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If you buy property that turns out to be stolen, you may find yourself charged with receiving stolen property. In Nevada, buying or receiving stolen property is a crime that ranges in seriousness from a misdemeanor to a category B felony, depending upon the value of the stolen property received. Below, review the definition and elements, the potential penalties, and common defenses for this crime.
NRS 205.275 defines the crime of receiving or buying stolen property. According to this statute, it is a crime to buy, receive, or possess stolen property for personal gain. It is also a crime to withhold property to prevent the original owner from again possessing his property.
A person can only be convicted of receiving stolen property if he knows or reasonably should know that the property is stolen. In other words, a person is guilty of this offense if he has actual knowledge that the property is stolen or if he receives the property under circumstances which would cause a reasonable person to know the property was stolen.
By statute, possession of three or more of the same or similar items with removed serial numbers is "is prima facie evidence" that a person has knowingly received stolen property. This means that possession of three or more items with destroyed serial numbers is enough for a conviction, although the jury or judge may still acquit if there is reasonable doubt.
There are many other facts which may be relevant in determining whether the accused should have known the property in question was stolen. For instance, if the defendant bought the property for far less than market value, that might indicate that the buyer should have known the property was stolen.
Here is an example to illustrate how certain facts may indicate that a person should know property is stolen. You compliment an acquaintance on a Rolex watch he is wearing. He offers to sell you the watch for a few hundred dollars and you accept. The fair market value of the watch is several thousand dollars. The watch has an engraving on the back with a name of a person other than your acquaintance. You sell the watch to a pawn shop. It turns out the watch is stolen, and you find yourself charged with receiving stolen property. Although you had no actual knowledge that the watch was stolen, the prosecutor will likely argue that the circumstances under which you bought the watch indicate that you should have known it was stolen. In particular, the prosecution will argue that you should have known the watch was stolen based on the seller's below-market-value asking price and the engraving. Of course, there are responses to these arguments and ways to defend a charge like this.
The potential penalty for receiving stolen property varies from a misdemeanor to a category B felony, depending upon the value of the stolen property. Specifically, if the value of the property is less than $650, the crime is a misdemeanor punishable by up to 6 months in county jail and/or a $1,000 fine. If the value of the property is $650 or more but less than $3,500, the crime is a category C felony punishable by 1 to 5 years in Nevada state prison and a fine of up to $10,000. Finally, if the value of the property is $3,500 or more, the crime is a category B felony punishable by 1 to 10 years in Nevada state prison and a fine of up to $10,000.
How is the value of the property established for the purpose of determining whether this crime is a misdemeanor or a felony? According to NRS 205.275(6), the value of the property is "the highest value attributable to the property by any reasonable standard." In other words, under Nevada law, the prosecutor is allowed to seek the highest possible punishment by attributing the highest value possible to the stolen property, so long as the valuation is arguably "reasonable."
In addition to incarceration and fines, restitution is mandatory for a conviction of for receiving stolen property. Restitution means that the person convicted of this crime will be ordered to repay the original owner for the value of the property lost. If the property is recovered, restitution will consist of any damage (i.e. loss in value) to the property, if any.
As explained above, receiving stolen property is a serious offense, and a conviction can result in substantial criminal penalties, including incarceration. Since the prosecutor must prove all elements of the charged crimes beyond a reasonable doubt, a successful defense will attack one or more of the elements of the crime. This can include an argument that the accused did not know and did not have any reason to know that the property was stolen. Another potential defense argument is that the accused did not actually possess the alleged stolen property. A defense attorney may also argue that the police committed certain constitutional violations while investigating the alleged crime, and that any potential evidence should be suppressed.
Even when the prosecution has substantial evidence of guilt, a criminal defense attorney will often be able to negotiate a favorable deal and avoid fines and incarceration.
I have successfully represented many individuals accused of buying and receiving stolen property in Las Vegas and throughout Clark County, Nevada. So if you have been charged with this or any other crime, call me immediately for a free consultation.


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Insulin binding and activation of the insulin receptor
The insulin receptor (IR) is a large, disulphide-linked, glycoprotein that spans the cell membrane with its insulin binding surfaces on the outside of the cell and its tyrosine kinase domains on the inside. IR is a symmetrical homodimer that contains two identical binding pockets, each created by the juxtapositioning of two distinct binding sites involving residues from both IR monomers (IR and IR´). The two binding pockets comprise site 1/site 2´ on one side of IR and site 1´ and site 2 on the opposite side. The current model for IR activation is that two distinct surfaces of insulin engage sequentially with either the site 1/site 2´ binding pocket or the site 1´/site 2 pocket. The formation of a site 1 – insulin - site 2 high-affinity, cross-link involves structural changes in both insulin and IR resulting in the activation of the intracellular tyrosine kinase and the initiation of the phosphorylation cascades that drive insulin signaling. Understanding how insulin binding induces signal transduction requires structures of: (i) insulin and IR in their basal states, (ii) insulin bound to the IR ectodomain, (iii) the activated IR kinase domain and (iv) the domain rearrangements associated with the formation of the high affinity insulin/IR complex that initiates activation of the intracellular kinase.
The structure of unbound insulin
Mature insulin consists of two polypeptide chains (A and B) held together by disulphide bonds. The processes involved in insulin biosynthesis were elucidated by Donald Steiner and colleagues beginning in the late 1960s[1]. They showed that insulin was synthesized as a single chain molecule, proinsulin, with the B-chain at its N-terminus, the A-chain at its C-terminus and a 35 residue connecting segment, the C-peptide, in the middle (Figure 1). The mature two chain molecule is generated from proinsulin by two subtilisin-like convertases that carry out the proteolytic removal of the C-peptide[1].
Figure 1. Sequence of human insulin precursor. The B- and A-chain segments of the processed protein are shown in cyan and light brown color, respectively, with the proteolytically removed C-peptide in gray. Disulfide bonds are indicated in green, while residues adopting a helical conformation in the mature protein are circled in black. (Click to enlarge)The primary chemical structure of mature insulin was determined by Frederick Sanger and colleagues at Cambridge University in the early 1950s[2]. Insulin was the first protein to have its sequence determined and Sanger was awarded his first Nobel Prize in Chemistry in 1958 for this achievement. The pioneering study showed that the human insulin B-chain consisted of 30 amino acids and the A-chain of 21 amino acids, with the B- and A-chains held together by two disulfide bonds CysB7 to CysA7 and CysB19 to CysA20, with a third intra-chain disulfide bond linking CysA6 to CysA11[2].
Figure 2. Insulin structure. (A) Tertiary structure of the porcine insulin monomer in its 2 Zn rhombohedral form [PDB entry 4INS]. (B) Structure of the human insulin mutant GlyB24 [PDB entry 1HIT], showing the flexibility of the B-chain C-terminus. For clarity, disulfide bonds are omitted in (B).
The crystal structure of porcine insulin was first reportded by Dorothy Hodgkin (née Crowfoot) and colleagues in 1969 as the 2Zn2+-stabilized hexamer at 2.8 Å resolution[3]. At the same time, and in isolation during the Cultural Revolution in China, the so-called "Beijing Insulin Structure Group" was also working to determine the structure of insulin and published their findings in 1972. The data revealed that the insulin monomer consists of a two-layered sandwich with the B-chain overlaying the A-chain. The B-chain consists of an N-terminal segment (residues B1–B6), a type II β-turn (B7–B10) a central α-helix (B9–B19), a type I β-turn (B20–B23), and a C-terminal β-strand (B24–B28), followed by residues B29 and B30, which are less well ordered (Figure 2). The A-chain consists of an N-terminal α-helix (A1–A8), a non-canonical turn (A9–A11), a second α-helix (A12–A18), and a C-terminal segment (A19–A21).
It is now recognized that human insulin is part of a larger family of sequence-related hormones that comprises insulin, the insulin-like growth factors IGF-I and IGF-II, the relaxin peptides relaxin-1, -2, and -3 and the insulin-like peptides INSL3, INSL4, INSL5, and INSL6[4]. The two IGFs each contain a single polypeptide chain, while each of the remaining members of the family contains a pair of chains resulting from the proteolytic processing of a single-chain precursor. Three-dimensional structures have been determined for these other family members and, as expected from their close sequence relationship, all have the same three-helix tertiary structure and the same disulfide-bonding pattern that was determined originally for human insulin[4].
Receptor binding surfaces of insulin
Extensive biochemical and structural characterization of the hormone over decades has demonstrated that the surfaces of insulin that bind IR sites 1 and 2 comprise residues predominantly drawn from the insulin dimerization (site 1) and hexamerization (site 2) surfaces[5][6][7]. These surfaces have both been shown to have closely related counterparts in the insulinlike growth factors (IGFs) IGF-I and IGF-II[8][9].
The structure of the insulin receptor dimer in its basal state
Figure 3. Cartoon of the insulin receptor dimer showing the distribution of domains across the α- and β-chains and the location of the α-β disulphide bonds linking the two chains in each monomer and the two α-α disulphide bonds linking the two monomers in the IR dimer. As discussed in the section Insulin receptor and insulin action the insulin receptor (IR) is a disulphide-linked homodimer with each IR monomer composed of several structural modules commonly found in other proteins. As summarized in Figure 3 these are (from the N-terminus to C-terminus): a leucine-rich repeat domain (L1), a cysteine-rich region (CR), a second leucine-rich repeat domain (L2), and three fibronectin type III domains (FnIII-1, FnIII-2, and FnIII-3), with FnIII-2 containing a large (~120 residues) insert domain (ID). The ID contains the furin cleavage site that yields the α-chain and β-chain of the mature receptor monomer. The intra-cellular C-terminal region of the IR monomer contains the tyrosine kinase catalytic domain, which is flanked by two regulatory regions - the juxtamembrane region and the C-tail.
The structure of the extracellular portion of the human IR (approximately 1800 amino acids) was reported by Colin Ward, Mike Lawrence and colleagues in a landmark paper in Nature in 2006[10] and represented a major milestone in insulin research. As shown in Figure 4 the structure revealed that the IR adopted a folded-over (inverted "V") conformation that placed putative ligand binding regions in close juxtaposition. One leg of each monomer consists of the L1–CR–L2 modules. The other leg of each monomer comprises the FnIII-1, FnIII-2, and FnIII-3 domains in an extended, linear arrangement. FnIII-2 contains the ID as an extended loop between the C and C´ strands of FnIII-2[10].
Figure 4. Structure of the IR before insulin binding. Click to enlarge figure. (A) Three-dimensional crystal structure of the IR ectodomain, showing the inverted "V" conformation with respect to the membrane. The background monomer is shown in molecular surface representation (beige) and the foreground monomer in secondary structure schematic representation (gray) with the constituent domains labeled. The disordered portions of the α-chain components of the insert domain are shown as dashed and their conformation shown here is speculative, with the approximate location of the inter-chain disulfide being indicated by a black line. The relative location of the components that make up the insulin binding site within one leg of the inverted "V" are highlighted and include the surface of the central β-sheet of the L1 domain of one monomer (purple), residues at the junction of FnIII-1 and FnIII-2 domains of the adjacent monomer (light green) and the helix formed by the C-terminal segment of α-chain (brown coil). (B) Detail of the conformation of the αCT segment on the surface the central β-sheet of the L1 domain in the crystal structure of the apo-form of the insulin receptor ectodomain. The figure is based on PDB entry 3LOH; (B) is from Smith et al[11], used by permission. (click to enlarge)The IR homodimer has a two-fold rotation axis that places the L2 domains of each monomer in contact with the FnIII-1 domain of the alternate monomer at the apex of the inverted "V" and places the L1 domains of the each monomer in contact with the FnIII-2 domains of the alternate monomer around the midpoint of the legs of the inverted "V" (Figure 4). At the base of the structure, the C-termini of the two FnIII-3 domains are poised to extend through the cell membrane to the intra-cellular juxtamembrane, kinase, and C-tail domains of the intact receptor. The FnIII-1 and FnIII-2 domains contain unusually large loops between their C and C´ strands[10]. In the FnIII-1 domains, the large CC′ loop enables formation of the Cys524–Cys524 dimer disulfide bond, while in the FnIII-2 domains an entire ID segment is contained within their respective CC′ loops. The single α−β disulfide bond between Cys647 (near the start of the ID) and Cys860 (at the beginning of the C′E loop of FnIII-3) is visible in the structure. The Cys524 α–α disulfide bond lies in a very weakly ordered region of the polypeptide, whereas the α–α disulfide bond(s) involving Cys862, Cys863, and Cys865 lies in a region of the ID (residues 655–755) that is entirely disordered in the crystal[10].
In a further refinement of the IR structure[11] residues 693 710 from the C terminal region of the IR α chain, the so called "αCT" segment, were shown to be lying across the central β sheet of each L1 domain. This αCT segment is essential for insulin binding and is known from chemical cross-linking to lie in close proximity to the L1 domain. The key features of the interaction of the 693–710 segment with the surface of the central β-sheet of the L1 domain are shown in Figure 4B. In particular, (i) the side chains of residues Phe701 and Phe705 are packed adjacent to each other in a hydrophobic pocket formed by the side chains of the L1 domain residues Leu62, Phe64, Phe88, Phe89, Tyr91, Val94, Phe96, and Arg118 - these two aromatic residues are conserved in type in IGF-1R (as Tyr688 and Phe692, respectively); (ii) the side chain of Tyr708 is packed approximately parallel to the strands of the L1 central β-sheet, in proximity to the side chains of Arg14, Gln34, Leu36, and Phe88 – again this residue is conserved in type in IGF-1R (as Phe695); (iii) the side chains of the αCT residue pair Glu698/Arg702 lie close to each other and interact with the side chains of the L1 domain residue pair Arg118/Glu120 respectively, with the four side chains forming a charge-compensating cluster; and (iv) the side chain of Leu709 is in hydrophobic interaction with the side chains of Leu37 and Phe64[11].
A remaining feature of interest is the fact that the αCT segment associated with each L1 domain in the IR dimer is contributed by the alternate monomer to that which contributes the L1 domain. This was first predicted[12] based on (i) the relative locations of the αCT segment and residue 755 from the C-terminal end of the ID and (ii) the knowledge that in the uncleaved pro-receptor, the αCT segment of one monomer would lie across the L1 domain of its partner since, proteolytic cleavage of IR into α and β chains occurs after dimer assembly. This trans arrangement of L1 and αCT has since been confirmed experimentally by complementation analysis and direct chemical crosslinking[11]. The observed association of the L1-β2 sheet and the αCT segment as a tandem structural element thus provides the first view of IR site 1 in its insulin-free form.
Insulin binding surfaces of the insulin receptor
The current model for insulin binding[7][13][14] proposes that each monomer in the IR dimer contains two different binding sites, referred to as site 1 and site 2, located on two different regions of the IR monomer. Binding of insulin to the low-affinity site (site 1) on either of the α-subunits is followed by a second binding event between the bound insulin and the second site (site 2) of the other IR α-subunit . Negative co-operativity occurs because high-affinity binding can only occur between the pair of sites (sites 1 and 2') on one side of the IR dimer or the corresponding pair of sites (sites 1' and 2) on the alternate side, i.e. the ligand/receptor bridging can oscillate from one side of the receptor dimer to the other. Two insulin molecules cannot bridge both site 1-site 2' and site 1'-site 2 pairs simultaneously[12][13].
The 3D structure of the IR dimer (Figure 4) is consistent with the model of insulin binding described above and allows a description of sites 1 and 2 to be made. Site 1 corresponds to the low-affinity site which controls ligand-binding specificity seen in soluble ectodomain constructs and binds residues predominantly from the surface of insulin involved in the formation of insulin dimers. Site 1 includes contributions from several distinct regions of the receptor: the L1β2 surface; the αCT peptide; and in the case of IGF binding, the CR region. The importance of the L1, αCT and CR regions in low-affinity ligand-binding comes from studies of receptors from patients with defective insulin signalling, site-directed mutagenesis, chimeric receptors and chemical cross-linking (reviewed in refs [13] and [15]). Only the L1 and CR domains are important determinants of ligand specificity because swapping the regions that contain the last 16 residues (CT) of the α-chain in IR/IGF1R whole-receptor chimeras[16] or mini-receptors[17] has little effect on ligand-binding. The L1 and CR domains contain the regions of greatest difference when the L1-CR-L2 structures of IR and IGF-1R are compared[18]. These are in the L1 domains around Phe39/Ser35 (IR/IGF-1R numbering) and in module 6 of the CR region where there is no sequence identity between the two receptors and very different electrostatic surface potential[18].
This alignment of the L1/αCT Site1 against the FNIII-1 and FNIII-2 modules of the monomer not contributing the L1 domain, suggests that the second binding site on IR (site 2´) that interacts with the hexamer surface of insulin corresponds to one or more of the loops at the junction of the FnIII-1 and FNIII-2 domains. Evidence supporting the requirement of this region for high-affinity binding comes from: (i) alanine scanning mutagenesis which reveals a reduction in insulin binding affinity upon individual mutation of residues Lys484, Leu552, and Asp591 (from the FnIII-1 domain) and residues Ile602, Lys616, Asp620, and Pro621 (from the FnIII-2 domain)[19]; (ii) a bioinformatic analysis, which reveals a conserved patch of residues in the vicinity of the FnIII-1/FnIII- 2 junction[20] and (iii) studies of whole IR/IGF-1R chimeras[16] and IR/IGF-1R hybrid receptors[21], which indicate that high-affinity insulin-binding requires insulin-specific components within the region 326-524 on the alternate receptor monomer to that providing the L1 domain.
The structure of the tyrosine kinase domain in its basal state
The crystal structure of the human IR tyrosine kinase (TK) domain in its unphosphorylated (basal) state was reported[22] by Stevan Hubbard and colleagues in 1994. This was the first structure of a tyrosine kinase to be reported, though the structure of a serine kinase (cAMP protein kinase) had been reported earlier. Like the serine kinases, the IR TK is composed of two lobes with a single connection between them (Figure 5A). The N-terminal lobe comprises a twisted β-sheet of five anti-parallel β-strands (β1–β5) and one α-helix (αC). The larger C-terminal lobe comprises eight α-helices (αD, αE, αEF, αF, αG, αH, αI, αJ) and four β-strands (β7, β8, β10, β11). The human IR TK lacks β-strands β6 and β9 present in cAMP protein kinase.
Figure 5. Three-dimensional crystal structure of the insulin receptor tyrosine kinase domain. (A) Inactive form, showing the secondary structure of the N- and C-terminal domains. (B) Interaction between the juxtamembrane residues 978–988 (red tube) and the N-terminal domain of the IR tyrosine kinase in its basal state (transparent pink surface); [PDB entry 1P14]. The N-C direction of the juxtamembrane segment (in red, panel B) is indicated by the red arrow. The image in panel B has been rotated 180° around the Y axis and 90° around the X axis relative to panel A. (Click to enlarge)In the inactivated IR TK, one of the three tyrosines in the activation loop, Tyr1162 (IR-B numbering), is bound in the active site but cannot be phosphorylated (in cis) because part of the A-loop interferes with the ATP binding site and the catalytic residue Asp1150 is improperly positioned to co-ordinate MgATP[22]. Upon activation (see later), auto-phosphorylation of residues Tyr1162, Tyr1158, and Tyr1163 occurs in trans by the kinase domain of the second monomer. Thus, in the basal state, Tyr1162 competes with the neighboring β-chain and other protein substrates for binding to the active site, but is not cis-phosphorylated because of steric constraints that prevent simultaneous binding of Tyr1162 and MgATP.
In 2003 Hubbard's group described the structure[23] of an extended IR kinase construct showing the molecular details of the interaction between the catalytic domain and the juxtamembrane region (Figure 5B). In IR, the proximal juxtamembrane regions show TK inhibition through the highly conserved residue Tyr984 (IR-B numbering, equivalent to Tyr972 in IR-A). This tyrosine residue interacts with several conserved residues in the N-terminal lobe of the IR kinase domain, stabilizing a non-productive position of the αC helix[23]. This juxtamembrane inhibition in IR is more significant than that contributed by the activation loop since, in the full-length IR found on cells, mutation of Tyr984 to Ala increases the basal phosphorylation state 30-fold, 10 times greater than the three-fold increase seen following mutation of the activation loop residue Tyr1162 to Asp[23].
The direction of the juxtamembrane segment relative to the lobes of the catalytic domain (Figure 5B) implies that, in the basal state, the catalytic domain is partially wrapped up and held inverted with respect to the cell membrane rather than be exposed and suspended from the end of the 41-residue (~140 Å) strand of juxtamembrane polypeptide (see Insulin receptor and insulin action Figure 4). We suggest that ligand binding results in an as yet unknown domain re-arrangement within the ectodomain that in turn affects the juxtamembrane/catalytic domain interaction, resulting in the release of the sequestered kinase domains and their subsequent transphosphorylation.
The structure of the insulin/insulin receptor complex
The complex with the major binding site - Site1 - In 2013 the Lawrence/Ward group described, for the first time, the structure of insulin bound to Site1, the major binding site on IR[24], composed of the central β sheet of the L1 domain and αCT. The result (Figure 6) was surprising. Firstly the direct interaction of insulin with the L1 domain of IR is seen to be sparse, the hormone instead engaging predominantly with the αCT segment of the site 1 tandem element. Secondly, the αCT segment is, with respect to its apo-IR counterpart, both displaced on the surface of the L1 β2 sheet, C-terminally extended to include residues 711-715 and N-terminally disordered (residues 697-704).
Figure 6
Figure 6. Structure of the insulin / IR site 1 complex. (a) Both IR monomers are shown in secondary structure schematic representation with the constituent domains labeled. The location of the disordered portions of the α-chain components of the insert domain (ID) shown here is speculative. The relative location of the components that make up the insulin binding site within one leg of the inverted "V" is circled and includes the surface of the central β-sheet of the L1 domain of one monomer (cyan), residues at the junction of FnIII-1 and FnIII-2 domains of the adjacent monomer (bright and dull green) and the helix formed by the C-terminal segment of α-chain (magenta coil). (b) Detail of the insulin - αCT – L1 domain complex (site 1 complex) based on PDB entry 4OGA. It is equivalent to the circled region on the left hand side of panel (a) viewed from the front. The directions of the respective polypeptide chains of insulin and the αCT segment are indicated by the positioning of a small blue sphere at the N-terminus of each chain and a small red sphere at each C-terminus. (c) As in panel (b) viewed from the top looking down the barrel of the L1 domain β-helix.
The αCT helix occupies volume that would otherwise contain insulin residues B26-B30 if the latter retained their receptor-free (storage-form) conformation (Figures 6b and 7). This observation confirms the so-called detachment model of insulin binding in which the C-terminal region of the B-chain displaces to expose the mostly hydrophobic core of the hormone[25][26]. The detachment model arose originally from a number of observations, including (a) that the single chain B29-A1 peptide linked insulin molecule is completely devoid of biological activity despite retaining the same crystal structure as that of wild type insulin, (b) that the B chain C terminal region (residues B20-B30) of the active PheB24Gly human insulin mutant is detected to be disordered in solution, and (c) that the structure of the insulin ValA3Leu clinical mutant, which exhibits a 500-fold reduction in insulin affinity relative to wild-type, has a structure identical to that of the native hormone and within which the side chain of the variant residue remains buried.
The two most critical hormone-engaging residues in the αCT segment are: (i) His710, which inserts into a pocket formed by invariant insulin residues ValA3, GlyB8, SerB9 and ValB12; and (ii) Phe714, which occupies a hydrophobic crevice formed by invariant insulin residues GlyA1, IleA2, TyrA19, LeuB11, ValB12 and LeuB15[24].
Frustratingly the insulin B chain C terminal segment that includes residues known to be important in insulin binding (GlyB23, PheB24 and PheB25), was unresolved in the initial insulin/IR site 1 complexes[24]. It is predicted to lie between the αCT segment and the proximal CR domain since different photo-probes attached to insulin LysB29 can label either CR or L1[4]. In addition, such a location must be the case for their counterparts in the single-chain molecules pro-insulin and the IGFs upon their binding to IR or IGF-1R. Further analysis of new data resolved this issue[26]. The results showed that on binding to site 1, the B-chain C-terminal segment detaches from the hormone core by undergoing two rotations that result in its repositioning between αCT and L1 (Figure 6b). The first is rotation of B20-B27 by ~ 10° about B20 and the second a further rotation of B20-B27 by ~ 50° about B24[26]. Although the first rotation effects maximal displacement at PheB24, the latter side chain undergoes a compensating rotameric change preserving contacts with the B-chain helix. The second rotation
Figure 7. Structural changes in insulin on receptor binding. (a) Structure of insulin in its storage form. (b) structure of insulin when bound to IR site 1. (c) an overlay of the two structures. The directions of the A and B polypeptide chains of insulin are indicated by the positioning of a small blue sphere at the N-terminus of each chain and a small red sphere at each C-terminus. positions B25–B27 anti-parallel to the first strand of L1–β2 and nearly perpendicular to the B-chain α-helix (Figure 6b). This series of conformational changes couples detachment of the insulin B-chain C-terminal strand with insertion of the αCT helix (residues 705–714) into the volume occupied by residues B25–B30 in the free hormone[24]. The salient feature of the B24–B27 segment in the IR complex is its alternating pattern of side-chain contacts with L1 and αCT: PheB24 and TyrB26 are primarily directed toward L1 whereas PheB25, and ThrB27 toward αCT. Such alternation was foreshadowed by photo–cross-linking studies of the insulin-holoreceptor complex[27]. A comparison of insulin in its closed (storage form) and open (receptor engaged form) is provided in Figure 7.
The refined structure[26] also provided data for the location of the last four residues (716-719) of the IR α-chain that were disordered in the initial structure[10]. Residues 716–719 are found to be directed away from L1 in an irregular conformation (Figure 6b). Although detailed conformations are uncertain, it is clear that the displaced B24–B26 segment inserts between the first strand of the L1–β2 sheet and αCT residues 715–718 (Figure 6b); contacts with PheB25 (above) stabilize residues 716–719.
In conclusion, the insulin/IR site 1 complex structures provide an explanation for a vast body of biochemical data relating to the insulin/IR interaction and reveal how insulin switches between a closed, stable 'storage form' and an open 'receptor activating' form[25][26]. Opening of this hinge enables conserved nonpolar side chains (IleA2, ValA3, ValB12, PheB24, and PheB25) to engage the receptor. Restraining the hinge by nonstandard mutagenesis preserves native folding but blocks receptor binding, whereas its engineered opening maintains activity at the price of protein instability and nonnative aggregation. These findings rationalize properties of clinical mutations in the insulin family and provide a novel foundation for designing therapeutic analogs[26].
The structure of the high affinity site 1-Site 2´ complex with insulin- To date no structure is available of insulin cross-linking both IR binding sites, Sites 1 and Site 2´. Nevertheless, the site 1 complexed structures described above support the view[4][24] that Site 2 most likely lies at the junction of the FnIII-1 and FnIII-2 domains of the IR monomer opposite to that providing the L1 domain to site 1. The structural re-arrangements associated with high affinity insulin binding and activation of the IR tyrosine kinase remain to be established. The existing structural data have highlighted four sites of inter-domain flexibility within IR, notably at the CR-L2, L2-FnIII-1, FnIII-1-FnIII-2 and FnIII-2-FnIII-3 junctions[28]. These would permit the receptor increased capacity to access conformations required for signal induction. The evidence comparing limited versus more extensive domain movements in IR activation following on ligand binding is discussed by Ward et al.[28].
The structure of the activated IR tyrosine kinase
Figure 8. Overlay of the inactive (blue, PDB entry 1IRK) and activated (orange, PDB entry 1IR3) forms of the domain, showing the displacement from the catalytic site of the activation loop (residues 1149–1170, highlighted as a thicker ribbon within each form) and the concomitant domain rotation which are observed upon activation. (Click to enlarge)The structure of the activated phosphorylated IR kinase in complex with a peptide substrate was reported by Stevan Hubbard in 1997[29]. It revealed that auto-phosphorylation of the three tyrosines in the A-loop leads to a dramatic change in its configuration. In the phosphorylated state, the A-loop is displaced by approximately 30 Å, resulting in unrestricted access to the binding site for MgATP and protein substrates. This movement facilitates a functional spatial arrangement of Lys1030 and Glu1047 (IR-B numbering), the residues involved in MgATP coordination, and of Asp1150, which is part of the highly conserved Asp–Phe–Gly triad. The A-loop rearrangement also leads to closure of the N and C-terminal lobes, which is necessary for productive ATP binding[29]. This closure involves significant rotation of the N-terminal lobe (Figure 8).
As discussed earlier, the major inhibition of the kinase domain is by Tyr984 (IR-B numbering) in the juxtamembrane segment[23]. Its interaction with, and inhibition of, the kinase domain would be significantly affected by phosphorylation. The precise way in which insulin binding to the extracellular domains of the IR induces domain re-arrangements that break these intracellular associations and result in kinase activation are not known.
Concluding Remarks
As summarized above there are now structures available for: (a) insulin in its receptor-free form, (b) IR ectodomain in its hormone-free form, (c) the tyrosine kinase domain in its inactive conformation, (d) insulin bound to IR site 1, and (e) the tyrosine kinase domain in its active (phosphorylated) conformation. What remain to be elucidated are the structure of the high-affinity complex wherein insulin cross-links receptor sites 1 and 2′ and induces changes in the relative positions of the subdomains of the extracellular portion of the IR dimer as well as the details on how these ectodomain rearrangements affect the trans-membrane and cytoplasmic regions of the receptor resulting in kinase activation and the initiation of signal transduction. The transmembrane segment of IR (residues 918-940, IR-A numbering) has been analysed in micelles by NMR and the region from Leu923 to Tyr937 shown to adopt a well-defined helical structure with a kink formed by Gly921-Pro922 at the N-terminus[30]. Cross-linking studies suggested that it may form dimers or oligomers under micelle conditions[30]. The idea that in the basal state the TM regions of the IR dimer are themselves in contact is supported by the demonstration that IR can be activated by an exogenously supplied 24 residue peptide (Lys 917-Arg943) containing the complete transmembrane segment[31]. This implies that ligand-induced activation of the IR involves separation of the interacting TM regions of the IR dimer. How the force is generated to pull these interacting segments apart on insulin binding remains to be established.
^ Steiner DE, Adventures with insulin in the Islets of Langerhans. J Biol Chem 2011; 286:17399-421.
^ Ward CW, Lawrence MC, Landmarks in insulin research. Frontiers in Endocrinol 2011; 2: article 76, pp 1-11.
^ Adams MJ et al., Structure of rhombohedral 2 zinc insulin crystals. Nature 1969; 224:491–5.
^ Ward CW et al., Ligand-induced activation of the insulin receptor: a multi-step process involving structural changes in both ligand and the receptor. Bioessays 2009; 31:422-34.
^ De Meyts P, Insulin and its receptor: structure, function and evolution. BioEssays 2004; 26:1351–62.
^ Glendorf T et al. 2008. Importance of the solvent-exposed residues of the insulin B chain a-helix for receptor binding. Biochemistry 2008; 47:4743–51.
^ Schäffer L, A model for insulin binding to the insulin receptor. Eur J Biochem 1994; 221:1127–32.
^ Gauguin L et al. 2008. Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I. J Biol Chem 2008; 283:20821–9.
^ Alvino CL et al. 2009. A novel approach to identify two distinct receptor binding surfaces of insulin-like growth factor II. J Biol Chem 2009; 284:7656–64.
^ McKern NM et al., Structure of the insulin receptor ectodomain reveals a folded-over conformation. Nature 2006; 443:218–21.
^ Smith BJ et al., Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for design of peptide agonists. Proc Natl Acad Sci USA 2010; 107:6771–6.
^ Ward CW et al., The insulin and EGF receptor structures: new insights into ligand-induced receptor activation. Trends Biochem. Sci. 2007; 32:129–37.
^ De Meyts P, Insulin and its receptor: structure, function and evolution. Bioessays 2004; 26:1351–62.
^ De Meyts , The structural basis of insulin and IGF-1 receptor binding and negative co-operativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia 1994; 37 (Suppl. 2), S135–S148.
^ Whittaker J et al, Comparison of the functional insulin binding epitopes of the A and B isoforms of the insulin receptor. J Biol Chem 2002; 277:47380–84.
^ Schumacher R et al, Signaling-competent receptor chimeras allow mapping of major insulin receptor binding domain determinants. J Biol Chem 1993; 268:1087–94.
^ Kristensen C et al, Specificity of insulin and insulin-like growth factor I receptors investigated using chimeric mini-receptors. Role of C-terminal of receptor α-subunit. J Biol Chem 1999; 274:37351–56.
^ Lou M-Z et al, Crystal structure of the first three domains of the human insulin receptor: comparison with the insulin-like growth factor receptor. Proc Natl Acad Sci USA 2006; 103:12429–34.
^ Whittaker L et al, High-affinity insulin binding: Insulin interacts with two receptor ligand binding sites. Biochemistry 2008; 47:12900–9.
^ Rentería ME et al, A comparative structural bioinformatics analysis of the insulin receptor family ectodomain based on phylogenetic information. PLoS One 2008; 3:e3667.
^ Benyoucef S et al, Characterization of insulin/IGF hybrid receptors: contributions of the insulin receptor L2 and Fn1 domains and the alternatively spliced exon 11 sequence to ligand binding and receptor activation. Biochem J 2007; 403:603–13.
^ Hubbard SR et al., Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 1994; 372:746–54
^ Li S et al., Structural and biochemical evidence for an autoinhibitory role for tyrosine 984 in the juxtamembrane region of the insulin receptor. J Biol Chem 2003; 278:26007–14.
^ Menting JG et al., How insulin engages its primary binding site on the insulin receptor. Nature 2013; 493:241-5.
^ Hua QX et al., Receptor binding redefined by a structural switch in a mutant human insulin. Nature 1991; 354:238-41.
^ Menting et al., A protective hinge in insulin opens to enable its receptor engagement. Proc Natl Acad Sci USA 2014; In press.
^ Xu B, et al., Decoding the cryptic active conformation of a protein by synthetic photoscanning: Insulin inserts a detachable arm between receptor domains. J Biol Chem 2009; 284:14597–608.
^ Ward CW et al., The insulin receptor changes conformation in unforeseen ways on ligand binding: Sharpening the picture of insulin receptor activation. Bioessays 2013; 35:945-54.
^ Hubbard SR, Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J 1997; 16:5572–81.
^ Li Q et al., Solution structure of the transmembrane domain of the insulin receptor in detergent micelles. Biochim Biophys Acta 2014; 1838:1313-21.
^ Lee J et al., Insulin receptor activation with transmembrane domain ligands. J Biol Chem 2014; 289:19769-77.


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Located at Broadway and 30th Street in Oakland's new hottest district, Broadway-Valdez, the mixed-use multifamily and retail development will be the lifestyle retail and dining destination for all surrounding East Bay communities.
Featuring 1,480-8,320 Sq. Ft. of retail and restaurant space, including new prominent storefronts with persevered and restored facades, and setback residential tower.
3000 Broadway's daytime population consists of a total of 305,742, making up from the many professionals of the medical campuses of Kaiser Permanente and Summit/Alta Bates as well as local residents. The population within three miles is 269,249, with an average household income of $100,000.
Within walking distance to Downtown, BART and minutes from Oakland's popular First Fridays.
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Today we are introducing a new weekly series entitled 4 Downs with...Each installment will feature a short interview with a Crusader coach or player to track the 2007 from an insider's point of view. SID Rhett Burns recently caught up with head coach Mike Taylor...
First Down: Describe the intensity of the opening week of practice.
"I think we have been practicing with high energy. Our older players have come back in good condition, so we are able to do some things we haven't benn able to do the last few years."
Second Down: How is your offensive and defensive installation schedule progressing?
"We are on schedule. We aren't quite as far along as I would like, but we are certainly doing well."
Third Down: Have any injuries set you back during the preseason?
"We have three or four freshmen who are struggling with some aches and pains, but have had no major injuries."
Fourth Down: Have their been any suprises in the opening week?
"No, not really. It will be interesting to see how they play in full contact tomorrow afternoon. Our returners have come back in great condition. We have some young running backs and linebackers who are looking good and can help us."


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Top Car Accident Lawyer in Vintage Oaks South of Seminary Menlo Park California
Many individuals in Vintage Oaks South of Seminary Menlo Park California decide to employ an accident lawyer after they've been involved in a car crash that results in accident and monetary losses.
Why Should You Work with a Legal Representative?
Technically, you can submit an injury claim versus an insurer on your own. Some individuals pick this path when they have actually suffered just moderate injuries and have the time to investigate the legal claims process themselves. Likewise, avoiding an attorney will conserve you some money in legal costs.
Nevertheless, an accident lawyer– especially a personal injury lawyer– can help you take on huge vehicle insurer and their team of attorneys. Your lawyer already knows the personal injury laws and procedural guidelines and can efficiently deal with all the legwork for you. She or he will function as your advocate throughout the whole case.
Since an insurer's attorneys have the understanding to reduce compensation as well as deny the claim completely, working with an accident lawyer is the very best alternative for people who:
- Have actually suffered extreme injuries.
- Are confronted with expensive medical costs.
- Have actually experienced a significant loss of earnings due to their injuries.
Reasons to Consult an Accident Lawyer
If any of the following apply to you, consider employing an accident attorney.
- Auto Accident Injuries
- Extreme Injuries
Generally, the intensity of your personal injuries is determined by the:
- Kind of injury (or injuries) you have actually sustained.
Length of time it takes (or will take) for you to recuperate.
- Cost of medical costs (and any other restorative treatments) you have actually incurred.
- This also can consist of the estimated cost of future medical treatments.
Long-Term or Permanently Disabling Injuries
Normally speaking, a long-term injury is one that lasts for around a year or longer, while a permanent injury is one that disables you for life. These kinds of accidents seriously affect your capability to end up being and stay used– not to mention the quality of your life.
Proving long-term and completely disabling injuries can be challenging company, and your personal injury attorney probably will talk to each medical professional you've seen. He or she even might request the presence of your doctor during any legal procedures.
Disputed Liability
When an insurance provider challenges its policyholder's liability for the car crash, the business is basically saying that the policyholder is not at fault (or is at least claiming you don't have adequate proof of fault) and, for that reason, the insurance provider is not responsible for paying for your damages.
An accident lawyer in Vintage Oaks South of Seminary Menlo Park CA will assist you offer this proof and reveal that the other party was undoubtedly at fault.
Refusal to Pay
Refusal to pay (which can however does not necessarily come from a disputed liability) or refusal to pay a fair amount is when an insurer outright will not make a reasonable settlement deal– or any deal at all.
Tips for Working with an Accident Legal Representative
Because of possible situations such as statutes of limitations (which can vary by state), it is essential to hire a personal injury attorney and get the claims process going as quickly as possible; nevertheless, you don't wish to hire the very first lawyer for whom you see a signboard on the highway.
Consider these suggestions as you search for the right accident attorney.
Personal Injury Focus
Just as there are many different physicians who focus on several areas of medication, there is a wide variety of legal representatives from which to select.
As you select your accident lawyer, ensure he or she focuses on personal injury accidents.
Lastly, examine your convenience level with the lawyer.
You can start assessing your convenience level from the beginning (for instance, how do you feel about the attorney's success rate with car accident cases?) and continue beyond the time you employ him or her.
In some cases, examining your convenience level can avoid you from employing a personal injury lawyer who isn't really well matched for your case; other times, it may encourage you it's time to change course with a brand-new lawyer.
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The presentation, held at Comillas, was attended by the Director of the Publications Service and Professor Salomé Adroher
The Publications Service of the University has just published the book "Retirement and Socio-Legal Protection of the Elderly", by Gerardo Hernández and María del Carmen Meléndez, and has now become part of the 'Comillas Library Collection. Social Sciences'. In addition to the two authors, Juan Díez Nicolás, Professor Emeritus of Sociology at the Complutense University of Madrid, attended the presentation of the work, held at Comillas as well as Salomé Adroher, Professor of Private Law at the University, and Belén Recio, Director of the Publications Service of the University.


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A Novelle by B. Auerbach, published in 1843 in Schwarzwälder Dorfgeschichten (vol. 1). It begins with the recent foundation of a society for rehabilitating released prisoners by finding them situations ...
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The Club
The Four Counties Gliding Club is a member of the Royal Air Force Gliding & Soaring Assocition, and exists to offer the sport of gliding to personnel of the RAF, and other armed serices, particularly those who would not normally experience flight in their everyday roles.
The club operates every weekend and bank holiday (weather permitting), with a fleet of training and single seater gliders, catering for all levels of the sport.
The name of the club is said to be derived from the number of counties visible from the top of a winch launch at Wittering. Although there is some dispute as to the actual four, Wittering sits roughly at the junction of Rutland, Lincolnshire, Cambridgeshire, and Northamptonshire, with the main runway crossing the boundary between Cambs. and Northants.
The Club currently operates from the Charlie South dispersal at the West end of the airfield (for full details see the Find Us page).
RAF Wittering
The Club was established at RAF Wittering in March 1956, the first flying taking place on Thursday 29th March. In its first year the club had a core of around 45 members, and a fleet consisting of a Mk.1 & Mk.3 Cadet, later supplemented with a Grunau Baby.
In that first year the club managed some 2500 launches, with around 200 flying hours, an average of 4.5 minutes per launch. It seemed the club would be accident free in its first year, until just short of the years end, when both the Mk.1 and Mk.3 were broken within minutes of each other! The Mk.1 blown over in a gust, and the Mk.3 broken in a heavy landing incident.
Although instructor numbers fluctuated in the first few years, the club continued to grow, acquiring a Kite and a second Mk.3, while converting the Mk.1 to a Mk.2 Tutor.
Launching in the early days was by Auto-Tow and Winch. The Wittering Chipmunk trainer was also converted for Aerotowing, and gave the opportunity for regular aerotows.
RAF Spitalgate
In the mid 60s the club made the first of many moves to a new site, travelling to RAF Spitalgate just outside Grantham, Lincolnshire. This move started the clubs long association with the East Midlands, from where many of the club's members still travel. With the transfer of Spitalgate to the Army, however, it was time for the club to move on.
RAF Syerston
In 1975 the club moved a few miles down the road to RAF Syerston, near Newark, Nottinghamshire, home of the Air Cadet Central Gliding School. This began one of the most prosperous and stable periods for the club during what many consider to have been the heyday of RAF Gliding in the late 70s to 80s. The club shared the airfield with two Volunteer Gliding Schools (643 & 644) of the Air Cadet Movement. The Club and ATC shared a good working relationship, but it would be this sharing arrangement that would eventually see the end of Four Counties at Syerston.
In 1990, Nottingham University Gliding Club left Saltby and came to fly with Four Counties at Syerston. While at first the clubs were kept very much separate, with the University restricted to flying their own gliders, as time progressed NUGC became an integral part of the club, bringing youth and enthusiasm and a steady stream of students willing to learn to fly, as well as contributing to the very healthy social scene!
RAF Barkston Heath
However, by early 2004 the Air Cadets were planning a change to their operations, which would require their use of the entire airfield. This, combined with unfriendly forces at Syerston and HQ Air Cadets, prompted yet another move.
The RAFGSA had plans to move the club back to RAF Wittering, but our old home was not ready to take us. Being forced out, and with nowhere to go, the Club Executive organized a sideways move to RAF Barkston Heath, near Grantham and just down the road from Spitalgate, as a stop-gap measure and by Easter 2004 the bare bones of the club was at Barkston. With no infrastructure in place (apart from generously donated space in one of the large hangars) and most of the Club possessions still at Syerston, the Clubs future was uncertain. Besides this, the gliding club at RAF Cranwell was only a few miles down the road. Two large RAFGSA club in such close proximity, sharing catchment areas, was clearly not tenable.
Despite this, the club continued in their efforts and gradually improved on the basic start, providing basic facilities and the basis of a stable club.
RAF Wittering (Again)
Sadly, after a year or more of hard work, early 2005 saw the likelihood of another move increasing, and by May 05 the Club was bound for RAF Wittering once more. Unfortunately, this move would be too much for NUGC who could not justify the cost of travelling down to Wittering, and so departed for a new start at RAF Cranwell with the gliding club there.
By June 2005 the club was operating at Wittering. The early days saw only one third of the airfield available for use (around half the launching area available today) and the club spread between the portacabins on Charlie South, and the huge space of 2 Hangar at the other end of the airfield, where the Station had kindly let us store our equipment.
Later, with partial funding from the GSA, the hangar was erected on the Charlie South Apron, and we moved our gliders and equipment up closer to our launching area, which had now been extended to its current dimensions. Around this time, the club was also donated a complex of portacabins, which were refurbished and converted by the members, into our current clubhouse.
In May 2006 the Loughborough University Gliding Club joined Four Counties from Husbands Bosworth, entering into much the same arrangement as we had with NUGC.
If you have any more information on the Clubs History, or wish to correct anything on this page, contact Pete Davey.


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A&B DigiPlan
A&B DigiPlan is a membership-based commercial construction planroom. We provide project documents to general contractors, subcontractors, and suppliers for projects in Arkansas, Missouri, Kansas, and Oklahoma.
Information for new members is located here.
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Somewhere you can direct your subs and suppliers and job superintendents to get plans for bidding or building. We can build your own company branded planroom for you. Scan your plans or digitally upload and you control who can download and look at them. Call us for a quote.
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The Joint Trade Union Movement is warning the government to brace for a "tsunami response" to its national day of resistance.
The union is threatening to shut down the country over retrenchment and the implementation of austerity measures.
As it continues to mobilize workers, the union went to south Trinidad where San Fernando city corporation workers joined the call for resistance.
Cameraman Ivan Toolsie was there and reporter Ria Rambally has this report.


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Top 5 most useful features of iOS 8
At first glance, iOS 8 is not so different from its predecessor, as iOS 7. However, internal changes are enormous. Apple has made available to the parties under the operating system functions, the app added Health, is responsible for collecting data from various fitness devices, updated many regular programs.
To release iOS 8 MacDigger publishes five of the most useful features of "eight", who will appreciate the majority of the holders of iPhone and iPad.
1 Widgets
Widgets have become an important new feature in iOS 8. And let the users of Android-smartphone chuckled ironically, Apple gadgets for users is a great achievement. The fact that on the iPhone and the iPad will be a third-party widgets, said before the release of iOS 6, but access to them only opened with the release of the eighth edition of the operating system. In 8 iOS application developers can fine-tune the interface of the platform with features extensibility. In particular, Apple has opened a number of new API, which allow you to use widgets for Notification Center.
Of course, the widgets can not be called revolutionary innovation as "live" graphical interface elements for several years are presented in the OS Android. And users iOS-jailbroken devices have long practiced the installation of third-party solutions from the catalog Cydia. However, thanks to the new API, widgets for "Notification Center" will be available to all users of OS. Its widgets for iOS 8 have shown Philips , Numerous , Microsoft and other developers.
2 Extensions
Apple in the eighth edition of iOS «opened» its mobile operating system. With the final release of iOS 8 application developers for the iPhone and iPad users can fine-tune the interface of the platform with features extensibility. Apple opened a number of new API, allowing to add third-party extensions.
Export Settings: iOS makes it easy to share your photos, videos, web links, and any other content in social networks such as Facebook or Twitter. In iOS 8 open export settings for all developers.
Editing pictures developers were able to integrate their filters and editing tools right in the app photos. This means that iOS 8 allows you to use the effects of third-party developers in any application.
Personal action: touching the "Action", you can add a photo to a contact or print the document. iOS 8 allows developers to extend these opportunities. For example, the developer will be able to add the ability to put a watermark, add anything to your Wish List or translate text into another language.
Keyboard: Developers can create new versions of the keyboard, which will be used throughout the system. When they become available, you can choose your favorite layout or input method.
Touch ID: now you can use the sensor to log into third-party applications and more without entering a password. Fingerprint reliably protected, and no iOS, no other applications do not have access to it.
Documents: Apple iOS expanded opportunities to work with documents – you can now open and edit them using a larger number of applications, and for export to other applications no longer need to create extra copies.
3 Interactive notice
In iOS 8 appeared active alerts: You can respond to SMS or messages from social networks without having to open the apps themselves. The same is true for e-mail, alarm clock, reminders, and other applications. Through interactive notifications, you can interact with programs, without having to open them in full-screen and not turning off a running program. For example, if you come to the iPhone SMS, you can respond to it directly in the window with the notification. The same applies to social networks: if someone wrote a post on Facebook, you can layknut it in a popup window, without running the client.
Like it or not, the ability to respond to the event directly from the pop-up warning – this is exactly what was missing after appeared in iOS Notification Center. Can only be rightly indignant: "Why was not this done before?"
4 Smart Keyboard
While Apple has provided an interface for the development of "non-native" keyboards, staffing application will be a worthy alternative to the high-speed methods of typing due to Predictive. In addition to the auto-correction, familiar from previous versions of iOS, the keyboard is not only completes the first letters of the word, but also predicts the next word based on the context of the message. Taking into account the content of the dialogue and the recipient's name. In addition, over time, the application keeps track of user brushwork in different programs, so that the proposed expression differed in business correspondence and in an SMS. The only pity is that the Russian language is not yet supported.
5. Continuity
Handoff – it is almost inseparable from the life of your devices. When the iPhone or iPad on iOS 8 is next to the Mac, the function allows you to start work on one Apple device and finish on another. Everything happens automatically when the devices are attached to the same account iCloud. Handoff works in native applications, Mail, Safari, Pages, Numbers, Keynote, Maps, Messages, Reminders, Calendar, and Contacts. And developers can embed Handoff in their own programs.
For example, you can open a web page or a map on your phone and continue from the same point on the Mac. Or, for example, to transfer from iPhone to laptop letter to quickly finish it on a device with a comfortable keyboard. Imagine that somewhere in a traffic jam on you found inspiration, and his hands instinctively started sketching designs for future presentations on your iPad. When they reached the house, you are transferring for Mac and continue to work with the last saved point. Then're going to walk the dog and apply the finishing touches on the iPhone. With technology Handoff in OS X Yosemite and iOS 8 it became a reality.
Besides Continuity allows you to make and receive calls from your iPhone to your Mac or iPad. The main thing that a smartphone must be connected to the same network Wi-Fi. Likewise operate SMS-message. And if you do not have access to the Internet via Wi-Fi, iPad or Mac, you can easily connect to the web through the iPhone with the function Instant Hotspot.
See also:
All the main functions of 8 iOS for iPhone, iPad and iPod touch
15 jailbreak tweaks that make up the iOS 8
8 functions iOS 8 borrowed from Android
Top 10 hidden features 8 iOS for iPhone and iPad
Follow us on Twitter , VKontakte , Facebook , Google+ or via RSS , to keep abreast of the latest news from the world of Apple, Microsoft and Google.
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A new poll reveals that over 20 per cent of Millennials consider dictators Joseph Stalin and Kim Jong Un to be "heroes."
One in five (23%) of Americans age 21-29 consider Soviet dictator Joseph Stalin a 'hero'; 26% for Vladimir Lenin; 23% for Kim Jong Un.
As many as 60 million people were killed under Stalin's rule. And in North Korea, Kim Jong Un has executed hundreds of his own citizens (at least) since 2011 when he came into power.
The poll, released by the Victims of Communism Memorial Fund, additionally revealed that almost half (44 per cent) of millennials prefer socialism over capitalism.
It has been a full century since Vladimir Lenin's Bolsheviks seized power in Petrograd and communism made its bloody debut on the world stage. Authors, activists, and politicians alike are asking the question: what has America learned from one hundred years of communism?
More Millennials would prefer to live in a socialist country (44%) than in a capitalist one (42%). Some even said they would prefer to live in a communist country (7%). The percentage of Millennials who would prefer socialism to capitalism is a full ten points higher than that of the general population.
It seems that the majority of America's largest generation would prefer to live in a socialist or communism society than in a free enterprise system that respects the rule of law, private property, and limited government. This is even more disconcerting when coupled with the fact that, despite Millennials' enthusiasm for socialism and communism, they do not, in fact, know what those terms mean.
One remarkable finding of our study is that, to a high degree, Americans favor absolute protections for free speech, regardless of their views of communism or socialism. Communists and socialists more broadly have historically and ideologically favored state regulation of the press, speech, and popular assembly. Our results suggest that Millennials who favor socialism and communism have not thoroughly considered the implications of their political beliefs.
Data does, in fact, suggest that socialist-supporting millennials know little about the system of government they openly support.
Only 16 per cent of Millennials can accurately define what socialism is. Yet more Millennials voted for socialist Bernie Sanders than for Donald Trump and Hillary Clinton combined.
These clueless young people busy themselves protesting social issues like transgender bathrooms, abortion, and confederate statues. They regularly riot when conservative speakers come to town. But they remain clueless when it comes to basic economics and history.
This ignorance is dangerous. It's time for Millennials to pull their heads out of the sand, and get a grip about what's going on in this nation.


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This big boy turned 5 years old today!
Here's a little info about him on his birthday. (I asked him these same questions last year on his birthday. You can click here if you want to see what his answers were last year.)
Here are some other things about Alex..
He is a super sweetie who LOVES his family & friends!
He loves to help out with everything.
He is wise beyond his years.
He loves to build with Legos.
He's a homebody.
He loves to sing.
He loves to dig in the mud.
He loves to play dress up.
He not only wants to be a cowboy when he grows up, but also a engineer, a tap dancer & a singer.
Since he is having his birthday party next Saturday, we just had a small birthday celebration at home after dinner. Instead of a birthday cake, he had birthday brownies with sprinkles & marshmallows.
We sang Happy Birthday to him, he blew out the candles,
and then it was time to open presents!
Look how excited he was when he opened his Lego City police station.
He said it was just what he wanted!
I can't believe that my baby is 5 years old!
Happy birthday A Man!


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The butt. The booty. The ba-donk-a-donk. The rumpus. The gluteus maximus. The home of the twerk and the only reason I still go to work. Call it whatever you want, but everyone's got one and everyone should know how to work one. I know my around a tush, and hence, a girl's heart.
Many love torn women claim that there's a hole in their heart waiting to be filled by the right man, and then, and only then, will they find true happiness. What these women are failing to see is that there is a far more tangible hole that can be filled by a man, or woman, or both. The path to love is dark and covered in lubrication. Love might not feel right all the time, and even slightly invasive, but in the end, love is a battlefield that is your anus.
I've heard a lot of women say that they refuse to do butt-stuff with their partners on the grounds of 'decency'. To them I say quit being stuck up. What makes your posterior so untouchable compared to the billions of others that are out there? What sets your rumpus apart from the dozens of others I've had before? Take the stick out of your ass, and let the love in instead. If you don't feel comfortable allowing your partner to peruse the depths of your derriere, you don't love him or her at all.
Have you ever explored your buttocks yourself? Immerse yourself. Get into it! It's a wonderful place filled with infinite possibilities, creative wonderment and slight discomfort. It will always be there for you, from birth 'til death, unlike some boyfriends or girlfriends I could mention. Make friends with it, tame it, train it, become one with it. Today, only you can make your life a little more anally satisfying.
I'm currently single and searching for bigger, better booty. But I'll always have my own butt, and this is what allows me to sleep at night (specifically with a plug). And remember; always, always, always keep your cucumbers and KY stocked up because I just realized I'm fresh out. Off to HEB!
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It's becoming the norm rather than the exception – "Oh Father, I'm not religious, but I am spiritual…" Another way to express such a disposition would be to say that one has chosen to set aside 'organized religion', while choosing to open themselves up to the undeniable forces of the spiritual realm. The premise being that the 'spiritual realm' is basically neutral – neither good nor bad.
Discover why and how 'New Age Philosophies' have not only come to entice our younger generations to travel down this garden path of error and lies, but also call for authentic Catholic witness on our part.
"The Culture of the Occult and the New Age"
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Securus Technologies' First Code Release of 2016 Upgrades Major Platforms
Newest release delivers enhanced front-end and back-end support to improve usage and performance
Feb 05, 2016, 02:55 ET
DALLAS, Feb. 5 2016 /PRNewswire/ -- Securus Technologies, a leading provider of civil and criminal justice technology solutions for public safety, investigation, corrections and monitoring, announces the first code release of 2016, improving and expanding our major platforms to benefit corrections agencies, inmates and family and friends.
"We exist to Serve and Connect to make our world safe. With the largest IT development staff in the corrections industry, Securus helps improve public safety and reduce the inconvenience of incarceration – making everyone's experience better," said Russell Roberts, Vice President of Marketing and Strategy at Securus Technologies. "This release exemplifies our consistency and perseverance of our mission." This first release of 2016 touched almost every major platform at Securus Technologies: Securus OnlineTM; Securus Video VisitationTM; ConnectUsTM; Secure Call PlatformTM; Investigator ProTM; and our SecureViewTM Tablet Program. The release provides additional patches, resolves defects and includes code deployments needed to stage a new confidential product to be released later this year.
"With each release, our product set becomes larger and we move further ahead of our competition. This isn't possible without a great team, a single state-of-the-art calling platform that all of our customers have been migrated to, and the investment strategy necessary to continuously improve technology for our constituents: family and friends; inmates; and corrections agencies," said Richard A. "Rick" Smith, CEO, Securus Technologies. "The Secure Calling Platform (SCP) and ancillary platforms represent the largest single calling platform in the world for corrections and law enforcement – we are #1 for a reason," said Smith.
Headquartered in Dallas, Texas, and serving more than 3,400 public safety, law enforcement and corrections facilities and over 1,200,000 inmates across North America, Securus Technologies is committed to serve and connect by providing emergency response, incident management, public information, investigation, biometric analysis, communication, information management, inmate self-service, and monitoring products and services in order to make our world a safer place to live. Securus Technologies focuses on connecting what matters®. To learn more about our full suite of civil and criminal justice technology solutions, please visit SecurusTechnologies.com.
Logo - http://photos.prnewswire.com/prnh/20100831/DA57799LOGO
SOURCE Securus Technologies, Inc.


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Math Journals
You might be wondering why you are seeing less work mats! Well it's because Miss Law either cut them up or recycled them in lieu of other problems! :) We are working on solving algebraic thinking and 10's and 1's problems. I am giving as little "set up" support as possible to see how they approach solving it. Some days, I will cut up the problems (see above) and take away the strategy given to see their thinking. The other day they were given four problems and asked to solve it. At share time, we saw how many different ways there were to get to the same answer! We saw pictures, numbers, drawings with lines all over it, multiplication, number sentences and skip counting! It was cool to see how they talked about their solutions with each other, or how they found a similarity/difference from one another.
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October 2016


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Crixeo: 'Haunted' Louisiana Mansions
Ghosts Along the Bayou: Three Haunted Louisiana Mansions
There's always been something gothic about Louisiana, with its haunting beauty and alluring ghost stories. Natives are no stranger to tales of the swamps, odd paranormal activity and haunted places. They're practically tradition! And when I was growing up, there were three homes in particular that captured my imagination, with backstories filled with blood and gore. Over the years, these stories have become a part of me, in a sense, still sticking to my bones and memory like a bowl of my mother's gumbo or my great-grandmother's rice and gravy. More than that, these tales have become a form of Southern mythology, with lessons folded into each haunting. So let me share these tales with you, and tell them as they were told to me:
The Myrtles, St. Francisville
There was a young, beautiful girl named Chloe who worked as a field slave for the Laurel Grove Plantation on Bayou Sara (now known as St. Francisville). She labored beneath the hot Louisiana sun most of her life, picking cotton and indigo petals, until one day the owner of the plantation — Judge Clark Woodruff — discovered the girl and decided to make her his mistress. Once Chloe began her work in the house, she realized her role was twofold: tend to the judge, as well as the children — all under the watchful eye of the judge's wife, Sarah.
Sarah neither liked nor trusted Chloe and often complained to her husband about her, saying the girl should be sent back to work in the fields. Afraid of losing her position in the house, Chloe turned to eavesdropping, hoping to gather information that might give her an advantage over Sarah. The only problem? Chloe was terrible at eavesdropping, and she was often caught. Each time, the judge would warn her to stop or else he'd have to punish her — but still Chloe listened in. Sarah increased the pressure on her husband to do something, and soon he did.
On that fateful day, Chloe made the mistake of listening in on one of Judge Woodruff's confidential conversations with a visitor and was caught when the visitor opened the door to leave, resulting in Chloe falling into the room on her knees. It was then that the judge dragged her out to the courtyard and sliced off her left ear, just before banishing her from the house to work in the kitchen.
Now, for Chloe, working in the kitchen was worse than working in the fields. The space made her feel claustrophobic, and the temperature was blistering hot. She soon felt the strongest urge to win her way back into the house — and the judge's good graces. She took to wearing a green scarf around her head, tilted to the left to cover the scar. And one day, as she watched the young children playing without her, Chloe hatched a plan. She knew if the children were sick, they'd call for her, so she decided to put an extra ingredient into their birthday cake, just enough to have them cry her name.
The celebration was only a few days away, so Chloe acted quickly. She plucked leaves off an oleander plant growing very near the house; then she boiled the leaves in milk and butter, which she added to the cake batter. And yes, the children soon got sick, as did their mother, Sarah, but because the poison of oleander is so potent, Chloe was unable to nurse them back to health. Two of the three small children died, as did Sarah, all while the judge was out of town.
Fellow slaves, fearing they would be punished for such a crime, made Chloe stand trial for the deaths in the family, found her guilty and sentenced her to hang from an oak tree. To make sure she never returned, they weighed her body down with stones and threw her into the river. But some say Chloe is still in the house, playing with the children. Guests who have stayed overnight at the bed and breakfast swear they've heard them laugh in the night, as Chloe whistles and works.
Delphine Macarty was a woman of high birth and privilege in Creole society, with plenty of wealth, beauty and charm to secure her spot among the New Orleans elite. She'd been married twice, accumulating even greater wealth, before she walked down the aisle with Louis Lalaurie, a surgeon who specialized in human deformities. Louis was somewhat younger than her, and she came with children in tow; but things appeared to be normal when the couple purchased their three-story mansion on the corner of Royal and Governor Nicholls Street in the French Quarter in 1832. There they threw fabulous parties, entertaining foreign dignitaries and business titans of the day. Delphine was at the height of her fame as a Creole queen of the New Orleans social scene. But rumors began to circulate among their neighbors, and people started to wonder what exactly was going on at 1140 Royal Street.
One night in 1833, a neighbor saw Delphine on the roof of the house, bullwhip in hand, chasing a small slave girl no older than eight. At one point, the girl lost her footing and fell to the stone courtyard below with a crunch. Older slaves were seen collecting the mangled body and burying the girl in the yard. The rumors grew more frightening, but no one knew anything for sure.
Then there was the fire. Witnesses said the cook started it. Police found her chained to the stove. Some say she was the grandmother of the child who'd fallen off the roof and that she'd decided to sacrifice her own life in the name of revenge against the Lalauries. And while the mansion burned, Delphine tried to save her artwork. Louis tried to make the rescuers leave, but a fireman found a lock on the attic door and decided to break through. There they found ghastly horrors unlike any New Orleans had seen before.
The room was dank with the smells of blood, feces and death. Slaves were shackled in heavy chains, starved and mutilated. One woman's joints had been broken and reset to make her resemble a crab; a man's head had suffered a major blow and maggots were crawling in and out of the injury. Another was covered in honey, with ants devouring his skin. And even more had random body parts sewn onto their flesh in awkward locations, or their intestines tied around their waists. A bucket of organs and chum was collecting flies in the center.
When the crowd saw these poor souls carried out on stretchers, the people formed an angry mob, demanding punishment for the wicked Madame Lalaurie, who they soon saw escape in her carriage. They chased the horses but failed to catch up, letting Madame Lalaurie get away. Some say she died in France; others, that she one day returned to New Orleans and lived out the rest of her days hiding from her crimes. But to this day, many visitors claim they hear muffled screams, knocking, scratching, and cries. And on certain nights, they say, you can still see that poor little girl falling from the roof, which is why they call the Lalaurie Mansion the most haunted house in New Orleans.
Félicité Chretien was what you might call a "man's woman." As a child she worked with her father running his plantation and broke the mold of what a Louisiana woman in the 1800s might accomplish. She rode horses astride, like a man, smoked cigars, visited New Orleans unchaperoned and often played poker with the men, her dark eyes and husky laugh both equally memorable. And after her husband and youngest child had died from yellow fever, she took it upon herself to raise her four remaining children while managing her husband's family plantation, just 14 miles north of Lafayette.
News quickly spread throughout the area about Félicité living alone in a 12-room redbrick mansion on 3,000 acres of cotton. There were even rumors that a former tenant of the home, a pirate by the name of Jean Lafitte, had buried treasure in the yard, which added to the appeal of robbing Chretien Point. And during the 1840s, a gang of men decided to do just that. In the dark of night, they traveled down Bayou Bourbeaux and snuck onto the property, creeping toward the house. Félicité heard strange noises from her bedroom and peeked through her window to discover the men advancing on her porch in the darkness. She grabbed her gun and a satchel of money, then headed toward the stairwell.
Félicité knew the children were sleeping, and the servants had already left for their homes across the field. There was only so much she could do, but she had to protect the house. Suddenly the front door opened, and she saw a man enter her foyer and begin to climb the stairs. "Stop," she cried out, holding up the money.
But the man did not stop. Instead, he continued to approach her, unfazed by her 4'10" frame. And when he got just close enough that she could see the whites of his eyes, Félicité raised her gun and shot the man clean in the middle of his head. His body collapsed on the stairs and bled into the carpet.
Quickly, Félicité jumped over the corpse and raced to wake up the men of the property, who lived in the back fields. They grabbed their guns and followed her to the house, where the other men still lurked out front.
"What do you want?" she screamed out to them.
"Our friend," they replied.
"He ran out back when he heard the gun. Your friend isn't here, and we will shoot you if you do not leave."
The men ran away from the plantation, leaving their friend behind.
The next day, Félicité had the intruder's body removed from her home, but some say his spirit remains. Rumor has it that when the maids tried to remove the bloodstains from the stairwell, they would not budge. And when guests stay in the home today, they swear they can hear someone climbing the stairs, only for a gun to go off in the night.
In the case of Chretien Point, there was indeed an intruder and Félicité famously protected her home that night. As for the ghost, no one can be sure if he actually exists, but at least we know the incident truly occurred, as it's recorded in the St. Landry Parish Courthouse. As for The Myrtles, and the legend of Chloe, it's very difficult to prove Chloe ever existed, and since the records say both Sarah and her two children — a daughter and a son — died of yellow fever, it's hard to believe the birthday cake incident ever happened. Even more damning is the fact that tales of Chloe didn't really begin until the 1950s, when an Oklahoma widow named Marjorie Munson purchased the house. And the only "proof" presented is a postcard with a blurry image of what appears to be an older woman, walking toward the kitchen in the breezeway; however, since this "proof" is presented as a product to be purchased, rather than as evidence, that makes me believe the entire story is completely false.
As for Madame LaLaurie, it appears the tale of 1140 Royal Street is a gross exaggeration of events. Yes, she and her husband appear to be guilty of abusing and starving their slaves — which is horrible — but as far as the medical experiments and grotesque mutilation of victims, the evidence leads one to believe those accusations are false. In addition, the small child who fell off the roof in the tale has never been identified. There are no records of a Nina, and no human remains were ever found buried in the courtyard. That particular story appears to have been created by a British travel writer and abolitionist named Harriet Martineau in the 1840s. As for the horror show in the attic? There are no police or historical records validating such a scene. Instead, this can be traced to a 1946 book by Jeanne DeLavigne titled Ghost Stories of Old New Orleans. Otherwise, there is no evidence to support this version of the tale. (For a deeper analysis, I highly recommend Mad Madame Lalaurie by Victoria Cosner Love and Lorelei Shannon.)
Of course, the truth isn't nearly as exciting as a good tale or ghost story. Having visited all three of these reportedly haunted places at one point or another, I can say there is something exciting about being there. And whether or not ghosts actually exist, there is value in telling these tales. After all, would The Myrtles be such an attraction for tourists if Chloe's tale had never existed? Would Haunted Louisiana tours be as much good fun without a stop at the "most haunted house in New Orleans"? Would it hurt to think Félicité Chretien was such a badass that she sent a burglar, who meant her family harm, into purgatory instead of hell? Isn't it fun to look at these old so-called haunted places and wonder, "What if?"


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|The latest from Nestor Miranda and Don Pepin Garcia is the full bodied masterpiece La Sirena. Rich and complex, this Ct. Broadleaf
Maduro wrapped beauty is loaded with tons of thick and chewy smoke. A wonderful balance of spice and sweetness, this cigar is
extremely enjoyable. Well made with almost a perfect draw and burn. Buy a box now, you won't be dissapointed.
|Handmade in Nicaragua
Wrapper: Connecticut Broadleaf Maduro
Binder: Nicaragua
Filler: Nicaragua
|Feel Free To Call Us


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Creating a sustainable jewellery industry
Thursday, August 22, 2013
Come along to the International Jewellery London Exhibition to share on the topic of ethical, social and humanitarian issues in the jewellery industry.
International Jewellery London takes place 1 - 4 September 2013 to showcase the finest jewellery manufacturers, brands and designers in the UK. On 2 September come along to take part in The Great Debate from 12 - 1:15pm.
In its seventh year, The Great Debate explores ethical and social questions for the jewellery industry, and has now moved on to talk about sustainability too. In 2013 the debate is looking outside of the jewellery industry to learn how the fashion and grocery industries are facing up to these challenges.
Panellists this year include Daniela Nordmeyer from Monsoon Accessorize, Alan Frampton, Director of Cred Jewellery and Michael Allchin, Chief Executive of The Birmingham Assay Office. The debate is a joint initiative between The Birmingham Assay Office and Reed Exhibitions. Plus, Catherine Sproule, the Chief Operations Officer of the Responsible Jewellery Council will make a special global announcement at the start of the debate.
Come along to share the panellists' inspirational enthusiasm, learn how they are making a difference and express your own views and ideas on the topic of ethical, social and humanitarian issues within the jewellery industry. There is no need to book for the debate, just come to the Inspirations Theatre at International Jewellery London at 12 noon. A visitor pass for the main exhibition will be required in order to attend.
To register please visit www.jewellerylondon.com/assay