Structural interactions between retroviral Gag proteins examined by cysteine cross-linking
about
Virus particle core defects caused by mutations in the human immunodeficiency virus capsid N-terminal domainAssembly of retrovirus capsid-nucleocapsid proteins in the presence of membranes or RNA.Structural analysis of membrane-bound retrovirus capsid proteins.Analysis of human immunodeficiency virus type 1 Gag dimerization-induced assemblyAtomic force microscopy and electron microscopy analysis of retrovirus Gag proteins assembled in vitro on lipid bilayers.Effects of Gag mutation and processing on retroviral dimeric RNA maturation.Nucleocapsid protein effects on the specificity of retrovirus RNA encapsidation.Analysis of the N-terminal region of the murine leukemia virus nucleocapsid proteinDefects in virion production caused by mutations affecting the C-terminal portion of the Moloney murine leukemia virus capsid protein.Molecular organization of Mason-Pfizer monkey virus capsids assembled from Gag polyprotein in Escherichia coli.Second-site compensatory mutations of HIV-1 capsid mutations.Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo.Structural analysis of human immunodeficiency virus type 1 Gag protein interactions, using cysteine-specific reagentsQuantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulersCapsid is an important determinant for functional complementation of murine leukemia virus and spleen necrosis virus Gag proteinsAnalysis of human immunodeficiency virus matrix domain replacements.Hantavirus nucleocapsid protein oligomerization.trans-acting proteins involved in RNA encapsidation and viral assembly in human immunodeficiency virus type 1.Murine leukemia virus particle assembly quantitated by fluorescence microscopy: role of Gag-Gag interactions and membrane associationAnalysis of quinolinequinone reactivity, cytotoxicity, and anti-HIV-1 properties.TR1.3 viral pathogenesis and syncytium formation are linked to Env-Gag cooperation.
P2860
Q33718140-CB003F3C-C5DE-4E26-ABE4-96BEF2F26A17Q33809649-D357A6E5-F58E-433D-8712-3AA24AF4B282Q33886226-38723B0C-783A-4880-9C33-83AE3F20CFB7Q34142733-51311D5E-EC3F-4E18-86FD-D2B04D8C821DQ34172241-C778B67D-95A2-4BE6-908A-B7C01B8FFA70Q34302140-BC5150B9-9B6E-487B-9F5F-E521CED63EFDQ34302330-FDB2ECF3-0164-4868-94DF-56B616663FE4Q34552402-F7F08E95-581C-4C50-8F02-D9EA6B140506Q34755046-AD693BAF-98A2-4DED-BD5D-45B5D2FF36C2Q34999719-7225A797-7B8E-4929-83E5-86C70BD85AE5Q35076692-B5949FAE-64F7-41FD-8F74-E2C6EBF0405FQ35848783-D8CFB96B-B832-48FD-B681-19FB594A3FDEQ35865879-6F15F178-F857-477C-B7FE-65E5213E68DEQ36640538-8FEEE6CF-7377-4274-B168-23BF9C873991Q37252303-1FD4BC1B-AC8E-4D17-B652-C4CE3994B927Q37255552-281620D1-8378-471E-9FBD-E83C0C5DDE70Q39607249-DCF01A68-0F1D-459C-B796-BB9FC81A08EDQ39873362-9468AF4E-554D-4929-82E9-63F2D0C4C5E4Q40011798-C7EC5F94-F240-4F1F-AA43-9682B02849F4Q40567901-08F68ECA-FBE6-4B60-98B3-6E722AAE5314Q42638352-1F3CA971-E6ED-4C19-9843-FABF8EC62541
P2860
Structural interactions between retroviral Gag proteins examined by cysteine cross-linking
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Structural interactions betwee ...... ined by cysteine cross-linking
@ast
Structural interactions betwee ...... ined by cysteine cross-linking
@en
type
label
Structural interactions betwee ...... ined by cysteine cross-linking
@ast
Structural interactions betwee ...... ined by cysteine cross-linking
@en
prefLabel
Structural interactions betwee ...... ined by cysteine cross-linking
@ast
Structural interactions betwee ...... ined by cysteine cross-linking
@en
P2860
P1433
P1476
Structural interactions betwee ...... ined by cysteine cross-linking
@en
P2093
P2860
P304
P407
P577
1995-02-01T00:00:00Z