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This statement is effective as of May 14, 2014. Please see previous version here.
This website is brought to you by British Motor Car Distributors, LTD (collectively, "we," "us," or "our").We respect the privacy of our users and those who visit our websites, mobile and other online applications and products and services (collectively referred to as "our website"). By using our website you consent to the use of your information and information about you in accordance with this Privacy Statement.
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We use commercially reasonable administrative, technical, personnel, and physical security measures designed to safeguard information about you in our possession against loss, theft and unauthorized use, disclosure or modification. Of course, despite these measures, we cannot guarantee perfect security of networks, servers and databases we operate or that are operated on our behalf.
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Our goal is to make your car buying experience the best possible. British Motor Car Distributors, LTD's virtual dealership offers a wide variety of new and used cars, Bentley, Lamborghini, Pagani incentives, service specials, and Bentley, Lamborghini, Pagani parts savings. Conveniently located in San Francisco, CA we also serve the greater Bay Area, East Bay and Marin County.
If you're looking to purchase your new dream car, you've come to the right place. At British Motor Car Distributors, LTD we pride ourselves on being the most reliable and trustworthy Bentley, Lamborghini, Pagani dealer around. Our inventory is filled with some of the sweetest rides you've ever seen!
We're the kind of Bentley, Lamborghini, Pagani dealer that takes the time and listens to the wants and needs of our clients. We understand that buying a car is a process that takes a certain amount of careful consideration.
It's a lot to wrap your head around but at British Motor Car Distributors, LTD we do our best to make the car buying experience an easy one. We're the kind of San Francisco, CA car dealer that helps you decide exactly what you're looking for. We won't ever make a sale that our customers will end up being unhappy with. We're proud to be the type of San Francisco, CA Bentley, Lamborghini, Pagani dealer that strives for 100% customer satisfaction.
We are the San Francisco, CA car dealership that caters for a whole variety of clientele. We understand that all of our clients have different financial situations and have done our best to ensure that our cars come in a variety of different shapes and sizes, and that their price tags vary as well. We not only have an amazing selection of brand new cars but have also acquired an impressive selection of pre-owned vehicles that are just as fantastic.
Because our customers are so important to us, we'll also take the time to find you some great financing options if you need them. At some point in our lives we all need a little financial boost, and at British Motor Car Distributors, LTD we do our best to find a reasonable loan that enables you to purchase the car you've always dreamed of.
If you would like to get in touch with us please don't hesitate to give us a call at (415) 477-7196 or stop by for a visit.
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Greetings Guest!!Dismiss Notice
In order to combat SPAM on the forums, all users are required to have a minimum of 2 posts before they can submit links in any post or thread.
[Buying] wanting to buy these LS items
Discussion in 'UO Rares Collector' started by Fraggles, May 2, 2010.

subset: commoncrawl


text: Mine's GT-R Runs 59.4sec Lap of Tsukuba, Coming To US?Mark Arnold2/21/08 11:20amFiled to: Tuner CarsMINE'SMinesMitsubishi EVO XNissanNissan GTRR35Subaru WRX STIGtrjdmTuners18EditPromoteShare to KinjaToggle Conversation toolsGo to permalink No, I'm not saying that I personally have a Nissan GT-R. I'm talking about Mine's, the Japanese Tuner of Gran Turismo and Best Motoring fame. Recently, they brought their R35 GT-R with all the Mine's go-fast goodies to the Tsukuba Circuit to do some testing, and they left with a best lap of 59.367 seconds. To put this in perspective, a normal R35 GT-R will run a lap of about 1:02, and a new Mitsubishi Evo X or Subaru STi will do it in about 1:06. To run a sub-one-minute lap is a benchmark for turbo-crazed JDM tuners. Of course, with a notable lap time, there are always factors (weather, driver) that have little to do with the actual car. Either way, the Their's Your's Mine's GT-R is indeed an impressive piece of kit. They've upgraded the suspension, exhaust, brakes, intake, rear spoiler, and the computer chip. Still in development are parts to further aid the aerodynamics of the mirrors, hood, front canards, front spoiler and side outlets. And what's even better— we hear they're bringing it to the US. All we've heard is that Mine's is bringing their white test car here next month. We're not exactly sure why this mega-Godzilla is coming to our shores, but we thought we'd give you a warning now, just in case things go terribly wrong and the monster destroys a city or eats a helicopter or something. [2009GTR.com][GT Channel]Reply18 repliesLeave a reply


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The Dimond Branch Library will temporarily close for remodeling from Friday, December 23 to May 2017. For more information see the announcement.
2-Part series Medicare and Healthcare Enrollment
Denise Lombard, Health, Long-term Care, Disability and Life Insurance Specialist will be answering questions on Healthcare and Healthcare Providers. She will also be enrolling participants into qualified healthcare programs.
The dates for the Healthcare Programs are; Saturday, September 13, 2014-12:30pm; Saturday, December 6, 2014-10:30am.


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DSL that enables you to navigate and find data within your JSON documents
JSPath is a domain-specific language (DSL) that enables you to navigate and find data within your JSON documents. Using JSPath, you can select items of JSON in order to retrieve the data they contain.
JSPath for JSON is like an XPath for XML.
It's heavily optimized both for Node.js and modern browsers.
You can install using Node Package Manager (npm):
npm install jspath
It also supports RequireJS module format and YM module format.
JSPath has been tested in IE6+, Mozilla Firefox 3+, Chrome 5+, Safari 5+, Opera 10+.
JSPath;// or JSPath;
|path expression
|any valid JSON
|input JSON document
|substitutions (optional)
Result will be:
'Jazz' 'Accord'
JSPath expression consists of two type of top-level expressions: location path (required) and predicates (optional).
To select items in JSPath, you use a location path. The location path consists of one or more location steps. Every location step starts with dot (.) or two dots (..) depending on the item you're trying to select:
You can use the wildcard symbol (*) instead of exact name of property:
If you need to locate property containing non-alphanumerical characters, you can use quoted notation:
Also JSPath allows to join several properties:
Your location path can be absolute or relative. If location path starts with the root (^) you are using an absolute location path — your location path begins from the root items.
Consider the following JSON:
var doc = "books" : "id" : 1 "title" : "Clean Code" "author" : "name" : "Robert C. Martin" "price" : 1796 "id" : 2 "title" : "Maintainable JavaScript" "author" : "name" : "Nicholas C. Zakas" "price" : 10 "id" : 3 "title" : "Agile Software Development" "author" : "name" : "Robert C. Martin" "price" : 20 "id" : 4 "title" : "JavaScript: The Good Parts" "author" : "name" : "Douglas Crockford" "price" : 1567 ;
// find all books authors JSPath;/* [{ name : 'Robert C. Martin' }, { name : 'Nicholas C. Zakas' }, { name : 'Robert C. Martin' }, { name : 'Douglas Crockford' }] */ // find all books author names JSPath;/* ['Robert C. Martin', 'Nicholas C. Zakas', 'Robert C. Martin', 'Douglas Crockford' ] */ // find all names in books JSPath;/* ['Robert C. Martin', 'Nicholas C. Zakas', 'Robert C. Martin', 'Douglas Crockford' ] */
JSPath predicates allow you to write very specific rules about items you'd like to select when constructing your expressions. Predicates are filters that restrict the items selected by location path. There're two possible types of predicates: object and positional.
Object predicates can be used in a path expression to filter a subset of items according to a boolean expressions working on a properties of each item. Object predicates are embedded in braces.
Basic expressions in object predicates:
JSPath allows to use in predicate expressions following types of operators:
|Returns is true if both operands are equal
|.books{.id == "1"}
|Returns true if both operands are strictly equal with no type conversion
|.books{.id === 1}
|Returns true if the operands are not equal
|.books{.id != "1"}
|Returns true if the operands are not equal and/or not of the same type
|.books{.id !== 1}
|Returns true if the left operand is greater than the right operand
|.books{.id > 1}
|Returns true if the left operand is greater than or equal to the right operand
|.books{.id >= 1}
|Returns true if the left operand is less than the right operand
|.books{.id < 1}
|Returns true if the left operand is less than or equal to the right operand
|.books{.id <= 1}
Comparison rules:
If both operands are strings, there're also available additional comparison operators: ####String comparison operators####
|Like an usual '==' but case insensitive
|.books{.title == "clean code"}
|Returns true if left operand value beginning with right operand value
|.books{.title ^== "Javascript"}
|Like the '^==' but case insensitive
|.books{.title ^= "javascript"}
|Returns true if left operand value ending with right operand value
|.books{.title $== "Javascript"}
|Like the '$==' but case insensitive
|.books{.title $= "javascript"}
|Returns true if left operand value contains right operand value
|.books{.title *== "Javascript"}
|Like the '*==' but case insensitive
|.books{.title *= "javascript"}
|Returns true if both operands are true
|.books{.price > 19 && .author.name === "Robert C. Martin"}
|Returns true if either operand is true
|.books{.title === "Maintainable JavaScript" || .title === "Clean Code"}
|Returns true if operand is false
Logical operators convert their operands to boolean values using next rules:
|1 (top)
|! -unary
|* / %
|+ -binary
|< >=
|== === != !== ^= ^== $== $= *= *==
Parentheses are used to explicitly denote precedence by grouping parts of an expression that should be evaluated first.
// find all book titles whose author is Robert C. Martin JSPath;/* ['Clean Code', 'Agile Software Development'] */ // find all book titles with price less than 17 JSPath;/* ['Maintainable JavaScript', 'JavaScript: The Good Parts'] */
Positional predicates allow you to filter items by their context position. Positional predicates are always embedded in square brackets.
There are four available forms:
index] — returns
index-positioned item in context (first item is at index 0), e.g. [3] returns fourth item in context
index:] — returns items whose index in context is greater or equal to
index, e.g. [2:] returns items whose index in context is greater or equal to 2
index] — returns items whose index in context is smaller than
index, e.g. [:5] returns first five items in context
indexTo] — returns items whose index in context is greater or equal to
indexFrom and smaller than
indexTo, e.g. [2:5] returns three items with indices 2, 3 and 4
Also you can use negative position numbers:
// find first book title JSPath;/* ['Clean Code'] */ // find first title of books JSPath;/* 'Clean Code' */ // find last book title JSPath;/* ['JavaScript: The Good Parts'] */ // find two first book titles JSPath;/* ['Clean Code', 'Maintainable JavaScript'] */ // find two last book titles JSPath;/* ['Agile Software Development', 'JavaScript: The Good Parts'] */ // find two book titles from second position JSPath;/* ['Maintainable JavaScript', 'Agile Software Development'] */
You can use more than one predicate. The result will contain only items that match all the predicates.
// find first book name whose price less than 15 and greater than 5 JSPath;/* ['Maintainable JavaScript'] */
Substitutions allow you to use runtime-evaluated values in predicates and pathes (as a path root).
var path = '.books{.author.name === $author}.title'; // find book name whose author Nicholas C. Zakas JSPath;/* ['Maintainable JavaScript'] */ // find books name whose authors Robert C. Martin or Douglas Crockford JSPath;/* ['Clean Code', 'Agile Software Development', 'JavaScript: The Good Parts'] */
Result of applying JSPath is always an array (empty, if found nothing), excluding case when the last predicate in top-level expression is a positional predicate with the exact index (e.g. [0], [5], [-1]).
In this case, result is an item at the specified index (
undefined if item hasn't found).


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Chilled Cherry Soup
|1⁄2 Cup (8 tbs)
|Orange slices
|6 (Thin Slices)
|Lemon slices
|6 (Thin Slices)
|Sliced fresh peaches
|1 Cup (16 tbs)
|Pitted cherries
|2 Cup (32 tbs)
|1⁄2 Cup (8 tbs)
|1⁄2 Teaspoon
|1 Dash
|1 Cup (16 tbs)
|1 Tablespoon
|Whipped cream
|1 Tablespoon (For Garnish)
Put fruit, sugar, cinnamon, salt, and water into cooker.
Close cover and put pressure control in place.
When pressure is reached, remove from heat and cool cooker at once under running water.
Remove 1/4 cup liquid from fruit.
Mix cornstarch with this; return to open cooker.
Stir for 1 minute more as mixture thickens slightly.
Put in a bowl and chill.
When served, garnish soup with whipped cream.
Recipe Summary
Rate It
Nutrition Rank
Nutrition Facts
Serving size
Calories 189 Calories from Fat 9
% Daily Value*
Total Fat 0.95 g1.5%
Saturated Fat 0.58 g2.9%
Trans Fat 0 g
Cholesterol 3.6 mg1.2%
Sodium 26.8 mg1.1%
Total Carbohydrates 47 g15.6%
Dietary Fiber 1.7 g6.6%
Sugars 37.7 g
Protein 0.92 g1.8%
Vitamin A 1.9% Vitamin C 61.7%
Calcium 1.8% Iron 2.1%
*Based on a 2000 Calorie diet


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5 Irresistible Gifts For A Healthier Easter Basket
Be inspired with our Easter gift basket ideas to make sure your kids stay in love with the Easter Bunny without OD-ing on chocolate and sweet treats!
Worried about the quantity of chocolate your kids are going to consume this Easter? Here's how to make sure they stay in love with the Easter Bunny – without OD-ing on sweet treats.
Easter Gift Basket Ideas With A Healthy Spin
Tot up the number of chocolate eggs heading your children's way this Easter and you'd be forgiven for worrying about their dental health. So take the chance to swap in a few healthier treats when you're building this year's Easter basket…
1. Slip in a cute soft toy – a bunny or chick would be most appropriate – to fill a bit of space without upping the calorie-count.
2. The Easter bunny eats carrots, right? Give his favourite veg a bit of child-appeal by tying a few carrot sticks or a mini Chantenay with seasonal ribbon or a snazzy popband before tucking into this year's treats basket.
3. Instead of mini chocolates, pack a traditional hollow cardboard or plastic egg with healthier trailmix, unsalted nuts and dried fruits.
4. Replace sweets with egg-shaped gifts, like a deliciously-scented eos lip balm (all the rage in the playground) or a LUSH bath bomb (they've got some great Easter-themed options). Watch out that smaller children don't try and take a bite, though…
5. Make a popcorn butterfly: Fill a sealable sandwich bag with popcorn and clip down the middle with a clothes peg to create 'wings'. Draw on a face and use craft wire to create antennae. Cute and healthy! Find more great no-candy snack ideas here.


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You missed it This great deal for GrindHouse MMA is over. But don't despair, we've got more great deals every day.
Related Deals That You May Like
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back by popular demand:
GrindHouse MMA
Classes at a Premier Mixed Martial Arts Facility
- Save 67%
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One of the largest mixed martial arts facilities in Missouri, GrindHouse MMA can bring out the fierce fighter within while also getting you in shape:
• $49 ($150 value) for one month of classes
• Classes have something for all experience levels
• Check out the weekly schedule
Why You'll Love It
GrindHouse's 5,300-square-foot facility is equipped with a 3,000-square-foot matted area, 20-foot MMA cage, weight and cardio machines, and much more. Muay Thai, boxing, boot camp, and MMA are a few of the wide variety of skill and fitness classes offered at this Lee's Summit center.
PAID VALUE EXPIRES ON February 20, 2022
PROMOTIONAL VALUE EXPIRES ON April 30, 2014


text:
Book your train journey to more than 1000 destinations in Europe.
Check timetables anywhere in Europe with our train planner.
Find the lowest fares at one glance on our top connections!
Book your hotel at the best rates with our partner Booking.com
Rent your car at the best rates all over Europe.
Did you book your train tickets at SNCB Europe, either online, through our app or via our contact centre? With MyTrain, you can find all your booking details, such as departure times or seat numbers, very easily.
And if you have a MyTrain profile, you can enjoy even more advantages:
- You can cancel or change your bookings online
- You can print out your tickets again at any time
- You can store your details and travel preferences and save time with each new booking
ICE trains serve the following stations amongst others:
BELGIUM : Bruxelles-Midi/Brussel-Zuid (Brussels), Bruxelles-Nord/Brussel-Noord (Brussels) and Liège-Guillemins ● THE NETHERLANDS : Amsterdam Centraal, Utrecht Centraal and Arnhem ● GERMANY : among others Köln Hbf (Cologne), Aachen Hbf, Frankfurt (Main) Hbf, Frankfurt Flughafen (airport), Berlin Hbf, Düsseldorf Hbf, Essen Hbf, Hamburg Hbf, München Hbf and Nürnberg Hbf (Nuremberg) ● SWITZERLAND : Basel SBB ● AUSTRIA : among others Linz Hbf and Wien Hbf (Vienna)
International ICE train tickets (to or from Germany, Austria or Switzerland) will now be issued from the Belgian train station of your choice. This means that your ticket price remains the same, regardless of whether you are travelling to/from Brussels, Liège, Antwerp, Ghent, etc.
Please note: the ICE departure/arrival train stations remain the same (Brussels (Midi/Zuid and Nord/Noord) and Liège-Guillemins). This means that you still need to change onto a Belgian domestic train for your connecting journey in Belgium. When booking your ticket, please specify your departure/arrival station in Belgium so that your ticket continues to be valid in Belgium.
Find out more >
There is a charge to use the Wi-Fi network in 2nd class on all ICE trains in Germany, while access to the network in 1st class is free. Note that there is no WiFi (in either 1st or 2nd class) on ICE trains while on Belgian or Dutch territory. Therefore on a journey from Brussels to Frankfurt, passengers can access WiFi from Aachen onwards.
See ICE routes with Wi-Fi access (in German).
The BordBistro is available to all passengers and offers a selection of light meals, sandwiches, salads, hot snacks and beverages.
The ICE 3 carriages (on the high-speed line between Cologne and Frankfurt) offer a Panorama Lounge where passengers can watch the train driver thanks to a glass partition! Panorama Lounges are available in 1st and 2nd class.
For seat reservations in the Panorama Lounges call the SNCB Europe Contact Centre on +32 (0)70 79 79 79 (int. charges - € 0.30/min.) or reserve at one of the 28 Belgian stations with international sales.
In Cologne, Frankfurt Airport and Frankfurt, 1st class passengers have access to the DB Lounges where they can get free coffee, tea and other beverages. Passengers can watch television on the large screens or read a variety of magazines and newspapers. Dedicated work areas with Internet connection are also available.
In contrast to other railway companies, no different fares for 'adults', 'youth' or 'seniors' are available for ICE services. Instead, you can choose between two fare categories: 'Sparpreis' and 'Flexpreis'. These are available in 1st and 2nd class. There are also fares for children (under 15 years old) and passengers with reduced mobility.
Tip: when booking online, you just indicate the number of passengers per age group and our booking system automatically gives you all the corresponding fares.
Seat reservation is always optional in 2nd class and costs €5 per journey (for both Sparpreis and Flexpreis fares). In 1st class, however, seat reservation is automatically included in the price of your ticket.
Check available fares online >
Children younger than 15 years old travel free of charge if they are accompanied by at least one parent or grandparent with either a Sparpreis or a Flexpreis ticket.
Please note:
Children travelling alone :
Passengers with reduced mobility and their companions
Blind and visually-impaired passengers and companions or guide dogs
Find your seat on board the ICE 3 trains between Brussels, Cologne and Frankfurt >


text:
Tropical Fish Keeping - Aquarium fish care and resources (http://www.tropicalfishkeeping.com/forum.php)
- Freshwater Aquarium Equipment (http://www.tropicalfishkeeping.com/freshwater-aquarium-equipment/)
- - Extra surface agitation (http://www.tropicalfishkeeping.com/freshwater-aquarium-equipment/extra-surface-agitation-12039/)
Extra surface agitation
I'm worried that my tank doesn't have enough surface agitation. The only thing oxygenating the tank right now is the filter, a magnum 350 in an 85 gallon tank (there's no fish in it yet). I'm just not convinced that air stones are the way to go, and I don't really want a wall of air bubbles.
What's your favorite, most discreet equipment you use for this?
Leave the water just low enough that the water returning from the filter actually has to fall into the tank. Best way I can think of.
Next would be to use a powerhead to spray air into the tank. Could be done at the bottom if you wanted to. Most descent powerheads come with a connection for airline.
Yeah, I've got the water falling about an inch from the filter back into the tank right now. I think I'll add a small/cheap powerhead since I can disguise it pretty well behind the top edging of the tank.
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The nutritional essentiality of zinc for the growth of living organisms had been recognized long before zinc biochemistry began with the discovery of zinc in carbonic anhydrase in 1939. Painstaking analytical work then demonstrated the presence of zinc as a catalytic and structural cofactor in a few hundred enzymes. In the 1980s, the field again gained momentum with the new principle of "zinc finger" proteins, in which zinc has structural functions in domains that interact with other biomolecules. Advances in structural biology and a rapid increase in the availability of gene/protein databases now made it possible to predict zinc-binding sites from metal-binding motifs detected in sequences. This procedure resulted in the definition of zinc proteomes and the remarkable estimate that the human genome encodes ~3000 zinc proteins. More recent developments focus on the regulatory functions of zinc(II) ions in intra- and intercellular information transfer and have tantalizing implications for yet additional functions of zinc in signal transduction and cellular control. At least three dozen proteins homeostatically control the vesicular storage and subcellular distribution of zinc and the concentrations of zinc(II) ions. Novel principles emerge from quantitative investigations on how strongly zinc interacts with proteins and how it is buffered to control the remarkably low cellular and subcellular concentrations of free zinc(II) ions. It is fair to conclude that the impact of zinc for health and disease will be at least as far-reaching as that of iron.
The chronology of events in the research of zinc biology is revealing as it unfolds through different disciplines and demonstrates an ever-increasing variety of functions. Three phases of discovery can be discerned: 1) the recognition that zinc is essential for all forms of life, 2) the detection of zinc in enzymes and other proteins as a basis of its catalytic and structural functions, and 3) a role of zinc(II) ions in cellular regulation, which is the main subject of this article (Fig. 1). Knowledge about molecular functions of zinc emerged slowly as zinc is refractory to investigations with most spectroscopic techniques, and analysis in biological tissues was challenging before sufficiently sensitive methods such as flameless atomic absorption spectrophotometry became widely available. Also, many zinc proteins are of such low abundance that they escaped detection through direct analysis. So far, only bioinformatics and systems biology approaches have taught us the full extent to which zinc is involved in cellular biology. Yet, the role of zinc as a cofactor in proteins did not seem to explain all its biological functions. The third and most recent phase of discovery demonstrates that zinc(II) ions are regulatory ions akin to calcium(II) ions and are fundamentally important for cellular control. Again, new insights became possible only with the development of new tools, in this case the advent of chelating agents that fluoresce when binding zinc(II) ions and that allow measurement of zinc(II) ions in cells with a sensitivity exceeding that of most other analytical techniques. This article focuses on these latest developments that address the roles of zinc(II) ions in cellular regulation, which, so far, are unique among the essential transition metal ions. These roles increase the significance of zinc for cellular biology tremendously and suggest that the micronutrient zinc has much broader functions than any of the other transition metal ions, including iron.
Jules Raulin, who trained under Louis Pasteur, reported in 1869 that zinc is essential for the growth of the fungus Aspergillus niger (1). His work is remarkable and decisive because he used chemically defined media to arrive at his conclusion. In the 1920s, it was discussed whether the presence zinc in human tissues is the result of environmental exposure that would affect humans adversely. Investigators at the Harvard School of Public Health in Boston measured zinc concentrations in human tissues and concluded that zinc is present endogenously and may serve biological functions (2, 3). It is instructive to read the conclusion of Drinker's and Collier: "one is struck…by the...failure of investigators to recognize this normal universality of zinc...leads us to believe that zinc is indispensable for the normal functioning of the body" (3). Considerable time elapsed after Raulin's original observation until zinc was shown to be essential for rats (1934) and for humans (1961) (4, 5). This early period of discovery was the subject of a Federation of American Societies for Experimental Biology symposium organized by Boyd O'Dell (6).
The biochemistry of zinc began in 1939 when erythrocyte carbonic anhydrase was found to contain stoichiometric amounts of zinc and the zinc was shown to be essential for its enzymatic activity (7). Thus, knowledge of a role of zinc in proteins preceded Ananda Prasad's seminal discovery of human zinc deficiency by more than twenty years (8). A second zinc enzyme, bovine pancreatic carboxypeptidase, was identified only fifteen years after the discovery of zinc carbonic anhydrase (9). Advances in analytical methods for isolating proteins and measuring metals in biological material, the latter largely pioneered by the late Bert L. Vallee and his colleagues (10), led to the discovery of hundreds of zinc proteins in all classes of enzymes, i.e., oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases (11).
A huge impact on the development of the field was the observation that Xenopus laevis transcription factor IIIA contains 9 repetitive sequences of C (cysteine) and H (histidine) residues that are involved in the binding of 9 zinc ions (12). This characteristic ligand signature of metal-coordinating amino acid side chains interspersed with noncoordinating amino acids ("spacers" a, b, c,) (CXaCXbHXcH, coordination type C2H2) forms relatively small protein domains that interact with nucleic acids like the fingers of a hand gripping a rod and hence became known generically as a "zinc finger." In these sites, zinc has primarily a structural role. At about the same time, nucleotide sequence databases increased rapidly in number and size and led to the landmark event of the sequence of the human genome. These databases allowed searches for homologies with established signatures of metal-coordinating amino acids and made it possible to predict zinc-binding sites. Using only the signature of the classic C2H2 zinc finger motif, 5092 protein domains containing this motif were identified in the human genome (13). The actual number of zinc proteins with this motif is smaller, however, because many proteins contain several zinc fingers, with as many as 36 zinc fingers observed in one particular protein. Also, signatures and 3-dimensional structures of other structural zinc sites in protein domains were discovered, such as sites with 4 cysteine ligands (C4), with 3 cysteine ligands and 1 histidine ligand (C3H), with 1 aspartate (D) and 3 histidine ligands (DH3), and others (14). Mining of databases for these signatures further increased the number of zinc proteins. Thus, in addition to the hundreds of zinc enzymes, hundreds of zinc finger proteins were now known. Many of the zinc-binding domains do not interact with nucleic acids but rather with other proteins, and, in some cases, with lipids (15, 16). It became customary to assign zinc finger domains in newly discovered proteins based on sequence homology rather than performing a chemical analysis of zinc. Predictions were initially verified experimentally. A now classic example is the prediction of a zinc binding site in human leukotriene A4 (LTA4)2 hydrolase. LTA4 hydrolase has a signature HExxH…E (E, glutamate) that aligns with that of the catalytic zinc in the bacterial proteinase thermolysin (17). Metal analysis confirmed that LTA4 hydrolase is indeed a zinc enzyme (18). The analogy with thermolysin suggested that LTA4 hydrolase has peptidase activity, which was then also confirmed experimentally (19). The crystal structure of human LTA4 hydrolase proved the prediction about its zinc-binding site to be correct (20).
When the entire human genome was scanned for zinc-binding signatures, it was predicted that at least 3% of the genes encode zinc proteins (21). However, it was pointed out that the actual zinc proteome could be considerably larger because this approach does not account for all zinc-protein interactions (22). Indeed, a bioinformatics approach led to the prediction that at least 10% (~2800 gene products) of the human genome encodes zinc proteins (23). This approach combines the information from databases for protein structures (24) and for protein domains (25) to scan gene databases, uses an automated procedure for analysis, and sets guidelines for manual curation of the information (26). Three data sets were obtained: metalloproteins with known signatures and unknown domains (2406 proteins), metalloproteins with known signatures and known domains (2506), and metalloproteins with unknown signatures and known domains (2407). The total number of zinc proteins is 3207; 2430 are identified by at least two methods and 1684 zinc proteins by all three methods (signatures, domains, annotations). As possible zinc proteins are counted: 397 hydrolases; 302 ligases; 167 transferases; 43 oxidoreductases; 24 lyases/isomerases; 957 transcription factors; 221 signaling proteins; 141 transport/storage proteins; 53 proteins with structural metal sites; 19 proteins involved in DNA repair, replication, and translation; 427 zinc finger proteins of unknown function; and 456 proteins of unknown function. The number of zinc proteins correlates linearly with the number of genes in a particular genome and is higher in eukarya (8.8%) than in bacteria and archaea (5–6%) (27). The increase in the zinc proteome in eukarya is due to the large number of additional zinc proteins involved in regulation, such as the zinc-binding domains of zinc finger proteins that extend considerably the conformational landscape of proteins and hence the possibilities for interactions, i.e., the interactome.
Predictions estimating the number of zinc proteins in the human zinc proteome demonstrated that the widespread use of zinc is in protein structure and function. However, they are based on known signatures and therefore are inherently limited (28–30). There are some examples of false positives, where zinc is not present in the protein because the site does not bind zinc or the site binds a different metal. Predictions do not take into account either where the protein is localized in the cell or the differences in metal utilization in some compartments such as mitochondria. Also, zinc binds between protein subunits, a function that it serves exceptionally well because it is redox inert and binds stronger than the other essential metal ions except copper(II). In these interface zinc sites, zinc has catalytic functions or, more frequently, structural functions in the quaternary (same subunits) or quinary (different subunits) structure of proteins (31). Because the ligands of interface zinc sites stem from different proteins and coordination may involve only one or two ligands from each of the protomers, signatures cannot be readily identified and used for homology searches, thus precluding estimates of the total number of such sites. Yet other proteins bind zinc transiently. This category includes proteins involved in the regulation of cellular zinc homeostasis and proteins that are regulated by zinc. Signatures of these sites are incomplete, raising questions as to the extent that additional signatures will increase the size of the zinc proteomes. Indeed, experimental work indicates that interactions of zinc with proteins are more frequent than predictions suggest (32). Extensive reviews on this second phase of discovery exist (33, 34). The third and ongoing phase of discovery focuses on the fact that free zinc(II) ions in addition to protein-bound zinc(II) ions are important for functions of zinc in biology.
With so many proteins requiring zinc, the questions of how, when, and where zinc is made available for proteins to become zinc proteins came increasingly into focus. A comprehensive answer is lacking, however. It is also not known whether the allocation of zinc when zinc becomes limiting occurs with any type of hierarchy to conserve basic zinc-dependent functions while suspending others. Another critical question is which processes and molecules control systemic homeostasis of zinc. A hormone such as hepcidin controlling iron metabolism has not been identified for the control of zinc. With discoveries of proteins involved in cellular zinc homeostasis, it became clear how complex the control is. Dozens of transporters were identified, in contrast to iron, where there are only a few. However, the specificity of most of these transporters is not well established. They are called zinc transporters, but several of them also transport other metal ions. The transporters are localized on the plasma membrane and on intracellular membranes. This extensive compartmentalization is characteristic for cellular zinc metabolism.
Several dozen proteins regulate cellular zinc. They store and release zinc, bind any excess of zinc to avoid unspecific reactions, transport zinc through membranes and cellular compartments, or sense zinc(II) ion concentrations.
Ten members of the zinc (Zn) transporter (ZnT) family (SLC30A) export zinc from the cytosol, whereas 14 members of the ZRT/IRT-like protein (Zip) family (SLC39A) import zinc into the cytosol. Together these transporters control cellular zinc and its traffic through the plasma membrane and between cytosol and various cellular compartments (35, 36). The transporters are regulated transcriptionally, translationally, and at the protein level through heterodimer formation, ubiquitination, phosphorylation, and proteolysis (35–37). Three-dimensional structures of Zip proteins are not available. Some of the members of the family may have additional zinc binding sites (38), which is the case for ZnT proteins. Escherichia coli Yiip is a homolog of the human ZnT proteins and a Zn2+/H+ antiporter residing in the inner membrane. Its 3-dimensional structure shows a dimeric protein with a transmembrane domain and a cytoplasmic domain and several zinc-binding sites in the monomer: a zinc site between the transmembrane helices involved in zinc transport, a zinc-binding site between the two domains with unknown function, and a binuclear zinc binding site in the cytoplasmic domain, which is thought to sense cytoplasmic zinc(II) ion concentrations and trigger a conformational change that allows transport of zinc through the membrane (39). Metal-response element–binding transcription factor-1 (MTF-1) is the only known eukaryotic zinc(II) ion sensor. It controls zinc-dependent gene expression of proteins at increased zinc concentrations. Sensing is thought to occur through a pair of its 6 zinc fingers with lower affinity for zinc than the other zinc fingers (40). In human MTF-1, the acidic activation domain also participates in metal sensing (41). MTF-1 is an essential protein in development as its genetic ablation in mice is embryonically lethal (42).
Humans have at least a dozen different metallothioneins (MTs), proteins with 60–68 amino acids, among which 20–21 are cysteines (43). The gene expression of most of them is under the control of MTF-1. Their expression increases the cellular zinc-binding capacity when the cellular zinc concentration increases. Characterization of the isolated protein demonstrated that zinc is bound exclusively to the sulfur donors of 20 cysteines in 2 zinc/thiolate clusters, 3 zinc(II) ions in the N-terminal cluster with 9 cysteine ligands, and 4 zinc(II) ions in the C-terminal cluster with 11 cysteine ligands (44, 45). Every one of the 7 zinc(II) ions binds to 4 sulfurs of cysteines. At least two properties of MTs are remarkable with regard to those of other zinc proteins. One property is the different affinities of binding sites for zinc in human MT-2 despite the fact that all 7 zinc(II) ions are in tetrathiolate coordination environments (46). With these characteristics, MTs are not simply trapping any zinc for storage but serve dynamic functions as both zinc acceptors and zinc donors. The other property is that MTs are redox proteins. Generally, zinc is redox inert in biology. However, in coordination environments with sulfur donors, sulfur is redox active, and redox reactions can modulate the stability of the complex (47). This chemistry makes it possible to mobilize zinc(II) ions from high-affinity sites. In this way, the redox environment affects the metal load of MT and the concentrations of cellular free zinc(II) ions. Oxidation of the sulfur donors leads to zinc release, whereas reduction of the oxidized sulfurs leads to zinc binding. An important consequence of these properties is that the structure of MT in vivo depends on both metal ion availability and redox state and is not necessarily the one derived from investigations in vitro with 7 zinc ions and all 20 cysteines reduced. It is important to recall that MTs isolated from natural sources are generally heterogeneous and that preparation of MT involves removing the metals, reducing any disulfides, and then reconstituting the protein with a complement of a given metal ion to obtain a homogeneous preparation. In vivo, the structure of MT is dynamic, and MT occurs with different metal loads, metal composition, and in different redox states. For example, the composition in eye tissue is Zn6Cu-MT, whereas it is Zn7-MT when the protein is induced with zinc (48). MT has a higher copper content when isolated from fetal or neonatal liver (49). The metal composition of isolated MT-3, which is a neuronal growth inhibitory factor, is Zn3–4Cu4-MT-3 (50). A crystal structure of MT was obtained from rat MT-2 induced with cadmium. This MT has an overall composition Cd5Zn2-MT with 2 zinc ions located at defined positions in the N-terminal domain (45). Thus, the metal composition of MT changes when the organism is exposed to metals in the environment, under physiological conditions, and in diseases that affect metal availability. MT is not fully saturated with zinc in the liver, as reflected by measurements of ~10% of the apoprotein and by the capacity to bind additional zinc (51). These results are consistent with the observation that the affinity of the protein for one of the seven zinc ions is much weaker than the affinities for the others (46). Also, the cysteines of MT may not be fully reduced under physiological conditions. MT with some of its cysteines oxidized has been observed in a cell line that produces increased amounts of reactive oxygen species (52) and in the heart of mice that have been oxidatively stressed with doxorubicin (53).
Zinc, like every other essential metal ion, is maintained at specific cellular concentrations to enable zinc-specific reactions and to avoid interference with the functions of other essential metal ions, such as preventing the coordination of the wrong metal ion to a metalloprotein. One component of the cellular homeostatic control is the buffering of zinc. The concept of metal buffering is similar to that of hydrogen ion (proton) buffering. Whereas the pKa of a ligand determines the pH for proton buffering, the pKd of a ligand determines the pMe for metal buffering. In analogy to the concept of pH, the concentration of free zinc(II) ions is expressed as the zinc potential, pZn = −log[Zn2+]i (54). These relationships explain why it is mandatory to know the affinity of proteins for zinc at physiological pH (pKd) to understand zinc buffering and the control of cellular zinc. Affinities of ligands for divalent metal ions follow the Irving-Williams series, according to which zinc(II) ions bind stronger than the other divalent metal ions of the first transition series, except for copper(II) ions. Affinities of cytosolic zinc proteins for zinc are in the range of picomoles per liter dissociation constants (55). As a consequence, most of the zinc is bound, and the free zinc(II) ion concentrations are commensurately low. Direct measurements from several laboratories with different methods provide estimates of free zinc(II) ion concentrations in the range of tens to hundreds of picomoles per liter (pZn = 10–11) (Table 1) (56–63) and confirm that the consideration based on binding equilibria is a valid approximation. Of note, estimates were already reported 40 years ago when the inhibition of the magnesium enzyme phosphoglucomutase by zinc was measured. The authors concluded that for the enzyme not to be zinc inhibited in muscle, the free zinc ion concentration must be <32 pmol/L (57). The typical total cellular zinc concentrations are a few hundred micromoles per liter, but at least six to seven orders of magnitude higher than those of free zinc(II) ions. Free zinc(II) ions, in contrast to protein-bound zinc(II) ions, are not devoid of any ligands, but the nature of the ligands is not known. Other terms, such as readily or easily exchangeable, mobile and kinetically labile zinc, are used in the literature for pools of zinc. Each term has a different meaning, and the terms should not be used interchangeably. As small as the free zinc(II) ion concentrations are, they are not negligible. In fact, they are critically important in cellular regulation.
The buffering causes a specific concentration of zinc(II) ions (pZn values) and is not to be confused with the buffering capacity, which describes the strength of buffering and the resistance to change and not the pZn at which buffering occurs. The physiological zinc-buffering capacity in an epithelial cell line is ~15 μmol/L (60). It is not very high. In fact, if it were high, zinc(II) ions could not readily participate in biological regulation. In molecular terms, ~30% of the buffering capacity is based on thiol-containing ligands (64). Oxidation of thiols under oxidative stress decreases the zinc-buffering capacity, making cells more vulnerable to the adverse effects of additional zinc(II) ions. Cellular zinc buffering is a dynamic process in which the pZn, the buffering capacity, or both may change. Increasing the zinc-buffering capacity by changing ligand concentrations allows the cell to handle more zinc while keeping the pZn value constant. Lowering the buffering capacity allows the cell to change its pZn under conditions such as zinc influx/efflux. According to the theory of buffering, both increases and decreases of the pZn value would then occur more readily. The same cell can have different pZn values when proliferating, differentiating, or undergoing apoptosis (60, 64). The significance of these dynamic processes is that global or local changes of zinc(II) ion concentrations provide a way to control cellular processes.
If affinities (pKd values), which control buffering, were the only factor to control cellular zinc(II) ion concentrations, zinc could move only in one direction of thermodynamic gradients, i.e., from lower to higher affinity sites. This is clearly not the case. Additional mechanisms are necessary to populate sites of somewhat lower affinity with zinc. One mechanism is the release of zinc(II) ions from a compartment in which zinc(II) ions are not in thermodynamic equilibrium with the cytosol.
A characteristic feature of eukaryotic cells is the extensive compartmentalization of zinc. Cells restrict the availability of zinc(II) ions through compartmentalization and control zinc via dynamic coordination environments that modulate the kinetics of metal association and dissociation (65). The transfer of zinc between different cellular compartments requires a large number of transporters and contributes to buffering. Such movements of metal ions are a kinetic phenomenon. This additional component of buffering in biological systems has been referred to as muffling (66). By removing zinc from a particular compartment, such as the cytosol, cells can cope with much higher zinc loads than through buffering alone. Cellular zinc buffering is thus a combination of the cytosolic zinc-buffering capacity and the zinc-muffling capacity based on the activities of transporters that remove zinc(II) ions from the cytosol to an organelle or to the outside of the cell (67). Buffering and muffling are not just housekeeping functions. They are fundamentally important for allowing zinc(II) ion fluctuations to occur, and as such, they are critical for zinc(II) ions as regulatory ions. Sequestration of zinc(II) ions in a cellular compartment is one way to store zinc temporarily in the cell and then release it again on demand. Compartmentalization resolves a long-standing issue of whether cells store zinc. Zinc is mainly stored in vesicles rather than in a protein with a high zinc-binding capacity akin to ferritin in iron storage. The chemical state of zinc in vesicles is not known. Free zinc(II) concentrations in these vesicles are much higher (lower pZn values) than in the cytosol, indicating different buffering of zinc. Estimates are 1–100 μmol/L in insulin-storing granules (62). The determination of subcellular pZn values is an area of considerable current interest. Measurements indicate that some subcellular compartments have much lower free zinc(II) ion concentrations than cytosol. Estimates are 0.9 pmol/L for the endoplasmic reticulum (ER), 0.2 pmol/L for the Golgi (63), 0.2 pmol/L for the mitochondrial matrix (68), and 0.14 pmol/L for mitochondria (69).
Perhaps the most exciting area in contemporary zinc biology is the role of released zinc(II) ions in information transfer within cells and between cells (70). In pathways stimulus → increase of [Zn2+] → targets, zinc(II) ions are signals. The preference of zinc(II) ions for specific coordination environments in proteins endows these signals with a certain degree of specificity. The amplitudes of zinc(II) ion signals determine which proteins are targeted because any target must have a commensurate affinity for zinc. Under conditions of stimulation, cellular zinc(II) ion concentrations increase and reach concentrations of >2 nmol/L only under oxidative stress and in apoptosis. Unless the buffering capacity changes or is exhausted, they return to their resting concentrations within minutes (71). As for the estimates of the steady-state concentrations of free zinc(II) ions (Table 1), a consensus is building on the amplitudes of zinc(II) ion fluctuations. A variety of experimental paradigms, such as oxidative stress, exposure to glucose, electrical stimulation, and chemical displacement of zinc with the tighter binding mercury(II) ion, increase the cellular free zinc(II) ion concentrations to a similar degree (Table 2) (72–76). Although the control of zinc(II) ion fluctuations was discussed above, the following discussion focuses on how zinc(II) ion signals are generated, transmitted to, and terminated at targets.
In addition to the release of zinc from proteins, two pathways of vesicular release of zinc(II) ions increase the concentrations of free zinc(II) ions. The first one is the release of zinc from vesicles into the extracellular space. The prime example is the release of zinc(II) ions from synaptic vesicles in a subset of glutamatergic neurons (77). One target of the released zinc(II) ions is the postsynaptic N-methyl-d-aspartate receptor, which zinc inhibits at low nanomoles per liter concentrations (78). Zinc(II) ions also modulate the activities of other neuroreceptors, and there is reuptake with functional effects in the presynaptic cell (79, 80). Which targets of zinc(II) ions are physiologically important depends on the effective concentrations of synaptic zinc. Zinc(II) ions also occur in other nonsynaptic vesicles and are released from cells by exocytosis from these vesicles that are loaded with zinc(II) ions by different zinc transporters, ZnT3 in neurons in the brain, ZnT8 in pancreatic β cells, or ZnT2 in epithelial cells of the mammary gland (81). Cellular release of zinc(II) ions has been observed in a number of cells in exocrine and endocrine glands. Somatotrophic cells in the pituitary gland, pancreatic acinar cells, β cells of the islets of Langerhans, Paneth cells in the crypts of Lieberkühn, cells of the tubuloacinar glands of the prostate, epithelial cells of the epididymal ducts, and osteoblasts all secrete zinc(II) ions (82). In pancreatic β cells, zinc(II) ions participate in the formation and structure of hexameric insulin, the storage form of insulin in the granules. Zinc(II) ions are secreted together with insulin from β cells. The purpose of co-secretion is not entirely clear but may relate to paracrine functions or to avoiding the formation of amyloid deposits from amyloidogenic proteins such as insulin and amylin. In mammary epithelial cells, exocytotic vesicles contain zinc(II) ions and supply the milk with zinc. Fluctuations of intracellular free zinc(II) ions occur in the mitotic cell cycle with two distinct peaks, one early in the G1 phase and another one early in the S phase (71). Mouse oocytes take up large amounts of zinc at the latest stage of maturation and then become growth arrested after the first meiotic division (83). On fertilization, the embryos resume progression through the cell cycle and, subsequent to calcium(II) ion oscillations, release intracellular zinc(II) ions into the extracellular space in a process that has been referred to as "zinc sparks."
The second pathway involves intracellular release of zinc(II) ions from vesicles. Stimuli targeting the zinc transporter Zip7 control the release of zinc(II) ions from a store in the ER to the cytoplasm (84). The pathway involves growth factor stimulation and casein kinase 2–induced phosphorylation of Zip7, which opens the store for zinc release (85). Lysosomal release in IL-2–stimulated T cells is a required signal for proliferation (86). In macrophages, stimulation of the immunoglobulin E FcεRI receptor and extracellular signal-regulated kinase/inositol trisphosphate signaling triggers zinc release, which is preceded by Ca2+ release (87). This phenomenon has been referred to as a "zinc wave." Zinc sparks occur within seconds, whereas zinc waves take minutes to develop. Thus, zinc(II) ion signals have different frequencies.
To transmit the zinc signal to targets, close proximity between the source of zinc(II) ions and their target(s) seems to be essential. Concentrations of picomoles per liter to nanomoles per liter cellular zinc(II) ions inhibit the activities of certain enzymes, such as protein tyrosine phosphatases (88). Protein tyrosine phosphatases are not recognized as zinc proteins, mainly because they are isolated with chelating agents to preserve their enzymatic activity. Kinetic investigation of isolated protein tyrosine phosphatases and buffered zinc(II) ion solutions demonstrate that the zinc inhibition constant of the cytosolic domain of receptor protein tyrosine phosphatase β is 27 pmol/L (89). Locally, the cellular zinc(II) ion concentration could be higher than the measured steady-state amounts indicate. Some protein tyrosine phosphatases are localized at the ER where zinc release occurs. The phosphorylation of Zip7, the zinc inhibition of protein tyrosine phosphatases, and fluctuations of zinc(II) ions indicate a role of zinc in controlling phosphorylation signaling. The match between free zinc(II) ion concentrations and the inhibition of target proteins is also evident from the measurement of 24 pmol/L free zinc(II) ions in erythrocytes and an IC50 of 80 pmol/L for zinc inhibition of erythrocyte Ca2+-ATPase (58, 90). The affinities of zinc proteins for zinc and the affinities of proteins that are targeted by signaling zinc(II) ions define the lower and upper ranges in which free zinc(II) ions regulate biological processes. Thirty years ago, before the molecules and mechanisms controlling cellular zinc were known, inhibitory control, vesicular sequestration of zinc, and complementarity of zinc and calcium in cellular regulation had been given as an answer to the question: "Zinc, what is its role in biology?" (91). The cellular roles of zinc(II) ions at exquisitely low concentrations, typically reserved for hormones, are most remarkable and constitute a novel principle for cellular signaling (Fig. 2).
The micromolar per liter concentrations of MTs in most cells provide a temporary reservoir of sufficiently tightly sequestered zinc and, compared with the picomoles per liter free zinc(II) ion concentrations, relatively large amounts of zinc that are available in a deliverable form on demand. This function of MT resembles those of metallochaperones, in particular because MTs have the capacity to transfer zinc via protein-protein interactions by an associative mechanism (92). MT has affinities for zinc in exactly the range of zinc(II) ion concentrations discussed here and therefore can participate in the distribution of zinc and the termination of zinc signals. Termination of zinc signals as inferred from experiments in vitro involves thionein, the apoprotein of MT. Thionein binds zinc and activates zinc-inhibited enzymes. In vivo, thionein is likely a molecule that is neither completely devoid of nor fully loaded with metal ions. The translocation of MTs in cells and their induction by many different cellular signal transduction pathways allow changes in the cellular zinc buffering and muffling capacities. Modulating the chelating capacity of MTs through changes of either their total amount or their redox state affords ways to control the regulatory functions of zinc(II) ions (93). Elevated zinc(II) ion concentrations induce MTF-1–controlled gene transcription of thioneins, the apoproteins of MTs, and the zinc transporter ZnT1, resulting in the binding of the surplus of zinc to MTs and the export of zinc from the cell. A host of other conditions also induce the apoprotein, indicating that forms of thioneins are produced for lowering the availability of cellular zinc(II) ions, and modulating zinc-dependent processes.
In summary, four observations define a range of picomoles per liter to low nanomoles per liter concentrations at which zinc(II) ions can serve regulatory functions: 1) the free zinc(II) ion concentrations and their fluctuations, 2) the affinities of MT for zinc, 3) the affinities of zinc proteins for zinc, and 4) the zinc affinities of proteins that are targets of zinc(II) ion signals (Fig. 3).
The concentration of cellular zinc is rather high, almost as high as that of ATP. Therefore, at the cellular level, zinc can hardly be considered a trace element. Zinc is used as a cofactor in proteins much more frequently than most vitamins. The control of a fluctuating pool of zinc(II) ions at remarkably low concentrations and with the participation of many proteins provides a new perspective on the molecular functions of zinc in biology in general and for the impact of zinc on human health in particular (94). Roles of zinc(II) ions in biological phosphorylations and in redox signaling are already well documented and are part of the spectrum of actions of zinc in cellular proliferation, differentiation, and cell death. Zinc is not just required for the function of proteins; it participates in the control of cellular metabolism and paracrine and intracrine signaling (95). Not only the availability of zinc itself, but the limited cellular zinc buffering capacity and the many mutations that affect the functions of proteins involved in the cellular control of zinc have major implications for the balance between health and disease. The zinc-buffering system seems to be rather sensitive to environmental factors. Acute and long-term exposure to chemicals that interfere with zinc buffering should be a major concern for health, and so should be chelating agents that bind zinc and decrease its availability and that of other metal ions that compete with zinc, e.g., cadmium. The concentration range at which zinc(II) ions occur is critical for explaining the global functions of zinc. Zinc is generally considered to be an antioxidant. However, it is redox inert and thus can serve such a function only indirectly. The term proantioxidant is more appropriate (96). Whether zinc elicits antioxidant, anti-inflammatory, or antiapoptotic effects depends on its concentration. Outside the physiological or pharmacological range, under conditions of both zinc overload and zinc deficiency, zinc(II) ions have the opposite effect: they become pro-oxidants with proinflammatory and proapoptotic properties. This intricate balance at a relatively narrow and tightly controlled range of concentrations needs to be considered when the physiological significance of results from experiments performed with zinc are evaluated and in nutrition when supplementation with zinc is considered (97).
All authors have read and approved the final manuscript.
2Abbreviations used: ER, endoplasmic reticulum; LTA4, leukotriene A4; MT, metallothionein; MTF-1, metal-response element–binding transcription factor 1; Zip, ZRT/IRT-like protein; Zn, zinc; ZnT, zinc transporter.
PubMed Central Canada is a service of the Canadian Institutes of Health Research (CIHR) working in partnership with the National Research Council's national science library in cooperation with the National Center for Biotechnology Information at the U.S. National Library of Medicine(NCBI/NLM). It includes content provided to the PubMed Central International archive by participating publishers.


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Definition of "(I) told you (so)!" - English Dictionary
(Definition of "(I) told you (so)!" from the Cambridge Advanced Learner's Dictionary & Thesaurus © Cambridge University Press)
Get a quick, free translation!
- (I'm) pleased to meet you idiom
- I've
- (I) beg your pardon idiom
- (I) tell you what idiom
- (I) told you (so)! idiom
- I, i
- I-9 form
- i.e.
- i/c
Create and share your own word lists and quizzes for free!
Word of the Day
to believe something or have an opinion or idea


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Product Development Engineering (PDE) seeks to help clients with delicate art and science of Transforming Product Ideas into Commercial Reality. PDE helps clients to recognize innovative and ground breaking ideas and then assists in driving the processes that turn those ideas into products.
PDE brings a deep and wide wealth of practical experience in the process of creating products. We can assist in any phase of the product development process from ideation, specification development, introduction into production and many other areas. Our product knowledge is a unique mix ranging from the specialty chemical industry to flat panel monitors. The industries we have serviced are similarly diverse.
Beyond the alchemy that is needed to create products we can offer assistance in business process improvement, regulatory affairs resolution of complex manufacturing and end user issues, and general management consulting. We apply a Six Sigma tools effectively.
Our approach toward problem resolution is data driven with a focus on timely, cost effective and comprehensive solutions. In the midst of often ambiguous situations, we gather the existing facts and go where they lead adjusting our course in response to new facts. Our drive is to resolve the problem and not cling to any perceived solution.
As we have matured as an organization we have come to realize that our emphases have common themes. We help clients focus on the three critical components of any successful company:


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Executive Director Salary
The average salary for an Executive Director is $75,246 per year. Experience has a moderate effect on income for this job.
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Job Description for Executive Director
Executive directors typically act as senior managers of organizations and businesses. Their responsibilities and duties can vary depending on where these professionals work; however, most duties are universal. Executive directors help to design, develop, and implement strategic plans to help their company work in a cost- and time-efficient manner. They are also responsible for overseeing day-to-day activity for the company, as well as developing future plans.Read More...
The executive director is in some ways the leader of the organization. It is the responsibility of the director to report to the chairman of the board on a regular basis. Although the board may give suggestions on how to improve the organization, it is the sole responsibility of the director to decide if those suggestion will be implemented or not. This role requires good leadership, organization, and motivational skills. These directors are in charge of motivating their members and helping the organization develop its company philosophy. It is also the job of the director to stay on top of what is going on within the company and its staff. The executive director must also keep track of the budget, company assets, and other resources to use them to their full ability. These directors must be able to adapt to changes and know how to manager people with different backgrounds. To become an executive director one typically should obtain a college degree in a program such as accounting, marketing, finance, or information technology.
Executive Director Tasks
- Direct and track operational budget decisions to increase strategic reach and report findings to the Board of Directors.
- Establish and maintain working relationships with the press, partners, the community and clients.
- Supervise department heads and conduct performance reviews.
- Develop, maintain, expand and promote departments, services and offerings.
- Analyze operations to enhance efficiency and meet strategic goals.
Executive Director Job Listings
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peerfly USA leads needed!
- Status Closed
- Budget $8 - $15 USD / hour
- Total Bids 15
Project Description
Need someone to deal with CPA lead generation.
Hello, I am looking for someone to provide me with some email submitted leads. I will
start off small preferably 30 leads a day, with the intent of increasing the traffic. I will
using a specific URL to track your lead progress through my system. I'm looking for experienced
providers only. The emails will be submitted on my lead capture page and I will be sending auto responder
emails to the leads no more than twice a day.
Please note:
The Rules:
Only quality sign-ups
Only unique and confirmed E-mail Addresses
Only unique and confirmed IP addresses
No Rotating IP addresses
No fake Emails
No duplicates sign ups
No fraudulent sign ups
No Automated Methods
No Cookie Cleaners
No Black Hat
No use of proxy servers
No Incentivized Traffic
No Auto Bots or Software
Yes 100% Real People
Yes 100% USA/Traffic
You can drive traffic by any ethical means, PPC, Optin Mail, SEO, Social Media anything that's genuine intent basically.
$[url removed, login to view] per qualified Email submitted (no pay for bounced emails)
$[url removed, login to view] per qualified sign up on webpage (it's free )
You will get paid Via Paypal
--There Will Be NO UP FRONT PAYMENTS--Get free quotes for a project like this
Skills Required
Looking to make some money?
- Set your budget and the timeframe
- Outline your proposal
- Get paid for your work
Hire Freelancers who also bid on this project
Looking for work?
Work on projects like this and make money from home!Sign Up Now
- Forbes
- The New York Times
- Time
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- Times Online


text:
Publication Name: Aiken Journal
Location: Aiken, South Carolina
Pages Available: 2,250
Years Available: 1874 - 2002Learn More About This Publication
Aiken Journal (Newspaper) - August 1, 1874, Aiken, South Carolina VOLUME 4.—NUMBER 182 [Written for the Aiken JournalTHE HIDDEN TREASURE fir. I-;'-,- active re] the Evening Hail (new paper be) made mpid tiwe to astore matron that a than hail 4 minutesprevioualy., The oblig chat told him the man got a* pj paid for it. • ':Mm the Hog-eve man. ^ Thursday, but failed to he was oerwulj- some messages we s deeirej^ro him with to his Governor Scott, other distingagEly#^hirigM 11 og-Eyeshspecimen of u§jgmi C£**$ ;


text:
Miley Cyrus, Michael Phelps, Lindsay Lohan set for VMAs
We already knew many of the performers slated to appear at MTV's Video Music Awards -- Rihanna, Pink, Kid Rock, Paramore, Lil Wayne, the Jonas Brothers. Now we know several of the presenters who will appear inside a Paramount Pictures soundstage, including uber-Olympian Michael Phelps, tween-pop sensations Miley Cyrus and the Jonas Brothers, actress-"singers" Lindsay Lohan and Scarlett Johansson, Ciara and the casts of High School Music 3 and Twilight.
Also slated to take part are DJ AM and former Blink-182 drummer and Meet the Barkers star Travis Barker, who will mix live drums and scratched records while several guest performers -- including Katy Perry, T-Pain, Lupe Fiasco and the Ting Tings -- step to the mic to revive hits from the past quarter-century.
More presenters and performers will be announced soon, so stay tuned. Comic actor Russell Brand will host. The whole shebang will air live only once in its original, unedited incarnation -- at 9 p.m. sharp on Sept. 7.
Also in music:
- Save the Air Festival set to rock Downtown Fullerton
- More Palladium shows: Flogging Molly, Rise Against, Mudvayne
- Jay-Z to headline reopening of Hollywood Palladium
- The Black Keys keep it raw at the Mouse House
- Wener's Winners: Nada Surf, Benji Hughes, Long Beach Blues
- Radiohead conjures more magic at the Bowl
- Tom Petty sticks to his blueprint in Irvine
- What should Gwen & Gavin name their third child?
Most Popular
- Large sewage spill in Tijuana, Mexico, flows north of border
- 3-month-old baby killed in I-5 Freeway crash in Tustin
- 17-year-old killed in 22 Freeway crash identified
- Video: Mater Dei tops Chino Hills in OT thriller to reach CIF-SS final
- Officer who discharged gun during Anaheim scuffle with teenager was in fear for his life,
User Agreement
Comments are encouraged, but you must follow our Privacy Policy Policy & Terms of Use
Keep it civil and stay on topic. No profanity, vulgarity, racial slurs or personal attacks. People who harass others or joke about tragedies will be blocked. By posting your comment, you agree to allow Orange County Register Communications, Inc. the right to republish your name and comment in additional Register publications without any notification or payment.


text: 000 WGUS83 KDLH 221305 FLSDLH FLOOD STATEMENT NATIONAL WEATHER SERVICE DULUTH MN 705 AM CST WED FEB 22 2017 ...The flood warning continues for the following rivers in Minnesota... Mississippi River Near Fort Ripley affecting Crow Wing and Morrison Counties .Snowmelt water and rainfall from this past Monday will flow through streams, rivers, and tributaries through this week. The abnormally warm weather has been steadily melting snow over the past several days. This in combination with up to three quarters of an inch of rainfall from Monday will result in modest rises on the Mississippi River. Water levels have risen to minor flood stage at Fort Ripley due to ice jamming downstream and fluctuations in stage of 1 to 2 feet are possible until ice breaks up and moves out. People with interests near area streams and rivers are encouraged to monitor the latest forecast. MNC035-097-231305- /O.EXT.KDLH.FL.W.0001.170222T1301Z-000000T0000Z/ /FTRM5.1.ER.170222T1122Z.170222T1800Z.000000T0000Z.UU/ 705 AM CST WED FEB 22 2017 ...Flood Warning now in effect until further notice...The Flood Warning continues for The Mississippi River Near Fort Ripley. * At 6:30 AM Wednesday the stage was 10.2 feet. * Flood stage is 10.0 feet. * Minor flooding is occurring and Minor flooding is forecast. * Forecast...The river will continue rising to near 10.5 feet by this afternoon then begin falling. * At 11.0 feet...This will cause minor flooding of rural areas near Fort Ripley.. This crest compares to a previous crest of 10.3 feet on May 22 2015. && LAT...LON 4644 9420 4630 9420 4617 9423 4616 9440 4626 9442 $$ BJH


text:
Help find me some leads
This project received 6 bids from talented freelancers with an average bid price of $144 AUD.Get free quotes for a project like this
Project Budget$30 - $250 AUD
Total Bids6
Project Description
I run a Digital Design agency that provides services for Web Design, eCommerce and iPhone applications.
I need works to help find me leads, I'm looking at finding work through the following;
Email Marketing:
- Sourcing Gold Coast based clients requiring our services (email mining) 250 local "Gold Coast Australia" businesses.
- Copywriter for email marketing
- Creating email campaign
Facebook Fans:
- Building Facebook fan likes - please suggest ideas and quote.
- Suggest a infographic idea for a web design agency. Please provide examples quote for 1 infographic on web design.
Help me to find more leads. Please provide any tips
Skills Required
Looking to make some money?
- Set your budget and the timeframe
- Outline your proposal
- Get paid for your work
Hire Freelancers who also bid on this project
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- Forbes
- The New York Times
- Time
- Wall Street Journal
- Times Online


text:
--------- Original message --------From:
"Cathy" <firstname.lastname@example.com>To:
<email@example.com>Subject: [IRIS-PHOTOS] TB: FLORENCE
NIGHTENGALEDate: 02-10-04 18:14Sorry can't read my notes on this
one...1st bloom.1st year early April '03Michael
Yahoo! Groups
Yahoo! Groups Links
To visit your group on the web, go to:http://groups.yahoo.com/group/iris-photos/
To unsubscribe from this group, send an email to:firstname.lastname@example.com
Your use of Yahoo! Groups is subject to the Yahoo! Terms of Service.


text:
:: Commercial Aviation News
Saturday, February 25, 2017
1,201 - 1,300 out of 4,251 news
Commercial Aviation
Military Aviation
Space & Strategic
Missiles & Munitions
Guns & Air Defense Systems
Sea Power
Ground Forces
Sensors & Electronic Gear
Wednesday, June 19, 2013
HGI Capital Group Orders 10 ATR 72-600s
Singapore Airlines Firms Up Order for 30 Airbus A350-900s plus 20 Options
Oman Air Places Order for Five Boeing 737-900ERs
Travel Service Announces Commitment for Three Boeing 737 MAX 8 Jetliners
Starspeed Signs Contract for a Second AW169 Helicopter
ERA Group Signs Contract for 10 AW189 Helicopters Plus Options at the Paris Airshow
Life Link III Signs Contract For Six AW119Kx Helicopters Plus Six Options
Tuesday, June 18, 2013
Elitaliana Signs for Three More AW169 Helicopters
Kestrel Aviation Orders Two More AgustaWestland AW119 Ke Helicopters
US Corporate Operator Signs Contract For Two AW139 Helicopters
Avianca Takes Delivery of its first ATR 72-600
Undisclosed Customer Orders 12 Bombardier Global 8000 Business Jets
Conviasa Confirms the Purchase of Seven Additional E190 Jets
Zhuhai Helicopter to Acquire Four Additional S-92 Helicopters
CITIC Offshore Helicopter Company to Acquire Two S-92 Helicopters
Syphax Airlines Orders Three Airbus A320neo Jetliners
Air Lituanica Selects Embraer E-Jets
Air Costa Acquires three E-Jets
Japan Airlines Orders Four Embraer 170 Jets
Korean Air Announces Commitment for Five Boeing 747-8s and Six 777-300ERs
Alaska Air Group Orders Up to 10 Bombardier Q400 NextGen Turboprop Airliners
VistaJet Places Order for up to 40 Bombardier Challenger 350 Business Jets
Comlux Becomes First to Take Delivery of an Airbus ACJ321 Aircraft
Boeing Launches 787-10 Dreamliner with 102 Commitments
Air Lease Corporation Signs Commitment for 30 Boeing 787-10X and 3 787-9 Dreamliners
Nordic Aviation Capital Orders 30 ATR 72-600 and 5 ATR 42-600 Airplanes
easyJet Selects 100 Airbus A320neo and 35 A320ceo Airliners
First SSJ100 Delivered to Mexican Airline Interjet
Monday, June 17, 2013
ILFC Orders 50 More Airbus A320neo Family Aircraft
DORIC Lease Corp Signs MoU for 20 Airbus A380 Jetliners
Qatar Airways Announces Agreement for Nine Boeing 777-300ER Airliners
GECAS Commits to Buy 10 Boeing 787-10X Dreamliners
Air New Zealand Takes Delivery of First A320 Equipped with Sharklets
Lufthansa Orders 35 Airbus A320neos, 35 A321neos and 30 A320ceo with Sharklets
Odyssey Airlines Disclosed as Customer that Ordered 10 Bombardier CS100 Jets
SCAC and Ilyushin Finance Co Sign Agreement on 20 Sukhoi Superjet 100 Airliners
Embraer Launches Second Generation E2 Regional Jet Family
Embraer Receives Letters of Intent with Undisclosed Customers for 65 E2 Jets
ILFC Signs Letter of Intent for up to 100 Embraer E190-E2 and E195-E2 Jetliners
Large Order for up to 200 Embraer E175-E2 Jetliners Placed by SkyWest
Japan Coast Guard Buys 11 Sikorsky S-76D Helicopters
Brunei Shell Takes Delivery of Two AW139 Helicopters
OHI Group Signs Contract for Additional Two AW139 Helicopters
Samsung Techwin Co Orders Two More AW139 Helicopters
LCI Orders 3 AgustaWestland AW139, 5 AW169 and 2 AW189 Helicopters
Friday, June 14, 2013
First Airbus A350-900 Airliner Takes to the Skies on its Maiden Flight
Thursday, June 13, 2013
Cebu Pacific Takes Delivery of its First Airbus A330-300 Airliner
LIAT Takes Delivery of its First ATR-600
Friday, June 7, 2013
New Suppliers for Embraer's Second-generation E-Jets Announced
ATR -600 Aircraft Receive ETOPS 120 Minutes Certification
Thursday, June 6, 2013
ATR 72-600 Certified to Operate at Take-off and Landing Temperatures as Low as -45C
Bombardier Delivers WestJet's First Q400 NextGen Airliner
Tuesday, June 4, 2013
Aeromar Introduces First ATR 72-600 in Mexico
Bombardier Discloses Gulf Air as Customer for 10 CS100 Jets
Friday, May 31, 2013
Thomson Airways Takes Delivery of its First 787 Dreamliner
TUI Travel Group Announces Commitment for 60 Boeing 737 MAX 8 and 9 Jetliners
Thursday, May 30, 2013
Singapore Airlines Places Order for 30 Airbus A350-900s and 20 Options
Monday, May 27, 2013
National Police Agency of Japan Orders EC155, EC135 and AS365N3+ Helicopters
Wednesday, May 22, 2013
Fourth AW139 VIP To Join UK and Ireland Corporate Fleet
China's State Grid General Aviation Company Orders an Eurocopter EC225 and Two AS350 B3e Helicopters
Oman Air Places Order for Three Airbus A330-300 Airplanes
Tuesday, May 21, 2013
Embraer Executive Jets Sells Lineage 1000
SkyWest Places Order for up to 200 Embraer 175 Jetliners
Pilatus Launches PC-24 Twin-Engine Super Versatile Jet
Monday, May 20, 2013
Embraer Lineage 1000 Jet Receives Steep-Aproach Certification
Bombardier Launches Challenger 350 Business Jet
Thursday, May 16, 2013
Exclases Russia Signs Contract for Five AW139 Helicopters to be Supplied by HeliVert
Exclases Holdings Signs Contract for a Grand New Helicopter
Wednesday, May 15, 2013
Southwest Airlines Orders 30 Boeing 737 MAX 7 and Five 737-800 Jetliners
Tuesday, May 14, 2013
Turkish Airlines Orders 40 Boeing 737 MAX 8, 10 737 MAX 9 and 20 737-800 Jetliners
Monday, May 13, 2013
Boeing Delivers First Direct Purchase 767-300ER to MIAT Mongolian Airlines
Embraer Selects Suppliers of Systems for Second-generation E-Jets
Sikorsky S-76D Helicopter Achieves Certification in Mexico
Wednesday, May 8, 2013
Sikorsky Delivers First of Two S-92 Helicopters to Turkish National Police
Tuesday, May 7, 2013
WestJet Announces Commitment to Buy 10 Boeing 737-800s
Monday, May 6, 2013
THK Gokcen Aviation Orders 17 Eurocopter EC135 Helicopters
Friday, May 3, 2013
Aer Arann gets its first ATR 72-600
Monday, April 29, 2013
ATR 42-600 and 72-600 Airplanes Certified by the FAA
Nepal Airlines to Buy Two Airbus A320s
United Airlines Places Order for up to 70 Embraer 175 Jetliners
Thursday, April 25, 2013
China Aviation Supplies Holding Company to Purchase 42 Airbus A320s and 18 A330s
Eurocopter Successfully Demonstrates its EC145 Unmanned Helicopter
Monday, April 22, 2013
British Airways Signs MoU for 18 Airbus A350-1000 Jetliners
RwandAir Orders a Bombardier Q400 Aircraft
Thursday, April 18, 2013
Antonov An-158 Jetliner Enters Service with Cubana de Aviacion
Turkmenistan Airlines Takes Delivery of First of Two AW101 VVIP Helicopters
Dassault Falcon 2000S and 2000LXS Business Jets Awarded FAA Certification
Tuesday, April 16, 2013
FLYNONSTOP to Launch Operations with the Embraer 190 Jet
Monday, April 15, 2013
Embraer Executive Jets Signs Deal for Lineage 1000 in China
Beechcraft Receives Order for King Air B200 from Japanese Aviation Services Company
Wednesday, April 10, 2013
Porter Airlines Signs Purchase Agreement for up to 30 Bombardier CS100 Jets
Bell Helicopter Wins Delaware State Police Contract for Two Bell 429s
Tuesday, April 9, 2013
Turkish Airlines Commitment to Order 40 Boeing 737 MAX 8s, 10 737 MAX 9s and 20 737-800s
Monday, April 8, 2013
Embraer Sells Two Embraer 190 AR Jets to Austral Lineas Aereas
Thursday, April 4, 2013
Sberbank Leasing Places Order for 12 Boeing 737-800 Jetliners
Thursday, March 28, 2013
Embraer Executive Jets Phenom 300 Sets Three Speed Records
Nordic Aviation Capital Orders Four Bombardier Q400 NextGen Airliners
Wednesday, March 27, 2013
Dassault Falcon 2000S and 2000XLS Jets Awarded EASA Certification
Weststar Aviation Services Orders Six AW139 and Two AW189 Helicopters
PT Travira Air to Buy Two S-76D Helicopters
1,201 - 1,300 out of 4,251 news
Equipment Guides
Military Aviation
Sea Power
Ground Forces
Space & Strategic
Commercial Aviation
Guns & Air Defense Systems
Sensors & Electronic Gear
Missiles & Munitions
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Is this a seafood restaurant?
Can a vegetarian person get a good meal at this restaurant?
Is this restaurant good for large groups?
Is this a Central European restaurant?
Is this an European restaurant?
Is this a Mediterranean restaurant?
Is this restaurant good for business meetings?
Is this restaurant romantic?
Is this restaurant good for dining on a budget?
Does this restaurant offer takeout or food to go?
Thanks for helping!
ideal for casual evening in smaller groups or even with a large company. Plenty of place but during busy conference days in Fulda you may need to maker reservations. Perfect location in the inner city near the "Schloss" and the Dom.
Had lunch at this restaurant after motorcycle ride to Fulda. The food is excellent but pricey. It lies is a nice part of town centrally located. Service is a bit slow but this is typical for many German restaurants.
The service its super bad, there is no irganization with the waiters, the price quality relation of the food is not righ, its a shame that the only latin restaurant in the city its so bad. The place and music its good but its a shame that the rest is horrible, even the toilets are stinky...
Best steak in years . My thanks to the chef . Kids and wife happy to 😀
The food was good and the place was good . Everybody happy , good service .
Even if you stroll by the place, it breats something caribean. It does not say white beaches and palm trees, but more the old-colonial style cuban sort of place.
When the terras is open, it gives a cosy atmosfere, and inside the cuban style is more prominent.
There is a large menu and a long list of cocktails (I have...
I think this was the only place nearby that was open at 23:00 on a Friday evening and served food (until 03:00). Fairly large menu with many dishes and lots of different drinks.
The food we had was all excellent and very tasty - service was also really good. The place was packed and a good athmosphere. There are outside...
Excellent location and food. We tried the salmon and rumpsteak and it tastet great! Nice staff and good prices. Nice tables outside and view of the Stadtschloss. :)
The restaurant is just opposite from the Stadtschloss. Very good service, big menue, and not german foods! SOmething different in Germany.
we stopped here for lunch after arriving earlier that morning to Germany. We each ordered a pizza dinner plate size that was quite yummy with a beer. The meal was a nice value for what we got and the view of the stadtschloss was very nice and the top part of the gardens were visible to the left of the...
The service was excellent, the table pleasantly positioned, very friendly service. The food was the best I had on my visit to Fulda. Returned the next afternoon for a cocktail!
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