Roles of matrix, p2, and N-terminal myristoylation in human immunodeficiency virus type 1 Gag assembly.
about
Identification of Staufen in the human immunodeficiency virus type 1 Gag ribonucleoprotein complex and a role in generating infectious viral particlesHIV type 1 Gag as a target for antiviral therapyUnderstanding the process of envelope glycoprotein incorporation into virions in simian and feline immunodeficiency virusesThe interaction between HIV-1 Gag and human lysyl-tRNA synthetase during viral assemblyStructure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assayMobility of human immunodeficiency virus type 1 Pr55Gag in living cells.Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packagingAnalysis of the initiating events in HIV-1 particle assembly and genome packagingExpression of HIV-1 antigens in plants as potential subunit vaccinesHIV-1 Vpr oligomerization but not that of Gag directs the interaction between Vpr and Gag.Novel approaches to inhibiting HIV-1 replication.Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding.Gag-Pol supplied in trans is efficiently packaged and supports viral function in human immunodeficiency virus type 1.Multimerization of human immunodeficiency virus type 1 Gag promotes its localization to barges, raft-like membrane microdomainsBinding of calmodulin to the HIV-1 matrix protein triggers myristate exposure.Myristate exposure in the human immunodeficiency virus type 1 matrix protein is modulated by pH.The TY3 Gag3 spacer controls intracellular condensation and uncoatingRapid localization of Gag/GagPol complexes to detergent-resistant membrane during the assembly of human immunodeficiency virus type 1.Construction and characterization of chimeric BHIV (BIV/HIV-1) viruses carrying the bovine immunodeficiency virus gag gene.Second-site compensatory mutations of HIV-1 capsid mutations.HIV-1 matrix protein binding to RNA.In vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (Bevirimat).Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamerRole of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Atomic Modeling of an Immature Retroviral Lattice Using Molecular Dynamics and Mutagenesis.Overlapping roles of the Rous sarcoma virus Gag p10 domain in nuclear export and virion core morphology.Positive and negative modulation of virus infectivity and envelope glycoprotein incorporation into virions by amino acid substitutions at the N terminus of the simian immunodeficiency virus matrix protein.Incorporation of pol into human immunodeficiency virus type 1 Gag virus-like particles occurs independently of the upstream Gag domain in Gag-polImportant role for the CA-NC spacer region in the assembly of bovine immunodeficiency virus Gag protein.HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphateAnalysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids.The conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 gag protein is important for virion assembly and release.Virus-like particles produced in plants as potential vaccines.The roles of lipids and nucleic acids in HIV-1 assemblyA HIV-1 minimal gag protein is superior to nucleocapsid at in vitro annealing and exhibits multimerization-induced inhibition of reverse transcription.Role of the Rous sarcoma virus p10 domain in shape determination of gag virus-like particles assembled in vitro and within Escherichia coli.Higher-order structure of the Rous sarcoma virus SP assembly domain.Hantavirus nucleocapsid protein oligomerization.Nucleic acid-independent retrovirus assembly can be driven by dimerization.
P2860
Q24599767-26CD8DC6-8419-42CA-84AC-359F9517E355Q24614498-B2DC3E0A-762C-4CE0-B924-051EAF6EBE1CQ27021655-FA0D6ED0-841D-47BD-B79E-E54BE05B7B62Q28205104-6E8C032F-37AB-4E48-B50F-E9A817C4AEE8Q28828191-71DDE4F2-1BD2-40E4-98E3-00FAB52B8CC3Q30447057-23E33F6F-E8F7-4E38-A5F1-E622BF41F99AQ30477939-981D09B4-7C4F-470F-B378-CCF35AC76F07Q30980940-E9A0EC4D-EE0B-4205-8B93-3A01B047A6ABQ30992792-50B3337D-4BF5-4D42-82D2-A92BE00FEE08Q33345905-65061F4B-BAD2-457C-992C-6F827C1B8A38Q33614489-DE0E7888-CC61-4914-8BE2-8E00D1A31A63Q33624690-109106A5-67D1-44BD-923C-741D98246A65Q33787084-0F4440EF-313C-4596-9FE4-C6A0998D97E9Q33844166-7DEB8366-48A7-445B-BE86-090AA0195E61Q33853532-FE937A1F-2DB3-4B9E-8F90-EB6096F7F3AFQ34439020-346F10D8-324C-42D6-A433-93B295ADE435Q34544143-9EECEF36-F501-4036-BEA7-EDA740D82A16Q34742382-8AB78D82-2867-45D6-A3AB-EF13E82E45F0Q34781698-5921F6CF-7A7A-429E-8347-38ACD234D59EQ35010631-F0B0C5C4-48F6-4ADD-B249-FDCD7633F4D6Q35076692-54F2CB7B-F92B-4CE8-BEA6-8C5C7CB307B1Q35114688-548595EF-6350-41E6-AF5E-563F5505CB16Q35139703-49CCEAA1-33D9-4761-9366-EF1F4194E6C4Q35635123-F4941EB0-7D65-4132-8D38-2A0B782166DBQ35761675-066B81AE-40D3-4403-8442-F06A2203FB8CQ35920838-0650506F-0159-42FE-BA10-6D5B42E6A467Q36099007-433E8057-D0B9-47C4-9347-009636060A5EQ36474005-D55478D3-5A43-46A9-8A46-DE1C3854FC7AQ36942505-90E2EA16-E631-4495-BACB-5DFAAE25CDD5Q36943348-29DF24DF-3E87-43AE-A145-9170C11144B9Q37187498-AC9DF047-FFEB-47FC-9A5B-087221010873Q37452038-78639A3E-7FF5-4A5D-92B8-4F445AEAC4C2Q37492757-3B13A752-9223-46AA-91A8-4295C5627F98Q38081975-B845BD8D-C4BD-412F-BC82-6050BEBC4E42Q38219405-C5E25552-B4EF-4224-AAC2-498B1A2C4CA4Q38330143-5BA3A722-E1B1-4513-89E4-697AB90479D9Q39539672-32A38B20-CAA1-439B-9740-C418046B6332Q39549065-745660F1-80E8-4DED-B631-798A9717EEDDQ39607249-45183E7C-4298-46C5-AF65-3C074DFDF05DQ39685711-800CF036-3526-42AF-91B9-BF700676476A
P2860
Roles of matrix, p2, and N-terminal myristoylation in human immunodeficiency virus type 1 Gag assembly.
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@ast
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@en
type
label
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@ast
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@en
prefLabel
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@ast
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@en
P2093
P2860
P1433
P1476
Roles of matrix, p2, and N-ter ...... ncy virus type 1 Gag assembly.
@en
P2093
D J Hockley
M V Nermut
Y Morikawa
P2860
P356
10.1128/JVI.74.1.16-23.2000
P577
2000-01-01T00:00:00Z