PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2558637-5 1989 Altogether the results indicated that Cys402, probably by participating in a disulfide bridge, is essential for (i) the CD4-binding ability of env gene products and for (ii) the physical stability of gp 120. Disulfides 77-86 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 200-206 34020817-6 2021 The clade A trimer, which we named "BG505 DS-SOSIP.664", contained an engineered disulfide (201C-433C; DS) within gp120, which further stabilized this trimer in a prefusion-closed conformation resistant to CD4-induced triggering. Disulfides 81-90 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 114-119 30948772-1 2019 Human immunodeficiency virus (HIV-1) entry is initiated by the binding between the viral envelope glycoprotein gp120 and the host receptor CD4, and followed by reduction of structural disulfides of gp120 and CD4. Disulfides 184-194 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 198-203 30948772-6 2019 Moreover, PX-12 inhibited the enzymatic activity of Trx1 and the Trx1-dependent disulfide reduction of gp120. Disulfides 80-89 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 103-108 32522853-7 2020 Shedding of gp120, known to severely complicate structural studies, can be prevented by using the uncleaved gp160JR-FL precursor with alterations in the protease cleavage site (R508S/R511S), or by introducing a disulfide bridge between gp120 and gp41 designated "SOS" (A501C/T605C). Disulfides 211-220 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 12-17 31619555-2 2019 The prototypic design, designated BG505 SOSIP.664, incorporates an inter-subunit disulfide bond (SOS) to covalently link the gp120 and gp41 ectodomain (gp41ECTO) subunits and a point substitution, I559P (IP) to further stabilize the gp41ECTO components. Disulfides 81-90 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 125-130 30948772-2 2019 The host thioredoxin-1 (Trx1) efficiently reduces disulfides of gp120 and CD4 in vitro, and recently CD4-dependent HIV-1 entry was shown to be inhibited by anti-Trx1-antibodies, indicating a central role for Trx1. Disulfides 50-60 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 64-69 27716795-9 2016 Together, these results provide a mechanism for conservation of disulfide linkage proximal glycosylation adjacent to the variable domains of gp120 and begin to explain how this could be exploited to enhance the immunogenicity of those regions. Disulfides 64-73 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 141-146 29470989-7 2018 Increases in the dynamics of regions important for HIV gp120 and MHCII binding in D1 also result allosterically after reducing the D2 disulfide, which are likely a consequence of the structural changes that take place in D2, findings that advance our understanding of the mechanisms by which redox exchange of the CD4 disulfides regulates its function. Disulfides 318-328 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 55-60 30021898-4 2018 The introduction of an artificial disulfide bond linking the gp120 and gp41 subunits (SOS) in combination with the I559P (IP) change has allowed structural characterization of soluble gp140 (sgp140) trimers. Disulfides 34-43 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 61-66 29729526-5 2018 Molecular modeling has confirmed that the twin-cysteines do form a disulfide bond in the gp120 subunit, which interacts with the V1 loop to stabilize the envelope trimer. Disulfides 67-76 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 89-94 27442017-5 2016 Moreover, mass spectrometry revealed some disulfide heterogeneity in the expressed proteins, particularly in V1V2-C1 region and most prominently in the TV1 gp120 dimers. Disulfides 42-51 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 156-161 26719247-4 2015 In contrast, the gp120 subunits of the native-like SOSIP.664 trimer almost exclusively retained the canonical disulfide bond pattern. Disulfides 110-119 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 17-22 26816344-2 2016 During entry, reduction of disulfide bridges in the viral envelope glycoprotein gp120 by cellular oxidoreductases is crucial. Disulfides 27-36 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 80-85 26719247-7 2015 The same factors may also be relevant to the production and purification of monomeric gp120 proteins that are free of aberrant disulfide bonds. Disulfides 127-136 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 86-91 26719252-7 2015 Using the redesigned subtype B and C trimer representatives as respective foundations, we further stabilized the NFL TD trimers by engineering an intraprotomer disulfide linkage in the prebridging sheet, I201C-A433C (CC), that locks the gp120 in the receptor nontriggered state. Disulfides 160-169 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 237-242 26458166-5 2015 Molecular docking of PTT onto gp120 argued that, with sufficient linker length, the peptide SH could approach and disrupt several alternative gp120 disulfides. Disulfides 148-158 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 30-35 26458166-5 2015 Molecular docking of PTT onto gp120 argued that, with sufficient linker length, the peptide SH could approach and disrupt several alternative gp120 disulfides. Disulfides 148-158 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 142-147 26458166-8 2015 Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane. Disulfides 133-143 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 190-195 26458166-8 2015 Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane. Disulfides 133-143 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 230-235 26458166-8 2015 Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane. Disulfides 133-142 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 190-195 26458166-8 2015 Overall, the results are consistent with the view that the binding of PTT positions the peptide SH group to interfere with conserved disulfides clustered proximal to the CD4 binding site in gp120, leading to disulfide exchange in gp120 and possibly gp41, rearrangement of the Env spike, and ultimately disruption of the viral membrane. Disulfides 133-142 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 230-235 25712564-3 2015 However, over-expression of HIV-1 gp120 in mammalian cells leads to the formation of aberrant disulfide-linked dimers that can bias the results of experiments aimed at measuring gp120 affinity with different ligands. Disulfides 94-103 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 178-183 26690492-2 2015 The three-dimensional functional structure of gp120 contains intramolecular disulfide bonds, which are critical for the interaction with the CD4 receptor. Disulfides 76-85 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 46-51 26311893-6 2015 The further addition of a disulfide bond (SOS) to link the gp120 and gp41 subunits in the uncleaved gp140-FL20-SOSIP protein increases native-like trimer formation to ~20 to 30%. Disulfides 26-35 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 59-64 26311893-7 2015 Analysis of the disulfide bond content shows that misfolded gp120 subunits are abundant in uncleaved CZA97.012 gp140UNC-Fd-His proteins but very rare in native-like trimer populations. Disulfides 16-25 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 60-65 25944298-5 2015 In this study, three gp120 (strain JR-FL) variants were constructed, in which deletions of single outer-domain disulfide bonds were expected to introduce local conformational flexibility and promote presentation of additional CD4(+) T-cell epitopes. Disulfides 111-120 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 21-26 25944298-6 2015 Following mucosal immunization of C57BL/6 mice with wild-type or variant gp120 lacking the V3-flanking disulfide bond, the typical pattern of dominant epitopes was observed, suggesting that the disulfide bond posed no barrier to antigen presentation. Disulfides 103-112 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 73-78 25944298-6 2015 Following mucosal immunization of C57BL/6 mice with wild-type or variant gp120 lacking the V3-flanking disulfide bond, the typical pattern of dominant epitopes was observed, suggesting that the disulfide bond posed no barrier to antigen presentation. Disulfides 194-203 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 73-78 25712564-6 2015 Removal of these aberrant disulfide-linked gp120 dimers by standard size exclusion chromatography is sufficient to restore the overall affinity of gp120 preparations for these ligands. Disulfides 26-35 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 43-48 25712564-6 2015 Removal of these aberrant disulfide-linked gp120 dimers by standard size exclusion chromatography is sufficient to restore the overall affinity of gp120 preparations for these ligands. Disulfides 26-35 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 147-152 23210856-7 2013 The method was applied for assigning the disulfide-bonding network of a recombinant monomer of the HIV envelope protein gp120. Disulfides 41-50 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 120-125 24146829-6 2013 We found that a single disulfide bond strategically inserted between the highly conserved layers 1 and 2 (C65-C115) is able to "lock" gp120 in a CD4 receptor bound conformation (in the absence of CD4), as indicated by the lower dissociation constant (Kd) for the CD4-induced (CD4i) epitope binding 17b antibody. Disulfides 23-32 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 134-139 24146829-7 2013 When disulfide-stabilized monomeric (gp120) and trimeric (gp140) Envs were used to immunize rabbits, they were found to elicit a higher proportion of antibodies directed against both CD4i and CD4 binding site epitopes than the wild-type proteins. Disulfides 5-14 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 37-42 24920818-6 2014 Destabilization of the gp120 conformation by deletion of single disulfide bonds preferentially enhanced responses to the cryptic I-Ak motif-containing sequences, as reported by T-cell proliferation or cytokine secretion. Disulfides 64-73 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 23-28 23592978-3 2013 In this study, we examined how the conserved gp120-gp41 association site, formed by the N- and C-terminal segments of gp120 and the disulfide-bonded region (DSR) of gp41, adapts to glycan changes that are linked to neutralization sensitivity. Disulfides 132-141 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 45-50 22230366-0 2012 Thioredoxin-1 and protein disulfide isomerase catalyze the reduction of similar disulfides in HIV gp120. Disulfides 80-90 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 98-103 22230366-4 2012 Here, it was demonstrated that PDI and Trx1 have similar gp120 disulfide targets as determined by labeling after reduction, but with some pattern differences, including overall stronger labeling with Trx1 than with PDI. Disulfides 63-72 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 57-62 22230366-7 2012 Carbohydrate binding agents (CBAs), previously shown to bind gp120 and inhibit HIV entry, were now demonstrated to inhibit gp120 disulfide reduction. Disulfides 129-138 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 123-128 22230366-2 2012 For entry, gp120 undergoes conformational changes that depend on the reduction of one or more disulfides. Disulfides 94-104 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 11-16 22230366-3 2012 Previous studies indicate that protein disulfide isomerase (PDI), thioredoxin-1 (Trx1), and glutaredoxin-1 (Grx1) catalyze gp120 reduction, but their specific disulfide targets are not known. Disulfides 39-48 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 123-128 20089653-0 2010 Influence of disulfide-stabilized structure on the specificity of helper T-cell and antibody responses to HIV envelope glycoprotein gp120. Disulfides 13-22 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 132-137 21689404-4 2011 We have previously stabilized soluble trimeric mimics of Env by introducing a disulfide bond between gp120 and gp41 and adding a trimer stabilizing mutation in gp41 (SOSIP.R6 gp140). Disulfides 78-87 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 101-106 22312332-7 2011 Fixation of the C-terminus by introducing a disulfide bridge between the N- and C-termini of the peptide significantly enhanced the affinity to gp120. Disulfides 44-53 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 144-149 20956336-5 2010 In order to increase the yield and stability of the spike, we used an endodomain deleted and gp120-gp41 disulfide-linked variant. Disulfides 104-113 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 93-98 20538591-3 2010 In this study, we describe a novel recombinant CD4 protein designed to bind gp120 through a targeted disulfide-exchange mechanism. Disulfides 101-110 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 76-81 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Disulfides 186-195 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 169-174 20458450-3 2010 In the present study, a kinetic trapping approach was used to capture the disulfide cross-linking intermediate between gp120 and PDI. Disulfides 74-83 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 119-132 20458450-5 2010 The active site mutant PDIs were able to covalently cross-link with gp120 through a mixed disulfide bond in vitro. Disulfides 90-99 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 68-73 20943653-0 2010 Disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin. Disulfides 0-9 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 41-46 20943653-1 2010 A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection. Disulfides 13-22 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 67-72 20943653-1 2010 A functional disulfide bond in both the HIV envelope glycoprotein, gp120, and its immune cell receptor, CD4, is involved in viral entry, and compounds that block cleavage of the disulfide bond in these proteins inhibit HIV entry and infection. Disulfides 178-187 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 67-72 20943653-3 2010 The target gp120 disulfide and its mechanism of cleavage were determined using a thioredoxin kinetic trapping mutant and mass spectrometry. Disulfides 17-26 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 11-16 20943653-4 2010 A single disulfide bond was cleaved in isolated and cell surface gp120, but not the gp160 precursor, and the extent of the reaction was enhanced when gp120 was bound to CD4. Disulfides 9-18 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 65-70 20943653-4 2010 A single disulfide bond was cleaved in isolated and cell surface gp120, but not the gp160 precursor, and the extent of the reaction was enhanced when gp120 was bound to CD4. Disulfides 9-18 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 150-155 20943653-5 2010 The Cys(32) sulfur ion of thioredoxin attacks the Cys(296) sulfur ion of the gp120 V3 domain Cys(296)-Cys(331) disulfide bond, cleaving the bond. Disulfides 111-120 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 77-82 20538591-4 2010 According to structural models of the gp120-CD4 receptor complex, substitution of Ser(60) on the CD4 domain 1 alpha-helix with Cys positions a thiol in proximity of the gp120 V1/V2 loop disulfide (Cys(126)-Cys(196)), satisfying the stereochemical and geometric conditions for redox exchange between CD4 Cys(60) and gp120 Cys(126), and the consequent formation of an interchain disulfide bond. Disulfides 377-386 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 169-174 20089653-4 2010 In this work, three disulfide bonds in the outer domain of gp120 were individually deleted in order to destabilize the local three-dimensional structure and enhance the presentation of nearby weakly immunogenic epitopes. Disulfides 20-29 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 59-64 19038358-6 2009 Grx1 catalyzes the reduction of two disulfide bridges in gp120 in a similar manner as PDI. Disulfides 36-45 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 57-62 17640393-9 2007 The HIV envelope glycoprotein gp120, for example, is regulated by thiol/disulfide exchange and contains allosteric -RHStaple bonds that can exist in the -LHStaple configuration. Disulfides 72-81 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 30-35 18237398-5 2008 However, its removal improved folding of a gp120 variant lacking the 385-418 disulfide bond, suggesting that it plays an auxiliary role in protein folding in the presence of this disulfide bond. Disulfides 77-86 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 43-48 18237398-5 2008 However, its removal improved folding of a gp120 variant lacking the 385-418 disulfide bond, suggesting that it plays an auxiliary role in protein folding in the presence of this disulfide bond. Disulfides 179-188 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 43-48 19018669-8 2008 This shows that the Cys228-Cys239 disulfide bond of gp120 is required for high-affinity binding to CD4. Disulfides 34-43 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 52-57 19086590-4 2007 According to this computational analysis 6 good disulfide binding states in Iranian gp120 were predicted. Disulfides 48-57 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 84-89 15994775-5 2005 In this construct, the gp120 and gp41 moieties are covalently linked by an intermolecular disulfide bond (SOS gp140), and an I559P substitution has been added to stabilize gp41-gp41 interactions (SOSIP gp140). Disulfides 90-99 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 23-28 17525470-7 2007 We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing. Disulfides 89-98 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 67-72 17525470-7 2007 We suggest that the mutations have altered the interaction between gp120 C5 and the gp41 disulfide loop, resulting in decreased accessibility of the furin recognition site and implying that the interaction between the gp120 C5 and gp41 loop is a conformational requirement for gp160 processing. Disulfides 89-98 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 218-223 16182193-3 2005 This could enable PDI to reduce gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry. Disulfides 38-47 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 32-37 16182193-3 2005 This could enable PDI to reduce gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry. Disulfides 38-47 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 106-111 17092531-4 2007 Soluble, stabilized, proteolytically cleaved, trimeric gp140 proteins can be generated by engineering an intermolecular disulfide bond between gp120 and gp41 (SOS), combined with a single residue change, I559P, within gp41 (SOSIP). Disulfides 120-129 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 143-148 12719576-1 2003 A mutant human immunodeficiency virus (HIV) envelope protein (Env) with an engineered disulfide bond between the gp120 and gp41 subunits (SOS-Env) was expressed on cell surfaces. Disulfides 86-95 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 113-118 15644496-2 2005 The triggering of fusion requires cleavage of two of the nine disulfide bonds of gp120 by a cell-surface protein disulfide-isomerase (PDI). Disulfides 62-71 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 81-86 14592831-6 2004 We further find that PDI facilitates thiol/disulfide rearrangement in gp120 during conformational change, whereas inhibition of this redox shuffling prevents gp41 from assuming the fusogenic 6-helix bundle conformation. Disulfides 43-52 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 70-75 12923196-4 2003 We found that the gp120-gp41 association function of the disulfide-bonded region is conserved. Disulfides 57-66 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 18-23 12773488-5 2003 Removal of the leader peptide critically depends on formation of at least some disulfide bonds in subunit gp120 during folding. Disulfides 79-88 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 106-111 12218052-6 2003 We conclude that on average two of the nine disulfides of gp120 are reduced during interaction with the lymphocyte surface after CXCR4 binding prior to fusion and that cell surface PDI catalyzes this process. Disulfides 44-54 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 58-63 11602730-2 2001 In this protection assay-based procedure, a soluble gp140 protein with a stabilizing intermolecular disulfide bond between the gp120 and gp41 subunits (SOS gp140) was affinity bound to immobilized 2F5 under physiological conditions. Disulfides 100-109 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 127-132 12218051-3 2002 Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors. Disulfides 38-47 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 91-96 12218051-3 2002 Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors. Disulfides 158-167 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 106-111 12218051-8 2002 We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4. Disulfides 109-118 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 150-155 12218051-9 2002 Conformational changes resulting from the opening of gp120-disulfide loops may drive the processes of virus-cell and cell-cell fusion. Disulfides 59-68 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 53-58 12163607-5 2002 A soluble form of Env, SOS gp140, can be made that has gp120 stably linked to the gp41 ectodomain by an intermolecular disulfide bond. Disulfides 119-128 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 55-60 8438588-6 1993 Gp160t, gp160t/sec, and gp120 formed oligomers which were stabilized by intermolecular disulfide bonds and/or noncovalent interactions and were also found to bind to soluble CD4. Disulfides 87-96 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 24-29 10623724-5 2000 To try to develop recombinant proteins that are better antigenic mimics of the native envelope glycoprotein complex, we have introduced a disulfide bond between the C-terminal region of gp120 and the immunodominant segment of the gp41 ectodomain. Disulfides 138-147 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 186-191 10623724-7 2000 The association of gp120 with gp41 is now stabilized by the supplementary intermolecular disulfide bond, which forms with approximately 50% efficiency. Disulfides 89-98 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 19-24 9225993-7 1997 Previous observations with other RNA and DNA viruses consistently showed that GSH antiviral effect occurred at late stages of virus replication and was related to the selective decrease of specific glycoproteins, such as gp120, which are particularly rich in disulfide bonds. Disulfides 259-268 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 221-226 7506556-2 1993 The epitope of this HuMAb was destroyed by reduction of gp120 disulfide bonds, but not by removal of N-linked carbohydrates. Disulfides 62-71 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 56-61 9870313-2 1998 A biotinylated disulfide-bridged peptide mimicking the complete loop of clade B consensus V3 domain of gp120 (V3Cs), but not a biotinylated V3LAI peptide or a control beta-endorphin peptide of approximately the same molecular weight (MW), was found to bind specifically to MDM membrane proteins, in particular two proteins of 42 and 62 kDa migrating as sharp bands after electroblotting onto Immobilon, and this was specifically inhibited by anti-V3 antibodies. Disulfides 15-24 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 103-108 9707171-6 1998 All these peptides used an oxidized Cys-X-Cys bridge to link the discontinuous sequence elements in a manner suggested by the known conserved disulfide bridges in gp120. Disulfides 142-151 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 163-168 9419208-3 1998 Sequence analysis revealed a TSP1 recognition motif, previously defined for the CD36 gene family of cell adhesion receptors, in conserved regions flanking the disulfide-linked cysteine residues of the V3 loop of HIV envelope glycoprotein gp120, important for HIV binding to its high affinity cellular receptor CD4. Disulfides 159-168 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 238-243 2014246-4 1991 The specificities of these mAbs have been mapped to sequences near the tip of the disulfide loop of the gp120 third variable domain, Lys-Arg-Ile-His-Ile and His-Ile-Gly-Pro-Gly-Arg, respectively. Disulfides 82-91 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 104-109 1727607-7 1992 Thus a disulfide loop at the V3 portion of gp160 is required for cleavage into gp120 and gp41, presumably because the loop is required for proper tertiary structure. Disulfides 7-16 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 79-84 34679128-4 2021 Initially, we boosted the expression of 17 candidate trimers by truncating gp41 and introducing a gp120-gp41 SOS disulfide to prevent gp120 shedding. Disulfides 113-122 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 98-103 34679128-4 2021 Initially, we boosted the expression of 17 candidate trimers by truncating gp41 and introducing a gp120-gp41 SOS disulfide to prevent gp120 shedding. Disulfides 113-122 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 134-139 34469718-3 2021 First, the signal peptide improves folding fidelity by enhancing conformational plasticity of gp120 by driving disulfide isomerization through a redox-active cysteine. Disulfides 111-120 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 94-99