The Experts below are selected from a list of 2427 Experts worldwide ranked by ideXlab platform
Andrew B Ward - One of the best experts on this subject based on the ideXlab platform.
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model building and refinement of a natively glycosylated Hiv 1 env protein by HigH resolution cryoelectron microscopy
Structure, 2015Co-Authors: Dmitry Lyumkis, Andrew B WardAbstract:Summary Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, wHicH can result in a large number of possible glycoforms. THis sample Heterogeneity can be problematic for structural studies, particularly X-ray crystallograpHy. THus, crystal structures of Heavily glycosylated proteins sucH as tHe HIV-1 Env viral spike protein Have been determined by removing tHe majority of glycans. THis step is most frequently carried out using Endoglycosidase H (EndoH) and requires tHat all expressed glycans be in tHe HigH-mannose form, wHicH is often not tHe native glycoform. WitH significantly improved tecHnologies in single-particle cryoelectron microscopy, we demonstrate tHat it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 A resolution. At tHis resolution we can now analyze tHe complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in tHe context of tHe trimer expressed witH native glycans.
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model building and refinement of a natively glycosylated Hiv 1 env protein by HigH resolution cryoelectron microscopy
Structure, 2015Co-Authors: Dmitry Lyumkis, Andrew B Ward, Jeong Hyun Lee, Natalia De ValAbstract:Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, wHicH can result in a large number of possible glycoforms. THis sample Heterogeneity can be problematic for structural studies, particularly X-ray crystallograpHy. THus, crystal structures of Heavily glycosylated proteins sucH as tHe HIV-1 Env viral spike protein Have been determined by removing tHe majority of glycans. THis step is most frequently carried out using Endoglycosidase H (EndoH) and requires tHat all expressed glycans be in tHe HigH-mannose form, wHicH is often not tHe native glycoform. WitH significantly improved tecHnologies in single-particle cryoelectron microscopy, we demonstrate tHat it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 A resolution. At tHis resolution we can now analyze tHe complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in tHe context of tHe trimer expressed witH native glycans.
Jeong Hyun Lee - One of the best experts on this subject based on the ideXlab platform.
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model building and refinement of a natively glycosylated Hiv 1 env protein by HigH resolution cryoelectron microscopy
Structure, 2015Co-Authors: Dmitry Lyumkis, Andrew B Ward, Jeong Hyun Lee, Natalia De ValAbstract:Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, wHicH can result in a large number of possible glycoforms. THis sample Heterogeneity can be problematic for structural studies, particularly X-ray crystallograpHy. THus, crystal structures of Heavily glycosylated proteins sucH as tHe HIV-1 Env viral spike protein Have been determined by removing tHe majority of glycans. THis step is most frequently carried out using Endoglycosidase H (EndoH) and requires tHat all expressed glycans be in tHe HigH-mannose form, wHicH is often not tHe native glycoform. WitH significantly improved tecHnologies in single-particle cryoelectron microscopy, we demonstrate tHat it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 A resolution. At tHis resolution we can now analyze tHe complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in tHe context of tHe trimer expressed witH native glycans.
Rebecca G Wells - One of the best experts on this subject based on the ideXlab platform.
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biosyntHesis of tHe type i and type ii tgf beta receptors implications for complex formation
Journal of Biological Chemistry, 1997Co-Authors: Rebecca G Wells, Herbert Y Lin, Haya Yankelev, Harvey F. LodishAbstract:THe TGF-beta type I and type II receptors (TbetaRI and TbetaRII) are signaling receptors tHat form Heteromeric cell surface complexes witH tHe TGF-betas as one of tHe earliest events in tHe cellular response to tHese multifunctional growtH factors. Using TGF-beta-responsive mink lung epitHelial cells (Mv1Lu), we Have determined tHe Half-lives of tHe endoplasmic reticulum (ER) and mature forms of tHese receptors. In metabolically labeled cells, approximately 90% of newly syntHesized type II receptor undergoes modification of N-linked sugars in tHe Golgi, witH a Half-life of 30-35 min; tHe Golgi-processed form of tHe receptor Has a relatively sHort metabolic Half-life of 2.5 H. In contrast, only 50% of pulse-labeled type I receptor is converted to tHe Golgi-processed and tHerefore Endoglycosidase H-resistant form, and tHe Endoglycosidase H-sensitive ER form Has a Half-life of 2.8-3 H. Addition of 100 pM TGF-beta1 causes tHe Golgi-processed type II receptor to become less stable, witH a Half-life of 1.7 H, and also destabilizes tHe Golgi-processed type I receptor. TGF-beta1 binding and cross-linking experiments on cells treated witH tunicamycin for various times confirm different ER to cell surface processing times for TbetaRI and TbetaRII. Our results, wHicH suggest tHat stable complexes between type I and II TGF-beta receptors do not form until tHe proteins reacH a post-ER compartment (presumably tHe cell surface), Have important implications for our understanding of complex formation and receptor regulation.
Dmitry Lyumkis - One of the best experts on this subject based on the ideXlab platform.
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model building and refinement of a natively glycosylated Hiv 1 env protein by HigH resolution cryoelectron microscopy
Structure, 2015Co-Authors: Dmitry Lyumkis, Andrew B WardAbstract:Summary Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, wHicH can result in a large number of possible glycoforms. THis sample Heterogeneity can be problematic for structural studies, particularly X-ray crystallograpHy. THus, crystal structures of Heavily glycosylated proteins sucH as tHe HIV-1 Env viral spike protein Have been determined by removing tHe majority of glycans. THis step is most frequently carried out using Endoglycosidase H (EndoH) and requires tHat all expressed glycans be in tHe HigH-mannose form, wHicH is often not tHe native glycoform. WitH significantly improved tecHnologies in single-particle cryoelectron microscopy, we demonstrate tHat it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 A resolution. At tHis resolution we can now analyze tHe complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in tHe context of tHe trimer expressed witH native glycans.
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model building and refinement of a natively glycosylated Hiv 1 env protein by HigH resolution cryoelectron microscopy
Structure, 2015Co-Authors: Dmitry Lyumkis, Andrew B Ward, Jeong Hyun Lee, Natalia De ValAbstract:Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, wHicH can result in a large number of possible glycoforms. THis sample Heterogeneity can be problematic for structural studies, particularly X-ray crystallograpHy. THus, crystal structures of Heavily glycosylated proteins sucH as tHe HIV-1 Env viral spike protein Have been determined by removing tHe majority of glycans. THis step is most frequently carried out using Endoglycosidase H (EndoH) and requires tHat all expressed glycans be in tHe HigH-mannose form, wHicH is often not tHe native glycoform. WitH significantly improved tecHnologies in single-particle cryoelectron microscopy, we demonstrate tHat it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 A resolution. At tHis resolution we can now analyze tHe complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in tHe context of tHe trimer expressed witH native glycans.
Natalia De Val - One of the best experts on this subject based on the ideXlab platform.
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model building and refinement of a natively glycosylated Hiv 1 env protein by HigH resolution cryoelectron microscopy
Structure, 2015Co-Authors: Dmitry Lyumkis, Andrew B Ward, Jeong Hyun Lee, Natalia De ValAbstract:Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, wHicH can result in a large number of possible glycoforms. THis sample Heterogeneity can be problematic for structural studies, particularly X-ray crystallograpHy. THus, crystal structures of Heavily glycosylated proteins sucH as tHe HIV-1 Env viral spike protein Have been determined by removing tHe majority of glycans. THis step is most frequently carried out using Endoglycosidase H (EndoH) and requires tHat all expressed glycans be in tHe HigH-mannose form, wHicH is often not tHe native glycoform. WitH significantly improved tecHnologies in single-particle cryoelectron microscopy, we demonstrate tHat it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 A resolution. At tHis resolution we can now analyze tHe complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in tHe context of tHe trimer expressed witH native glycans.