Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.
about
Magic angle spinning NMR of virusesDesign and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery.The three lives of viral fusion peptidesFolded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionConditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid bindingBiochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor designSwapped-domain constructs of the glycoprotein-41 ectodomain are potent inhibitors of HIV infectionQuantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy.Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations.HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle statepH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide.Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.HIV-1 gp41 transmembrane oligomerization monitored by FRET and FCS.Solid-state nuclear magnetic resonance (NMR) spectroscopy of human immunodeficiency virus gp41 protein that includes the fusion peptide: NMR detection of recombinant Fgp41 in inclusion bodies in whole bacterial cells and structural characterization o
P2860
Q26825587-815BE1AF-C653-4AAC-8D12-367C3D800923Q30912819-3716685C-3734-44E3-915F-B6DAB84C2867Q33770459-16D0D839-8451-4E34-BD86-5781B91B8AD1Q34579843-650BDFA5-E2D4-4502-9973-BA87D97172F4Q35142768-AFE41F69-EEE0-45AE-99AB-B36EDE8A02B1Q35210688-8991F36D-377C-457F-A153-DF9D5D88F771Q35434452-9E8BF1CF-CC00-4E47-ADBA-4B484DB3E9E0Q35563298-8AAB2778-C26D-40F0-B1A5-DB10E19FD436Q36036157-2F8213CB-0C03-4C66-84B9-92955A260081Q37074027-70CFA235-E2D2-40FC-A2AE-5FE96D3A7F30Q39339121-E6AADE88-4311-4CD2-AC03-F3D0353C8F62Q41889237-7C1A1561-84B4-4CFA-9684-D12B031C78CAQ42003499-1BC7E4C5-604E-4593-AC3C-043D201D5448Q42202737-218D17D9-D6F2-4A78-9E73-A4B318AFC9E0Q42929024-1A51FD65-52C1-415C-A689-671DC0AB1B25Q43457528-26387553-22AA-4BAA-B1B3-AB46828ED1CEQ47551930-0B3300C6-9133-4309-8397-A073BCF57AADQ49906318-8188031C-D246-41C6-95EE-B17D3C402777Q56979426-FB332315-CE19-4001-A6C0-9295BA6475B6
P2860
Hairpin folding of HIV gp41 abrogates lipid mixing function at physiologic pH and inhibits lipid mixing by exposed gp41 constructs.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@en
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@nl
type
label
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@en
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@nl
prefLabel
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@en
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@nl
P2093
P2860
P356
P1433
P1476
Hairpin folding of HIV gp41 ab ...... ng by exposed gp41 constructs.
@en
P2093
David P Weliky
Kelly Sackett
Matthew J Nethercott
Yechiel Shai
P2860
P304
P356
10.1021/BI8019492
P407
P577
2009-03-01T00:00:00Z