about
Coordination of Genomic RNA Packaging with Viral Assembly in HIV-1HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchThe matrix domain contributes to the nucleic acid chaperone activity of HIV-2 Gag.The Life-Cycle of the HIV-1 Gag-RNA ComplexEffect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMRRoles played by acidic lipids in HIV-1 Gag membrane bindingMultifunctional nature of the arenavirus RING finger protein Z.Membrane binding and subcellular localization of retroviral Gag proteins are differentially regulated by MA interactions with phosphatidylinositol-(4,5)-bisphosphate and RNA.Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology DomainHIV-2 genome dimerization is required for the correct processing of Gag: a second-site reversion in matrix can restore both processes in dimerization-impaired mutant virusesDynamic Association between HIV-1 Gag and Membrane Domains.Analysis of small molecule ligands targeting the HIV-1 matrix protein-RNA binding site.Investigation of the HIV-1 matrix interactome during virus replication.Elucidating the mechanism by which compensatory mutations rescue an HIV-1 matrix mutant defective for gag membrane targeting and envelope glycoprotein incorporation.Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells.Trimer Enhancement Mutation Effects on HIV-1 Matrix Protein Binding Activities.Reconstitution of selective HIV-1 RNA packaging in vitro by membrane-bound Gag assemblies.Methods to Study Determinants for Membrane Targeting of HIV-1 Gag In Vitro.Interrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association.Phosphoinositides as regulators of protein-chromatin interactions.Membrane interaction of retroviral Gag proteins.The roles of lipids and nucleic acids in HIV-1 assemblyThe HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranesExosomes from uninfected cells activate transcription of latent HIV-1.Effect of multimerization on membrane association of Rous sarcoma virus and HIV-1 matrix domain proteins.Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages.Analysis of HIV-1 Gag protein interactions via biotin ligase tagging.Synchronized HIV assembly by tunable PIP2 changes reveals PIP2 requirement for stable Gag anchoring.Inhibition of HIV-1 Gag-membrane interactions by specific RNAs.HIV-1 Pr55Gag binds genomic and spliced RNAs with different affinity and stoichiometry.Analysis of quinolinequinone reactivity, cytotoxicity, and anti-HIV-1 properties.A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In VitroBasic motifs target PSGL-1, CD43, and CD44 to plasma membrane sites where HIV-1 assembles.Inositol phosphates compete with nucleic acids for binding to bovine leukemia virus matrix protein: implications for deltaretroviral assembly.
P2860
Q26739673-4F2C892C-A994-470C-8E2D-15397E1D9928Q26746070-E428A2A5-0A1A-412D-A3D1-E91577B575FDQ27303006-4C8155A9-A0A7-4054-AFEB-EB9B50B3F73DQ28076985-7EA0CF41-2B26-457B-ACF3-9B493D56CED9Q28554716-E13E4945-A3E9-401A-8624-36116F0C3BFEQ34615838-D89C0B5C-2F34-49C4-BD63-8285AD148FE0Q34645925-2FB7D7A1-597D-4616-9C41-3824FD43D706Q35072137-6C9E1EB8-6668-4820-ADCF-E4A638E2EA2AQ35199166-3F55284A-D17F-4B36-B1C8-312A2AEC5E1CQ35761675-E5BC9874-4613-4285-B4B5-E9140BFE3C5EQ35861246-9FF54E4C-7D62-477C-9F08-AF67986AAD6AQ35943592-6B779B07-3FC8-4303-B6D6-3FCD3B6BFA1FQ36102200-34295070-8127-4B3E-9271-24B0DB3C81CBQ36508756-FD778AD8-4F22-4D0B-B495-A386736283E9Q36535838-1EECC8FD-A841-4FC7-971A-C7C33874EB42Q36833301-EB5E1D82-5DB5-410B-8D96-9EDD3DB94320Q36911677-0278D38E-F6E2-4036-8C01-F68067DB73A4Q36950860-B7938036-E6C7-4BBC-8824-AB673B83D064Q37098853-64343A77-BF1A-46D3-8FB6-36AA2E0E147BQ37272001-0A2B74C7-DB5D-43B1-BF0A-7560B3C7DD74Q37633410-C2C75FF7-A5D7-46D8-ABDD-927255A2684CQ38006941-23A70895-4C2C-434A-A56F-57AEE04C985FQ38210206-DDD156C7-A378-49D0-A682-E529E58260FDQ38219405-08A8A4E1-2EE0-4F99-8574-C02B9B8A2ECBQ38302959-96B5F8AD-6E29-4DAA-A919-A445FE1B4A60Q38702490-86102F36-C90C-454F-9FFA-20DD9AFA6F92Q39083964-E49395F0-391B-4907-B939-9629D2C847FBQ39578041-ADB4AE50-DD14-4F10-AF7B-3F96A1917183Q39795056-30F2CEC4-30D0-4254-AA4F-FA73EE5FC592Q40175971-83A75429-566E-4ECB-9C38-DC119C2DDDC0Q40433937-2B0315E6-DAA8-4EDE-8F6E-69EA9057F669Q40476785-43C0746C-F6D8-4122-B6AA-793078D49FEBQ40567901-E2B32343-FDED-4099-88DC-43D30DE4826CQ41730903-0675A9A4-8B35-4F5B-83E6-7BC13CA51880Q41844831-74AB2304-4797-4141-949B-F29428C1BA57Q45352137-2265D298-E24B-44D5-8FBD-194B77746EB0
P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
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
name
HIV-1 matrix protein binding to RNA.
@ast
HIV-1 matrix protein binding to RNA.
@en
type
label
HIV-1 matrix protein binding to RNA.
@ast
HIV-1 matrix protein binding to RNA.
@en
prefLabel
HIV-1 matrix protein binding to RNA.
@ast
HIV-1 matrix protein binding to RNA.
@en
P2093
P2860
P1476
HIV-1 matrix protein binding to RNA
@en
P2093
Ayna Alfadhli
Eric Barklis
Hans Peter Bächinger
Henry McNett
Seyram Tsagli
P2860
P304
P356
10.1016/J.JMB.2011.04.063
P407
P577
2011-07-01T00:00:00Z