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.

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.

Item
http://www.wikidata.org/entity/Q41889237
Dissociation of the trimeric gp41 ectodomain at the lipid–water interface suggests an active role in HIV-1 Env-mediated membrane fusionThe 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 bindingInsights into the Conformation of the Membrane Proximal Regions Critical to the Trimerization of the HIV-1 gp41 Ectodomain Bound to Dodecyl Phosphocholine Micelles.Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide maProtonation and pK changes in protein-ligand binding.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.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

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.

Item
http://www.wikidata.org/entity/Q41889237
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
HIV gp41 six-helix bundle cons ...... ions for HIV-host cell fusion.
@en
type
label
HIV gp41 six-helix bundle cons ...... ions for HIV-host cell fusion.
@en
prefLabel
HIV gp41 six-helix bundle cons ...... ions for HIV-host cell fusion.
@en
P1433
P1476
P2093
P2860
P2888
P304
P31
P356
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
HIV gp41 six-helix bundle cons ...... ions for HIV-host cell fusion.
@en
P2093
P2860
P2888
P304
P31
P356
P433
P478
P577
P5875
P698
P932