. The Statistical Universe: We look up to an expanse of sky that is billions of light-years in size, but the universe may be far larger than what we are able to see.


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Content tagged with: iport
Great Yorkshire Way - driving jobs and growthwww.doncaster.gov.uk/services/transport-streets-parking/finningley-and-rossington-regeneration-route-scheme-farrrs
Great Yorkshire Way (formerly known as The Finningley and Rossington Regeneration Route Scheme (FARRRS) project) - has provided a new link road from the M18 at junction three to Doncaster Sheffield Airport with links into Rossington and the iPort development.
Transport schemes and projectswww.doncaster.gov.uk/services/transport-streets-parking/transport-schemes-and-projects
During the past decade there has been significant investment in major transport schemes in Doncaster which have been developed by the council's transportation unit.
iPort is a £400 million inland port project and one of UK's largest logistics developments.


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Literacy by the Numbers
Literacy Services of Indian River County tutored 320 students last year, 20% of which were older adults. The demand has grown significantly. In order to sustain our literacy program and add more students to our program, we need your continued support.
Whether making a one-time gift, monthly recurring donations or a planned gift, your contribution will help fulfill the mission of Literacy Services of Indian River County and continue a legacy of learning.Click here to purchase event tickets or to make a donation
Planned Giving
Including Literacy Services of Indian River County, Inc. as a beneficiary in your retirement plans, will, living trust, life insurance or charitable annuities offers an opportunity for you to extend your legacy of literacy. Your attorney and accountant can assist you with arranging a planned gift. To schedule an appointment to discuss the opportunities, please contact LSIRC at 772.778.2223.
Why does adult literacy matter to Indian River County?
It increases financially stable families
It improves our local workforce and reduces infrastructure costs
It creates a healthy economic environment
And it helps ensure children learn to read at an early age, stopping another generation of illiteracy


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2006-07 Ford Fusion Mercury Milan Clutch Kit EXEDY FMK1004 - 1ATCK001941ATCK00194
This Exedy clutch set includes:
- Clutch Disk
- Outside Diameter Size - 225mm (8-7/8")
- Spline Diameter - 15/16"
- Number of Splines - 22
- Pressure Plate
- Throw-out Bearing
- Alignment Tool
- Installation Guide
If you are noticing a strong burning smell or slipping from your clutch it may be time to change it. This Exedy Clutch Set even includes a throw out bearing and the special alignment tool to ensure a hassle free installation.
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This item is backed by a 2 Year Warranty. In the event this item should fail during intended use, we will exchange the part free of charge (excludes shipping charges) for the original purchaser.
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This item is backed by a warranty against defects in materials and workmanship under its intended use. The warranty does not cover normal wear and tear. Please keep your invoice for proof of this warranty.
Vehicle Fit
- 2006-2007 Ford Fusion Clutch Kit L4 2.3L EXEDY FMK1004
- 2006-2007 Mercury Milan Clutch Kit L4 2.3L EXEDY FMK1004
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The new system for urinalysis
Diagnosticap system.
The Diagnosticap™ is supplied as a complete integrated system. The system comprises a Urine container & Lid and the Diagnosticap™. The cost of the complete Diagnosticap™ system is the equivalent of a conventional, singular, 8 parameter reagent strip.
The Diagnosticap™ can conduct the following chemical reagent tests:
Glucose, Ketone, Specific Gravity, Blood, pH, Protein, Nitrite and Leucocytes.
The patient provides a sample and using the screw-on Lid, seals it within the Urine container before presenting it to the clinician. The "push-fit" Diagnosticap™ is placed onto the Lid locking all components together. This action ruptures the watertight seal in the Lid and allows the urine to pass into the testing chamber and interact with the chemical reagent pads. The liquid sample remains isolated from the tester at all times.
The Diagnosticap™ incorporates conventional chemical reagent paper. The interaction between urine and chemical reagents inside the Diagnosticap™ is identical to that seen with traditional reagent strips.
The Diagnosticap™ is supplied in an airtight storage container, 100 per container. Included in each container is a manual reader, a plastic disc detailing all the result colours required for aligned visual analysis.
The process allows low volume urine samples be tested to a high degree of accuracy as the volume of urine is channeled directly onto the reagent pads.
Urine containers & Lids are supplied 100 per box.
Digital Diagnosticap™ Analyser.
The Diagnosticap™ system is inserted into the analyser directly after exposing the reagent pads to the urine sample. Once docked inside the analyser the internal lens automatically captures the results at specific, predetermined time intervals. Upon completion, the full image analysis data is passed to the PC via a USB cable. The USB cable also powers the desktop analyser.
The results data is presented on the PC screen via desktop software. The clinician will have the option to print out the results or upload them into the patient's digital record.
The Digital Diagnosticap™ Analyser is self-calibrating, highly accurate and very low maintenance. £95+VAT.
The Digital Diagnosticap™ Analyser is designed to receive the Diagnosticap™ only.
Laboratory requirements.
Samples that require laboratory analysis are sent directly to the lab without being decanted into a boric acid container. The Diagnosticap™ system already contains boric acid. The reagent pads within Diagnosticap™ are not affected by the presence of boric acid.
A Diagnosticap™ system that does not contain boric acid is also available for clinicians.
Upon receipt of the sample the laboratory unscrews the lid and Diagnosticap™. The urine container is then loaded directly into standard racking for automated handling.
The Diagnosticap™ system uses the same container from patient to laboratory; this creates less label printing and risk of sample mix-ups.
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UGC NET 2014 Notification, Exam dates, Online Application form and Eligibility Criteria
Council of Scientific & Industrial Research (CSIR) invites Online Applications from Indian Nationals to Join CSIR-UGC National Eligibility Test . UGC NET June 2014 Online Registration process & Notification will be available from 10th February, 2014 and end up on 04th March, 2014. www.iupsc.in provides the complete details of UGC NET 2014 such as Exam Date, Online Application form and Notification , kindly read this article completely.
About UGC NET 2014 :
CSIR has conducted Joint University Grants Commission National Eligibility Test (NET) twice in a year . CSIR NET is conducted to appoint the candidates on Junior Research Fellowship and to check the eligibility for Lectureship.
Eligibility for UGC NET 2014 :
Age Limit :
1. For JRF (NET) posts : Candidates age should not exceed 28 years as on 01/01/2014.
2. For LS(NET) : Not Mentioned.
Educational Qualification :
1. For JRF post : Candidates should have done BS-4 years program/BE/B. Tech/B. Pharma/MBBS/ Integrated BS-MS/M.Sc. or Equivalent degree/BSc (Hons) or equivalent degree or students enrolled in integrated MS-Ph.D program with at least 55% marks for General & OBC (50% for SC/ST candidates, Physically and Visually handicapped candidates) .
Note : Candidates having bachelor's degree, whether Science, engineering or any other discipline, will be eligible for fellowship only after getting registered/enrolled for Ph.D/integrated Ph.D. program within the validity period of two years.
2. For Lectureship (NET) : Candidates must possess Ph.D degree with qualified Master's Degree before 19 September 1991, with minimum 50% Marks.
Examination Fee :
1. General Candidates are required to pay Rs. 400/-.
2. Other Backward Classes (OBC) Candidates need to Pay Rs. 200/-.
3. SC/ST/Physically Handicapped/Visually Handicapped Candidates have to pay only Rs. 100/-.
How to Apply : Candidates seeking Admission to the Test (UGC-NET June 2014) must apply Online through a link www.ugcnetonline.in . After submission of online application, Candidates have to send hard copy of completely filled Online Application form along with Examination fee to the Address given below :
Sr. Controller of Examination,
Human Resource Development Group,
Examination Unit, CSIP Complex,
Library Avenue, Pusa, New- Delhi, Pin- 110012
Important Dates of UGC NET 2014 :
Date for commencement of Online registration : 10-02-2014
Last date for Online submission of application : 04-03-2014
Last date for receipt of hard copy of Online Application : 08-03-2014
Date of UGC NET 2014 Exam : 22-06-2014
UGC NET 2014 notification and Online form will be available on http://www.ugcnetonline.in/
****All the visitors are informed that they are free to write their query or problems in our comment box given below, we will try to give solution to your problem as soon as possible****


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Characterization of in vitro substrates of protein kinases by peptide library screening provides a wealth of information on the substrate specificity of kinases for amino acids at particular positions relative to the site of phosphorylation, but provides no information concerning interdependence among positions. High-throughput techniques have recently made it feasible to identify large numbers of in vivo kinase substrates. We used data from experiments on the kinases ATM/ATR and CDK1, and curated CK2 substrates to evaluate the prevalence of interactions between substrate positions within a motif and the utility of these interactions in predicting kinase substrates. Among these data, evidence of interpositional sequence dependencies is strikingly rare, and what dependency exists does little to aid in the prediction of novel kinase substrates. Significant increases in the ability of models to predict kinase–substrate specificity beyond position-independent models must come largely from inclusion of elements of biological and cellular context, rather than further analysis of substrate sequences alone. Our results suggest that, evolutionarily, kinase substrate fitness exists in a smooth energetic landscape. Taken with results from others indicating that phosphopeptide-binding domains do exhibit interpositional dependence, our data suggest that incorporation of new substrate molecules into phospho-signalling networks may be rate-limited by the evolution of suitability for binding by phosphopeptide-binding domains.
1. Introduction
Substrate recognition by kinases is mediated both by recognition of the substrate sequence surrounding the phosphorylation site and by other contextual elements including co-localization and distal-site interaction. The specificity of protein kinases for their substrate sites has traditionally been described at one of three levels of complexity. The first level is that of the match to a phosphorylation motif [1], a description in terms of which amino acids are frequently present at which positions relative to the site of phosphorylation (e.g. 'S/T-P-X-R/K', for the cell-cycle-dependent kinase Cdk1 [2]). These descriptions are practical and readable, but are generally neither sufficient nor necessary descriptions of a kinase's substrates [2]. At a more complex level, the in vitro specificity of a kinase can be described using a position-specific scoring matrix (PSSM), wherein the probability of each amino acid at each position relative to the site of phosphorylation is given. Any higher-order information on what amino acids are more or less likely to co-occur in the positions surrounding the site of the phosphorylation is lost [3]. As a result, the suitability of non-ideal kinase substrates can be captured, instead of only substrates that match the most likely amino acid at each position. Both of these descriptions represent simple models of the specificity of a kinase for its substrates, using only sequence information local to the potential site of phosphorylation. The motif description is a simple Boolean descriptor: to an extreme approximation, the kinase will phosphorylate sites that fit the motif, and will not phosphorylate those that do not. The PSSM description is more nuanced: given a sequence, a score can be calculated that should approximately reflect the suitability of the substrate sequence for the kinase. At the final, most complex level, several models of kinase–substrate specificity more complex than the PSSM have been proposed. These include neural networks (NetPhosK [4] and NetPhorest [5]), hidden Markov models (KinasePhos) [6], support vector machines (PredPhospho [7]) and Bayesian decision theory (PPSP [8]). These more detailed models are based on the assumption that better predictions of kinase substrates can be obtained if machine-learning algorithms are allowed to use information of higher-order in developing classifiers. One potential failing of these methods is the fact that they use large databases of substrate–kinase pairs identified by different experimental methods under different conditions, such as Phospho.ELM [9] and UniProtKB/Swiss-Prot [10]. While this provides a large training set, it also poses the risk of convolving kinase specificity with additional biases present owing to different portions of the source data being collected by different methods.
It is important to determine whether higher-order models of amino acid sequence specificity than that provided by a PSSM can improve description of the in vivo activity of a kinase or, more especially, improve prediction of kinase–substrate interactions, rather than overfit data or fit co-dependencies created by study biases instead of the kinase's own biophysical selectivity. If a kinase does not recognize each amino acid position on its substrate in an energetically independent manner, then models for describing and predicting kinase substrates should take this into account. If, on the other hand, the assumptions of energetic independence that lead to models such as the PSSM hold true, then future improvements in our ability to predict novel kinase substrates will depend instead on identifying and quantifying the contribution of other factors important to the kinase–substrate interaction, such as recognition via distal interaction sites, protein localization and dynamics and the presence or absence of other facilitating or inhibitory post-translational modifications [11].
Of note, the majority of protein kinases do not have a known motif specificity; a recent atlas of computationally predicted consensus specificities covers only 35 per cent of the human kinome [5]. Conversely, only 12 per cent of the curated phosphorylation sites in Phospho.ELM are currently attributable to a particular kinase [9]. For most kinases, a large set of known substrates gathered by a single method does not exist. Nonetheless, there are a small number of single experiments described in the literature that identify a large number of kinase substrates. From these datasets, it may be possible to gain an understanding of the role of cooperativity among substrate amino acid positions in determining kinase specificity. We therefore set out to assess directly the degree to which statistically significant positional interdependencies among kinase substrate sequences can be identified. For this work, three recently available datasets including substrates of three highly pleiotropic kinases were selected. Matsuoka et al. [12] identified 905 putative substrate sites for the DNA-damage-dependent kinases ATM (ataxia telangiectasia mutated) and ATR (ataxia telangiectasia and Rad3 related) (and possibly other ionizing radiation-induced kinases such as DNA-PK) using quantitative mass spectroscopy. Blethrow et al. [13] identified 71 direct proline-directed human substrate sites for Cdk1/Cyclin B, using a kinase modified to accept a chemically labelled adenosine triphosphate (ATP) analogue, followed by covalent capture and identification of labelled sites via mass spectrometry. While there are not as many substrate sites available in this dataset as in the ATM/ATR dataset, these data are extremely appealing, in that the data are direct observations of the substrates of a single kinase in a single experiment; there are few potential sources of external bias. Finally, Salvi et al. [14] have curated a set of 492 putative substrate sites, from a number of species, of casein kinase2 (CK2). These sites were not identified in a single experiment; just over 300 were identified from the literature by Meggio & Pinna [15], while the remainder were extracted from the large-scale databases PhosphoSite [16] and Phospho.ELM [9]. While some of the problems of heterogeneous data may be present in this dataset, it is possible that curation by experts in the particular kinase, CK2, may mitigate these problems.
2. Results
(a) Statistical significance of interpositional dependencies among kinase substrates
We first interrogated the degree to which second-order substrate preferences can be identified in datasets associated with substrates of the DNA-damage-dependent kinases ATM and ATR [12]. At substrate positions relative to the fixed site of phosphorylation, we counted the number of occurrences of each amino acid. At each pair of positions, we counted the number of co-occurrences of each pair of amino acids. In order to determine the significance of enrichment (or reduction) of co-occurrence of a pair of amino acids, we then compared the actual degree of co-occurrence with the distribution of co-occurrences that might be expected by chance given the individual levels of occurrence for each amino acid (see §4c,d). We expected to find a large number of significant deviations, driven by kinase structural biophysics or by evolutionary selection for some downstream functional constraint. Contrary to this expectation, although we observed small deviations in the frequencies of individual amino acid pairs from what might be most expected by chance, these were rarely statistically significant when subjected to rigorous analysis (table 1). That is, almost all of these deviations correspond to what would be expected under a model of position-wise independence by random chance.
Despite a large dataset of 861 substrate sites of ATM and ATR, only a handful of statistically significant deviations from what would be expected by chance under a position-independent model can be identified (table 1). Each of these involves the phosphorylated position (i.e. whether a serine or threonine is phosphorylated). Phosphoserine at the fixed position occurs more frequently than can be explained by chance with proline or glycine at the −1 position, with glycine at the +2 position and with serine at the +3 position. Conversely, phosphothreonine co-occurs less often than can be explained by chance with these amino acids. This result is likely caused by the statistical boosting power of the oriented phosphorylated position; while a pair of arbitrary positions may populate a space of 20 × 20 amino acid pairs, pairs of positions including the phosphorylated serine or threonine exist in a space of only 40 amino acid pairs, enabling the effective identification of lower degrees of energetic cooperativity.
The same methodology was applied to substrates of Cdk1/Cyclin B [13] and CK2 [14]. Strikingly, the set of 71 proline-directed substrates examined of Cdk1/Cyclin B has no pairs of individual amino acids that deviate from a frequency that might be expected by chance at any pair of positions, and among the 432 curated substrates of CK2, only a single amino acid pair at a single pair of positions deviates significantly from what might be expected by chance (table 1). We reasoned that, as in the case of ATM and ATR, we might be able to boost the power of our significance testing procedure by engineering a situation where fewer than the normal 400 pairs of amino acids were accessible. To facilitate this, we combined the 20 amino acids into six functional categories: acidic, basic, hydrophobic, polar, aromatic and a final 'structural' group for the amino acids proline and glycine. Even after the space of possible amino acid pairs is reduced approximately 11-fold in this manner, from 20 × 20 to 6 × 6, only a surprisingly small number of statistically significant deviations be found: a single instance for Cdk1/Cyclin B, and four more for CK2.
Despite the use of some of the cleanest and broadest data available on the in vivo substrates of protein kinases, there is only in rare instances statistically compelling evidence for interpositional dependencies.
(b) Utility of interpositional dependencies in predicting novel kinase substrates
Although the number of statistically significant deviations from a position-independent description of substrate specificity for these kinases is strikingly small, this lack of significant findings is not, of itself, evidence that the kinase recognize their substrates in a position-independent manner. The smaller the cooperative (or anti-cooperative) energetic effect of a pair of amino acids on kinase binding or catalysis, the larger the sample size of substrate sequences that would be required to reliably detect it. The fact that we find only a small number of interdependent sequence elements indicates either that these kinases largely recognize their substrates in a position-independent manner, or that the predominant level of cooperativity is too small to be detected given the available numbers of substrate sequences.
We chose, therefore, to take a step back and examine the issue of substrate sequence interdependencies at a more pragmatic level. The most common motive in trying to determine a substrate specificity descriptor for a kinase is to predict new substrates and new phosphorylation sites. We reasoned that, though very few amino acid pairs at pairs of positions among kinase substrates exhibit statistically significant interdependence, there might be sub-significant interdependencies contributing in aggregate to kinase substrate specificity. To assess directly whether the inclusion of second-order information improved models of kinase substrate specificity, first- and second-order probabilistic models of the specificities of ATM/ATR, CDK1/Cyclin B and CK2 were built and compared (see §4f,g).
For each kinase, 1000 first- and second-order models were trained on a randomly selected training set of 90 per cent of the substrates, and then tested for their ability to identify the withheld true substrate test set from among a background of shuffled negative control substrates (figures 1a and 2a). These shuffled controls are generated by shuffling amino acids among substrates, while maintaining their positions relative to the site of phosphorylation. This procedure preserves the position-wise amino acid frequencies of the substrates, but randomizes pairwise interdependencies. Neither a first-order nor a second-order model does a particularly good job of identifying true substrates from among these shuffled negative controls. The first-order models score potential substrates of the modelled kinase having a given sequence as a function of the probabilities of individual amino acids appearing in individual positions among the training data, neglecting all higher-order effects. The second-order models score substrates accounting for both the individual probabilities at single positions and the probabilities of pairs of amino acids at pairs of positions, neglecting the contribution of triplet and higher-order combinations (see §4f). These models are used to score a set of 870 potential ATM/ATR substrates (87 true substrates, 783 shuffled negative control substrates). The top 10 per cent (87/870) of scores are taken as predicted substrates from the models. First-order models captured a median value of 10.3 per cent (9/87) true positives among putative hits, whereas the second-order models capture a median value of 12.6 per cent (11/87) true positives (figure 1a). Similar results are seen for CK2 (first-order, 13.6% (6/44); second-order, 18.2% (8/44)). Random selection of sequences, as an important point of comparison, would produce 10 per cent true positives.
When the same procedure was applied to CDK1/Cyclin B, we observed that less than 10 per cent of the test data were scored with a non-zero probability of being a kinase substrate according to the second-order model, resulting in supplementation of predicted substrate sites with a random selection of positive and mock test substrates to make up a total of 10 per cent of the test data selected (see figure 1a for results, electronic supplementary material, figure S1 for receiver operating characteristic (ROC) curves). To combat this, we also examined the fraction of true positives, restricting the number of predictions analysed for each of 1000 random partitions of training and test data to the least of three quantities: 10 per cent of the test data, or the number of non-zero probability predictions in the first- or second-order model (figure 2a). Over 1000 such partitions, a mean of 1.32 sequences per test dataset are assigned a non-zero score. For both the first- and second-order models, the median fraction of these that are true positives is 0 per cent. In each case, then, the second-order model fails to perform compellingly better than the first-order model, and in fact, all models are similar in quality to random selection of peptides from among the test and mock data. The small improvement of both the first- and second-order models over random selection implies that the shuffled negative control substrates are, at the level of sequence, similar in quality to the true substrates.
Identifying true substrates from among mock substrates with an identical position-specific amino acid distribution is, clearly, a difficult task. We reasoned that a less stringent, and more realistic and pragmatic test would be the identification of true substrates from among a background of potential proteomic substrates (figures 1b and 2b). Such a background can be generated by randomly selecting from the proteome peptides that conform to the most conserved elements of the substrate specificity of the kinase. For ATM/ATR, the motif 'S/T-Q' was used to select mock substrates. For CDK1/Cyclin B, the motif 'S/T-P' was used. In both cases, the selected motif is almost invariably a feature of true substrates. In the case of CK2, the motif 'S/T-X-X-D/E' is common, occurring in about 75 per cent of the substrates in the dataset used. Proteomic peptides conforming to this motif were randomly selected and used to test CK2 substrate specificity models created using either the full dataset, or just the subset that itself conforms to the motif. Again, 90 per cent of the substrate data were used to train models, and then the other 10 per cent of true substrates and a nine-to-one excess of proteomically derived mock substrates were scored, and the top 10 per cent of high-scoring peptides were taken as positively scored (figure 1b). The process was repeated 1000 times, and the median number of true positives was noted. Because less than 10 per cent of peptides tested for CDK1/cyclin B and CK2 had non-zero probability scores, the procedure was repeated, limiting the number of examined top-scoring substrates to 10 per cent, or the fewer of non-zero-scoring peptides in the first- or second-order model (figure 2b).
In this context of proteomically derived mock substrates, all models had a much better predictive capacity than that observed when attempting to identify true kinase substrates from among negative control substrates generated by position-wise shuffling of the true substrate sequences. When first-order models of ATM/ATR specificity were applied to a field of 10 per cent true substrates and 90 per cent proteomically derived mock substrates, a median of 36.8 per cent (32/87) of the top 10 per cent of high-scoring sequences were true positives, versus 31.0 per cent (27/87) for second-order models (figure 1b). Drastically, for CDK1/Cyclin B, 50.0 per cent (4/8) of hits were true positives for first-order models, whereas second-order models captured only 12.5 per cent (1/8) true positives. Models of CK2 substrate specificity were similarly effective at separating true substrates from 'S/T-X-X-D/E' sequences in the proteome, whether trained and tested using the entire CK2 dataset (first-order, 45.5% (20/44); second-order, 34.1% (15/44)) or only the portion itself conforming to the 'S/T-X-X-D/E' motif (first-order, 54.6% (18/33); second-order, 33.3% (11/33)). As was true for CDK1/Cyclin B when tested using position-wise-shuffled negative controls, less than 10 per cent of peptides tested for CDK1/Cyclin B and CK2 had non-zero probability scores. The procedure was therefore repeated limiting the number of examined top-scoring substrates to 10 per cent, or the fewer of non-zero-scoring peptides in the first- or second-order model (figure 2b). Very few test substrates for CDK1/Cyclin B, whether true substrates or proteomic mock substrates, receive non-zero scores—none for 883 of 1000 trials, and an average of 1.04 among the remaining 117 trials. While the median fraction of these peptides that are true positives is 100 per cent in the first-order case and 0 per cent in the second-order case among the 117 trials, this is largely an artefact of the fact that most of these 117 trials have only one sequence with non-zero score, making the test largely binary in nature. The means of the same distributions are 71.4 per cent and 41.5 per cent for the first- and second-order models, respectively.
While all models do better than random selection at separating true from proteomically derived mock substrates, in each case, the second-order model is a less accurate predictor than the first-order model, indicating that the pairwise amino acid frequencies among pairs of positions in the training data are not representative of the pairwise amino acid frequencies among the test data. The second-order models are thus systematically overfit to the training data.
3. Discussion
Although the occurrence of significant cooperativity (or anti-cooperativity) is rare among the ATM/ATR, CDK1/Cyclin B and CK2 substrates examined here, a relatively small number of pairs of amino acids that act cooperatively in the bulk context were identified. Most of these do not lend themselves to facile biophysical explanation, with the possible exception of the statistically significant preference for serine over threonine as the phosphorylatable residue in the context of ATM/ATR substrates with proline or glycine in the −1 position, glycine in the +2 position or serine in the +3 position. The difference between a serine and a threonine side chain is quite modest: the threonine has an additional methyl group attached to the beta carbon. The disfavouring of threonine at the phosphorylated position in concert with specific residues at other positions among ATM and ATR substrates is likely caused by one of two biophysical effects: either a steric clash between the threonine methyl group and the residue disfavoured in tandem, or the threonine methyl disfavouring a substrate backbone configuration amenable to kinase–substrate interaction in the context of the other residue.
While crystal structures of the kinases studied here in complex with substrates do not exist, there is a crystal structure solved of the kinase Cdk2/Cyclin A in complex with an optimized substrate peptide [18]. Cdk2 shares 66 per cent sequence identity with Cdk1, and has similar substrate specificity as well. In this structure, there are no close contacts between the amino acid side chains of the substrate peptide, perhaps partially explaining the lack of interdependence seen among Cdk1/Cyclin B substrates.
None of the datasets used in this work is perfectly suited to the task of describing the bulk substrate specificity of a kinase. Although ATM and ATR have a large number of substrates determined in the course of a single study, the two are individual kinases treated, perhaps incorrectly [19], as having identical specificity. Moreover, substrates of the kinases were identified using a cocktail of antibodies [12], and the specificities of these antibodies must be convoluted with those of ATM and ATR to generate the final list of putative substrates. Nonetheless, if ATM preferred different amino acids at individual positions than ATR, then pairs of residues independently preferred at pairs of positions by each of the two kinases would have appeared as being enriched relative to what would be expected under a position-independent model. The curation of CK2 substrates [14], no matter how expertly performed, is subject to the study biases of those who originally reported CK2 substrates in the literature. As with ATM/ATR, however, these biases would be expected to introduce, and not negate, apparent interpositional dependencies. CDK1/Cyclin B substrates were identified by in vitro phosphorylation of lysates with an engineered kinase [13], but the number of substrates identified was small with respect to what might be needed to adequately describe the frequency of pairs of amino acids at pairs of positions. Strikingly, the three data sources examined span a wide range of sizes and cover several collection methodologies. Across all three cases, the same consistent pattern of rare interpositional interaction is found.
The methodology applied here is fundamentally similar to both the statistical coupling analysis developed in the research group of Ranganathan [20] and to the mutual information method of Gfeller et al. [21]. While each of these methods is aimed at identifying interpositional correlations, we chose our method to directly examine statistical significance of enrichment or diminishment of co-occurrence of pairs of amino acids, rather than using information or entropy as an intermediate metric of statistical significance. Our interest is primarily in identifying co-occurrence rates that are poorly explained by chance, and our methods are meant to approach this goal as directly as possible.
The surprising scarcity of amino acid pairs occurring significantly more or less frequently among a kinase's substrates than would be expected if each amino acid were independently recognized by the kinase might have one of, or a combination of, several explanations. First, it may simply be true that kinases largely recognize each amino acid of their substrates independently, although this seems biophysically implausible. Second, it is possible that kinases incubated in vitro with an infinitely varied library of potential substrates would express statistically significant preferences. In vivo, however, a kinase is exposed to a subset of the possible amino acid sequence space: it is limited in access to peptide sequences encoded by the genome, in the same subcellular localization and structurally accessible. This convolution may lead to the obfuscation of a kinase's pure biophysical preferences. Finally, there is probably a contribution of effect size. It seems unlikely that each substrate sub-site is recognized independently in kinases, and rather more likely that the energetic contribution of second-order effects exists but is very modest. The smaller the size of such effect, the larger the sample of substrates necessary to detect it will be.
A low degree of interpositional dependence in kinase substrate specificity has interesting implications for the evolution of phosphorylation sites and of phosphorylation signalling networks. If each substrate sequence position contributes independently to the ability of a kinase to phosphorylate its substrates, then the evolutionary fitness landscape of substrates as a function of the amino acid at each position is smooth, with a single minimum. That is, there are no non-global local minima acting as traps in kinase substrate fitness space—for any non-ideal substrate, there exist one or more single mutations that would improve the fitness of the substrate for the kinase, with no concerted double or higher-multiple mutations necessary.
Work by other research groups demonstrates that this property of position-wise independence is not uniformly common to all components of phosphosignalling pathways. Yaffe et al. [22], in studying the phosphopeptide-binding protein 14-3-3, found that substrates adhered to one of two mutually exclusive sequence modes. Liu et al. [23] have demonstrated that SH2 domains, which recognize and bind to phosphotyrosine-containing peptides, will vary in their specificity at some substrate positions as a function of what amino acids are present at other positions. For example, the SH2 domain of Crk binds to peptides with a phosphotyrosine along with a leucine or a proline in the +3 position. Proline at the +2 position, however, is allowed only when the identity of the +3 position is leucine and not proline. Other work by Gfeller et al. [21] has shown a similar property among the SH3, PDZ and WW peptide-binding domains. Although these domains do not bind phosphopeptides in general, a subset of the WW domains (not explicitly studied by Gfeller et al.) does bind specifically to phosphoserine- and phosphothreonine-containing peptides with a proline in the +1 position.
This fundamental difference in the way that kinases and phosphopeptide-binding domains recognize their substrates—kinases in a position-independent manner, but phosphopeptide-binding domains exhibiting clear second- or higher-order preferences—may indicate that the evolution of kinase substrates is a fast or easy step in the evolution of phosphosignalling networks. Single mutations can always improve a non-optimal kinase substrate, whereas the substrates of phosphopeptide-binding domains, which operate in signalling networks to read the phosphorylation events left by kinases, may sometimes require concerted mutations in potential substrates in order to become more fit for binding (figure 3). Evidence for the existence of significant numbers of functionless phosphorylations [24] is consistent with this possibility; a build-up of non-functional phosphorylations is consistent with kinase–substrate evolution being an easy step in signalling network evolution.
It is clear from the results presented here that the specificity of these kinases for the amino acid sequences proximal to the site of phosphorylation among their in vivo substrates is largely well-described by a first-order model. Adding second-order information to first-order models of kinase specificity, at least for these kinases, seems to add only a minimal benefit in terms of predicting novel substrates. In some cases, adding second-order information even reduces the quality of a first-order model, indicating that the second-order models are overfit to irrelevant interpositional correlations in the training data. In order to predict novel kinase substrates, it may instead be beneficial to integrate simple sequence models with other contextual information such as known interactions [11], subcellular localization, protein structure and distal-site recognition.
In the present work, we elected to restrict our models to using only local sequence information directly, in order to isolate the effect of second-order information on improving first-order models. Sequence information also informs substrate fitness in indirect ways not examined here. Intrinsic protein disorder seems to be enriched in proximity to sites of protein phosphorylation, and consideration of protein disorder improves ab initio prediction of the location of sites of phosphorylation [25]. Likewise, the evolution and conservation of protein sequence surrounding a site of phosphorylation might give clues to which neighbouring residues are responsible for recognition, and what the relevant constraints on flanking sequence are, though aligning sequences in disordered regions of proteins is quite difficult.
It is tempting to speculate that the approximately first-order nature of substrate recognition by these kinases reflects evolutionary freedom for the development of new kinase substrates: the energy landscape for substrate fitness is smooth, with multiple-step mutations generally unnecessary to improve the fitness of any potential kinase substrate. It remains to be seen, however, whether the results reported here extend to other kinases, or to the complete repertoire of substrates for the kinases analysed here.
4. Material and methods
(a) Data sources
We attempted to find long lists of substrates for a variety of kinases, identified in as unbiased a manner as possible. We chose two datasets that identified a long list of substrates via a single experiment: one for ATM/ATR [12] that identified 894 individual human phosphosites with the canonical 'pS/pT-Q' motif of ATM and ATR, and one for Cdk1/Cyclin B [13] that identified 77 human sites, 71 of which contained the canonical proline-directed 'pS/pT-P' motif. Additionally, we identified a third dataset collected by expert curation that enumerates 432 specific sites of CK2 phosphorylation from a variety of species [14].
(b) Data preparation
For the ATM/ATR and CDK1/Cyclin B data sources, full protein sequences were retrieved using protein identifier and sequence information from the source publication. In some cases, the source data contained duplications of the same site, or were not sufficient to unambiguously identify the protein and site referenced. The remaining sequences were used to find peptide sequences including the site of phosphorylation, as well as the seven residues upstream and downstream of the phosphorylation. This preparation yielded 861 putative human ATM/ATR sites and 71 putative human Cdk1/Cyclin B sites. Protein identifiers and sequences are provided as electronic supplementary material, tables S1 and S2. The CK2 data were originally published including the sequences of phosphorylation sites, including six residues to the N- and C-terminal sides of the site of phosphorylation itself, and the data were used directly.
(c) Identification of overrepresented and underrepresented amino acid pairs
For each kinase, we attempted to identify those pairs of amino acids, at pairs of positions relative to the phosphorylated residue that co-occurred among substrates with a frequency not adequately explained by their individual prevalences and chance. The positions considered were selected by inspection of a motif logo [26] built from substrate sequences as a sequential set of positions that contain more information than the background (see electronic supplementary material, figure S2). For ATM/ATR substrates, positions from −2 to +3 relative to the site of phosphorylation were considered. For CDK1/Cyclin B, positions −2 to +4 were examined. For CK2, positions −1 to +5 relative to the phosphorylation site were considered. For every pair of amino acids at each pair of positions, the statistical significance of deviation from what would be expected by chance, if the positions were recognized independently by the phosphorylating kinase, was calculated using a hypergeometric distribution. If a kinase has N total substrates, with m having amino acid a at position x, n having amino acid b at position y and k having both, then the expression gives the statistical significance of enrichment of amino acid a at position x and amino acid b at position y co-occurring. This is exactly equal to the probability of finding k or more sequences with both amino acids at the two positions by chance, assuming the two are not recognized cooperatively. Conversely, the expression gives the significance of reduction, or the probability of finding k or fewer instances of both amino acids at the two positions by chance if they are recognized independently.
(d) Statistical significance cut-off determination
Two methods were used to set a cutoff for statistical significance values for the interactions between amino acid pairs that corresponds to a 5 per cent false-positive rate. The first was entirely empirical: 1000 times for each dataset, we randomly shuffled the data at each amino acid position across all sequences, such that the probability of each amino acid at each position is preserved, but any pairwise interactions were scrambled. For each shuffling, the significances of enrichment and reduction of all pairs of amino acids at all pairs of positions were calculated as for the true data. The single most significant result for each of these thousand negative controls was identified. In the true data, any result more significant than can be found in 95 per cent of shuffled controls was taken as significant and presented—that is, we accepted as a positive result any p-value that did not appear in randomized data more than 5 per cent of the time.
The more rigorous false discovery rate control method described by Benjamini & Hochberg [17] was also used, independently on one vector each of statistical significances of enrichment and reduction for each pair of substrate positions for each kinase examined. A q* value of 0.05 was used, and the set of hypotheses tested were only those that could not be trivially accepted: for enrichment, only those pairs of amino acids that occur at least once apiece independently, and for reduction only those pairs of amino acids that co-occur once or more.
Although the false discovery rate control procedure is only well-suited to series of significance tests that are statistically independent, and the interdependence of statistical significance values calculated by studying the frequency of pairs of amino acids at each pair of positions is difficult to accurately characterize, results were in strong agreement with those generated using the empirical procedure.
(e) Simplified amino acid alphabet
Because the numbers of substrates identified for each kinase of interest is small compared with the number of possible pairs of amino acids at each position, all calculations were repeated using a simplified amino acid alphabet comprised of six classes: the acids (D,E), the bases (K,R), the hydrophobes (A,I,L,M,V), the aromatics (F,W,Y), the polar side chains (C,H,N,Q,S,T) and the structural amino acids (G,P). Significant results generated using this simplified alphabet are reported only when no pair of individual amino acids from the pair of classes is itself capable of recapitulating the significant result.
(f) First- and second-order models of kinase substrate specificity
Probabilistic models of kinase substrate specificity were generated that approximate the many-order probability distribution across all amino acid positions using only single positions, or using single positions and pairs of positions, according to the generalized Kirkwood superposition approximation as described by Killian et al. [27]. The expression: gives p(1), a first-order approximation of the probability of a given sequence of amino acids x1 to xm at positions 1 to m as the product of the probability of each independently. This approximation neglects any cooperative effect of pairwise or higher-order combinations of amino acids. The expression gives p(2), a second-order approximation of the same probability that accounts for individual and pairwise influences, but neglects any higher-order effects. The probabilities multiplied in the numerator are all of the probabilities of pairs of amino acids at all pairs of positions, whereas the probabilities in the denominator are those for individual amino acids at single positions as in the first-order approximation.
(g) Evaluation of kinase substrate specificity models
Models were trained for each kinase by randomly separating the data to 90 per cent for training to populate probabilistic models as described earlier, and 10 per cent for testing. The testing portion of the data was combined with nine times as many mock substrate sequences, generated in one of two ways. First, mock sequences were generated by shuffling amino acids among the test substrate sequences within each amino acid position, preserving exactly the probabilities of amino acids at each position while randomizing pairwise interactions. Second, mock substrate sequences were generated by selecting appropriate sequences randomly from the human proteome (International Protein Index [28], v3.55). These sequences were selected from among all sites containing the amino acid sequence 'S/T-Q' for ATM/ATR, the sequence 'S/T-P' for CDK1/Cyclin B and the sequence 'S/T-X-X-D/E' for CK2. Because an acid at the +3 position relative to the site of phosphorylation is not an absolute requirement for CK2, additional models were trained and tested against proteomic mock substrates for CK2 using only the subset of 323 substrates conforming to the 'S/T-X-X-D/E' motif. The ability of each probabilistic model to identify true substrates among a background of mock substrates was measured by counting the number of true substrates among the best 10 per cent of potential substrates scored. This procedure was repeated using 1000 random divisions of the substrate data into test and training sets, and the mean and standard deviation are reported. In some cases, the best 10 per cent of potential substrates under a second-order model included some substrates with a probability score of 0. In these cases, the potential substrates with a score of 0 included in the best 10 per cent were selected randomly from all potential substrates with a score of 0.
Because peptides with a 0 per cent probability score would probably not be taken as hits by a researcher using these models to predict substrates, we repeated the procedure taking as a maximum the best 10 per cent of potential substrates, but limiting ourselves to those with a probability score of more than 0. For each of the 1000 random divisions of test and training data, the same number of high-ranking sequences was examined for both the first- and second-order model: the least of 10 per cent of the sequences, the number given a non-zero score by the first-order model, or the number given a non-zero score by the second-order model. If no sequences passed these criteria for one of the 1000 divisions, then this division was not included in distributions to calculate median statistics. This procedure led us to look at 87 of 870 sequences in all 1000 test sets for ATM/ATR, a mean of 2.01 of 80 sequences in 654 of 1000 test sets for CDK1/Cyclin B, and 44 of 440 sequences in all 1000 CK2 test sets, when comparing with position-wise-shuffled substrate sequences. When comparing with proteomic mock substrate sequences, we used 87 of 870 sequences in all 1000 ATM/ATR test sets, a mean of 1.04 of 80 sequences in 117 of 1000 CDK1/Cyclin B test sets and a mean of 25.2 or 15.4 in all 1000 test sets for CK2, when the training and test data did or did not include sequences not matching the 'S/T-X-X-D/E' motif, respectively.
The authors thank members of their research groups, and particularly Dr David Clarke for helpful discussion. This work was supported by NIH grants no. CA112967 (M.B.Y. and D.A.L.), ES015339 (M.B.Y.) and R24-DK090963 (D.A.L.), and by a Singapore-MIT Alliance Fellowship to C.L.
One contribution of 13 to a Theme Issue 'The evolution of protein phosphorylation'.
- This journal is © 2012 The Royal Society


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The challenge
The partnership began in 2011, using the Christian O'Connell Breakfast Show as a platform for Wickes to reach their trade customers every morning. The objective for Wickes was to deepen trade loyalty and provide the serious 'DIYer' with the tools they need to do a professional job.
Our Approach
From this we knew it was crucial to create content that would focus on celebrating the trade, whilst providing light hearted entertainment appealing to all listeners.
The Idea
Christian O'Connell Breakfast Show – now in it's 3rd year sponsored by Wickes.
As Christian O'Connell bursts on-air each morning with features and cleverly constructed stunts, the Wickes promotional ideas and mechanics focused on talking to the trade, whilst ensuring that the humour at the core of each idea appealed to the masses:
- To celebrate Wickes' 40th birthday Christian gave away 40 prizes in one show. The mechanic was simple and we called it, 'Tool Do You Do?' Listeners simply impersonated power tools to win some, making for a laugh-out loud feature and an innovative way to celebrate their birthday.
- To celebrate a Wickes deal on self assemble benches, we created 'The Wickes Shelf Help Group'. We asked listeners to share their DIY nightmares through submitting a photo of their small DIY issues! A rogues gallery of mini DIY disasters was then displayed and every Friday we called two of the best on air to battle it out to win a Wickes voucher. There was a fully integrated online tab to enter and we created a #shelfhelp, allowing listeners to tweet their entries to @absoluteradio using this hashtag. The breakfast team also managed to integrate the bench into the overall feature through Richie and Adrian (a Wickes employee), demonstrating just how 'easy' it is to build a bench live on air.
- To celebrate the start of the World Cup, Wickes and Absolute Radio held the first ever Wickes Cup in the Charlton Wickes store car-park. The tournament was filmed/edited and broadcast socially on the very same day! Christian and Richie were onsite broadcasting their entire show live - from the very first game to the lifting of the trophy!
The sponsorship has truly developed into a two way partnership, with Wickes featuring Christian and Richie in their trade catalogue and promoting a 'tune in' message through their other national advertising.


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An often overlooked element of marketing is your e-mail address.
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ORADELL, N.J. — Hundreds of guests enjoyed a grand opening reception Wednesday at the new Oradell home of the Fertility Institute of New Jersey and New York .
The co-medical directors — Dr. Inna Berin of Hillsdale and Dr. Zalman Levine of Teaneck — gave guided tours.
Sparkling chandeliers lit the way through 9,100 square feet of state-of-the-art labs, operating and recovery rooms, and clinical areas.
The practice moved from its Westwood location, where it started in 1995.
"We have grown quite a lot. We have 22 staffers," Berin said. "This space was much bigger and we got to design it from scratch."
The metrics of the medical practice tell the tale.
The most key one, Berin said, is the pregnancy rate: 65 percent for patients under age 35, which is one of the highest rates nationwide.
"If they end up doing pre-implantation genetic screening (PGS), that rate can go up to 80 or 85 percent," she said, "and that's irrespective of their age if they have normal embryos."
There are more statistics:
Every month, 20 pregnant patients, after their first trimester, are released, goodie bag in hand, to the care of their obstetricians/gynecologists.
"The chance of miscarriage after that point is less than 5 percent," Berin said.
The practice offers an array of services, starting with fertility checks for patients thinking of getting fertility treatments.
It also freezes and stores eggs for those not yet ready to conceive, Berin said. There are 2,000 frozen embryos onsite.
For those trying to conceive, she added, there's oral medication, intrauterine insemination (IUI), and in vitro fertilization (IVF).
Levine, who is both a medical doctor and a rabbi, said PGS is one of the most major advances in the fertility world over the last few years.
"When a couple needs IVF, we can use PGS, a technology that allows us to take biopsies of each embryo and to actually test the embryo to see whether the chromosomes in it are normal," he explained.
In that way, embryos can be screened out if they are not compatible with life or if they're so abnormal that they wouldn't take.
"By placing an embryo inside a woman's uterus that we know has a good chromosomal makeup," Levine said, "we can significantly increase the chances of that woman becoming pregnant, carrying the pregnancy to term, and having a healthy baby."
Through everything, Berin said, the practice strives to be warm and personal.
"We cry together," she said. "We laugh together."
The guest list for the reception included local obstetricians/gynecologists and other healthcare providers as well as Oradell first responders and the New Milford Ambulance Corps.
The institute, located at 680 Kinderkamack Road in the borough, serves patients in New Jersey and in Rockland, Orange, and Sullivan counties in New York.
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In 1991, Jan Thompson attended a reunion of World War II veterans who were prisoners of war in the Philippines. She accompanied her father, one of those veterans.
"I was just dumbfounded at what I heard," she said. "I walked out saying, 'Why doesn't anyone know about this?'"
She spent the next 22 years working on a project so people would know.


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Eliza Doolittle's track "Big When I Was Little" would have you believe that the diminutive singer skips her way through the streets of planet positive. It's almost gratingly peppy and bright. But today, Doolittle — real name Eliza Sophie Caird — has cast off the Crayola colors and denim cutoffs in favor of something akin to a Nirvana-listening grunge groupie. She's wearing ripped jeans slung low below her hips, revealing a familiar flash of flesh, with a non-descript dark top and scuffed Pumas. The 25-year-old Londoner tells us about her sophomore album "In Your Hands" (out now), post-breakup blues and why her look makes her feel liberated.
You're a big fan of small clothes and flashing a little bit of skin. Do you shrink your clothes or shop in the kid's section?
[Laughs] I have a cashmere jumper that I shrank in the wash and yeah, sometimes I like that kind of kid's T-shirt look.
You were at the Henry Holland show. What do you like about him?
Henry's more than a designer, he's an inventor. He was the first one to do the bandana print that's gone crazy.
Normally you're in bright colors. Do you ever just want to be inconspicuous and wear black?
I actually haven't been wearing as many colors as I used to. I'm the kind of person that gets obsessed with one thing until I get bored and then I move on. Right now, I'm loving baggy jeans with rips.
When did you decide to start flashing a bit of flesh?
It wasn't a decision and I don't really think I flash that much. My rule is no nipples, no nunny.
Well that kind of kills my next question, but are you ever worried about being branded slutty?
No, I think I'm more of a free spirit. If I cover up too much it doesn't feel right.
Is it kind of liberating, like being naked?
Yeah, it's liberating and itreally is just a comfort thing for me — I don't think I'm overtly sexual in the way I dress. If I were covering up all the time, it wouldn't express who I am.
While we're speaking of expression, is making music a cathartic experience for you?
Music is the only thing that is going to be there for me no matter what. So when I finish a song, I play it out loud — it's the best thing I've ever felt. Better than love, I think. ... Sometimes I can tell when I'm writing catchy melodies and I'm proud of it. Although, if there were an actual formula for it, I'd be f—ing loaded by now.


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The Disability Resources Office envisions a campus community where all students with disabilities are valued and informed.
Its mission is to facilitate the educational and personal development of SUNY Cortland students with disabilities. Our goal is to ensure equal access to all programs and activities and facilitate the architectural and attitudinal accessibility of the campus environment. Accordingly, the office serves in a multidimensional role as advocate, educator, and coordinator of accommodations. Operational philosophy is rooted in the belief that the persons served are students first and disabilities are secondary.
You may read our newsletter and follow us on Facebook, Twitter, and on our Academic Apps blog.
Log into the Test Administration Scheduling System. More information on the system and test accommodations can be found on our Test Administration Services web pages for students and faculty.


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Orphan Black: Watch Season 1 Episode 3 OnlineMatt Richenthal at . Comments
Sarah reacted to the revelation that she's one of many clones on Orphan Black Season 1 Episode 3, growing more anxious than ever to get her money and get out of town.
But she hit a slight obstacle in this plan when her ruse as a detective led her to the body she buried.
Viewers also saw Alison, Cosima and Sarah meet for the first time on this installment, with Cosima trying to explain to Sarah just what the heck is going on.
Elsewhere, Felix actually interacted with Alison and Sarah was yelled at for breaking "the first rule of clone club." What is it? Watch the installment from start to finish now and find out:
Matt Richenthal is the Editor in Chief of TV Fanatic. Follow him on Twitter and on Google+.