CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol.
about
Membrane remodeling and mechanics: Experiments and simulations of α-SynucleinC-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.Freezing point depression of water in phospholipid membranes: a solid-state NMR study.The cholesterol recognition/interaction amino acid consensus motif of the influenza A virus M2 protein is not required for virus replication but contributes to virulence.Model-based approaches for the determination of lipid bilayer structure from small-angle neutron and X-ray scattering data.Fusion-competent state induced by a C-terminal HIV-1 fusion peptide in cholesterol-rich membranes.Membrane-proximal external HIV-1 gp41 motif adapted for destabilizing the highly rigid viral envelopeIn Vivo Analysis of Infectivity, Fusogenicity, and Incorporation of a Mutagenic Viral Glycoprotein Library Reveals Determinants for Virus IncorporationAccurate predictions of population-level changes in sequence and structural properties of HIV-1 Env using a volatility-controlled diffusion model.The Chlamydia trachomatis CT149 protein exhibits esterase activity in vitro and catalyzes cholesteryl ester hydrolysis when expressed in HeLa cells.Membrane structure correlates to function of LLP2 on the cytoplasmic tail of HIV-1 gp41 protein.Large changes in the CRAC segment of gp41 of HIV do not destroy fusion activity if the segment interacts with cholesterol.Effect of cholesterol on structural and mechanical properties of membranes depends on lipid chain saturation.Cholesterol-induced suppression of membrane elastic fluctuations at the atomistic level.Determination of bending rigidity and tilt modulus of lipid membranes from real-space fluctuation analysis of molecular dynamics simulations.Cholesterol crystal induced arterial inflammation and destabilization of atherosclerotic plaque.Use of a Cholesterol Recognition Amino Acid Consensus Peptide To Inhibit Binding of a Bacterial Toxin to Cholesterol.Influence of cholesterol and β-sitosterol on the structure of EYPC bilayers.The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function
P2860
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P2860
CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
CRAC motif peptide of the HIV- ...... nd interacts with cholesterol.
@ast
CRAC motif peptide of the HIV- ...... nd interacts with cholesterol.
@en
type
label
CRAC motif peptide of the HIV- ...... nd interacts with cholesterol.
@ast
CRAC motif peptide of the HIV- ...... nd interacts with cholesterol.
@en
prefLabel
CRAC motif peptide of the HIV- ...... nd interacts with cholesterol.
@ast
CRAC motif peptide of the HIV- ...... nd interacts with cholesterol.
@en
P2093
P2860
P50
P1476
CRAC motif peptide of the HIV- ...... and interacts with cholesterol
@en
P2093
Alexander I Greenwood
Jianjun Pan
Thalia T Mills
P2860
P304
P356
10.1016/J.BBAMEM.2008.01.008
P407
P577
2008-01-16T00:00:00Z