The HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranes
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On the Selective Packaging of Genomic RNA by HIV-1Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.Hydrodynamic and Membrane Binding Properties of Purified Rous Sarcoma Virus Gag Protein.HIV-1 Nucleocapsid Mimics the Membrane Adaptor Syntenin PDZ to Gain Access to ESCRTs and Promote Virus BuddingMembrane Binding of HIV-1 Matrix Protein: Dependence on Bilayer Composition and Protein Lipidation.Glutamic Acid Residues in HIV-1 p6 Regulate Virus Budding and Membrane Association of Gag.Self assembly of HIV-1 Gag protein on lipid membranes generates PI(4,5)P2/Cholesterol nanoclustersHIV-1 Pr55Gag binds genomic and spliced RNAs with different affinity and stoichiometry.
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The HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranes
description
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name
The HIV-1 nucleocapsid protein ...... mal binding to lipid membranes
@en
type
label
The HIV-1 nucleocapsid protein ...... mal binding to lipid membranes
@en
prefLabel
The HIV-1 nucleocapsid protein ...... mal binding to lipid membranes
@en
P2093
P2860
P356
P1433
P1476
The HIV-1 nucleocapsid protein ...... mal binding to lipid membranes
@en
P2093
Hugues de Rocquigny
Noémie Kempf
Pascal Didier
Saurabh Bora
Viktoriia Postupalenko
Youri Arntz
P2860
P304
P356
10.1128/JVI.02931-14
P407
P577
2014-11-19T00:00:00Z