Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
about
Structural dynamics of native and V260E mutant C-terminal domain of HIV-1 integrase.C-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.All-atom models of the membrane-spanning domain of HIV-1 gp41 from metadynamics.The membrane-spanning domain of gp41 plays a critical role in intracellular trafficking of the HIV envelope protein.Highly conserved structural properties of the C-terminal tail of HIV-1 gp41 protein despite substantial sequence variation among diverse clades: implications for functions in viral replication.Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid bindingNeutralizing epitopes in the membrane-proximal external region of HIV-1 gp41 are influenced by the transmembrane domain and the plasma membrane.The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External RegionHIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.T-cell antigen receptor (TCR) transmembrane peptides: A new paradigm for the treatment of autoimmune diseases.Computer-Aided Approaches for Targeting HIVgp41.Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.The cholesterol-binding motif of the HIV-1 glycoprotein gp41 regulates lateral sorting and oligomerization.The conformational feasibility for the formation of reaching dimer in ASV and HIV integrase: a molecular dynamics study.Conserved arginine residue in the membrane-spanning domain of HIV-1 gp41 is required for efficient membrane fusionThe dynamics of interconverting D- and E-forms of the HIV-1 integrase N-terminal domain.Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assayConformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.
P2860
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P2860
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 21 June 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
@en
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
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type
label
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
@en
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
@nl
prefLabel
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
@en
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
@nl
P2093
P2860
P1476
Molecular dynamics studies of the transmembrane domain of gp41 from HIV-1.
@en
P2093
A Rachael Curran
Donald M Engelman
Jong Hwa Kim
Taryn L Hartley
P2860
P304
P356
10.1016/J.BBAMEM.2009.06.011
P407
P577
2009-06-21T00:00:00Z