Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism.

Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism.

Item
http://www.wikidata.org/entity/Q30558462
The central proline of an internal viral fusion peptide serves two important rolesAllosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivityThe amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility.Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex.The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function.Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike proteinOligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.Potent HIV fusion inhibitors against Enfuvirtide-resistant HIV-1 strainsIdentification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: implications for designing novel anti-HIV fusion inhibitors.Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion.Chemical shift assignment and structural plasticity of a HIV fusion peptide derivative in dodecylphosphocholine micellesA peptide pertaining to the loop segment of human immunodeficiency virus gp41 binds and interacts with model biomembranes: implications for the fusion mechanism.Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.Evidence that the transmembrane domain proximal region of the human T-cell leukemia virus type 1 fusion glycoprotein gp21 has distinct roles in the prefusion and fusion-activated states.Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry.Expression and biochemical analysis of the entire HIV-2 gp41 ectodomain: determinants of stability map to N- and C-terminal sequences outside the 6-helix bundle core.Switching of turn conformation in an aspartate anion peptide fragment by NH . . . O- hydrogen bonds.
P2860

Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism.

Item
http://www.wikidata.org/entity/Q30558462
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Biophysical characterization o ...... ons on viral fusion mechanism.
@ast
Biophysical characterization o ...... ons on viral fusion mechanism.
@en
type
label
Biophysical characterization o ...... ons on viral fusion mechanism.
@ast
Biophysical characterization o ...... ons on viral fusion mechanism.
@en
prefLabel
Biophysical characterization o ...... ons on viral fusion mechanism.
@ast
Biophysical characterization o ...... ons on viral fusion mechanism.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
P356
P1433
P1476
Biophysical characterization o ...... ons on viral fusion mechanism.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921