Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 gag polyprotein.
about
Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle releaseHIV type 1 Gag as a target for antiviral therapyVirus maturation as a new HIV-1 therapeutic targetPharmacological intervention of HIV-1 maturationThe choreography of HIV-1 proteolytic processing and virion assemblyAlkyl Amine Bevirimat Derivatives Are Potent and Broadly Active HIV-1 Maturation Inhibitors.Mutational analysis of the octapeptide sequence motif at the NS1-NS2A cleavage junction of dengue type 4 virusStructural and functional insights into the HIV-1 maturation inhibitor binding pocketStructure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396Analysis of Rous sarcoma virus Gag protein by mass spectrometry indicates trimming by host exopeptidase.In vitro protease cleavage and computer simulations reveal the HIV-1 capsid maturation pathway.Replacement of the P1 amino acid of human immunodeficiency virus type 1 Gag processing sites can inhibit or enhance the rate of cleavage by the viral proteaseNovel approaches to inhibiting HIV-1 replication.Investigation of the structure and dynamics of the capsid-spacer peptide 1-nucleocapsid fragment of the HIV-1 gag polyprotein by solution NMR spectroscopyThe capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation.Phosphorylation and proteolytic cleavage of gag proteins in budded simian immunodeficiency virus.Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV- 1 maturation inhibitor bevirimatp6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expressing proteaseConstruction and characterization of chimeric BHIV (BIV/HIV-1) viruses carrying the bovine immunodeficiency virus gag gene.Hydrogen bonding at a conserved threonine in lentivirus capsid is required for virus replication.Removal of human immunodeficiency virus type 1 (HIV-1) protease inhibitors from preparations of immature HIV-1 virions does not result in an increase in infectivity or the appearance of mature morphologyIn vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (Bevirimat).Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.Genetic analysis of the major homology region of the Rous sarcoma virus Gag protein.Aberrant Gag protein composition of a human immunodeficiency virus type 1 vif mutant produced in primary lymphocytesDifferential proteolytic processing leads to multiple forms of the CA protein in avian sarcoma and leukemia viruses.Determinants of the human immunodeficiency virus type 1 p15NC-RNA interaction that affect enhanced cleavage by the viral protease.Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease.Development of a novel anti-HIV-1 agent from within: effect of chimeric Vpr-containing protease cleavage site residues on virus replicationCleavage of p15 protein in vitro by human immunodeficiency virus type 1 protease is RNA dependent.Necessity of the spacer peptide between CA and NC in the Rous sarcoma virus gag proteinEfavirenz enhances HIV-1 gag processing at the plasma membrane through Gag-Pol dimerizationExpression of virus-encoded proteinases: functional and structural similarities with cellular enzymesImpact of human immunodeficiency virus type 1 resistance to protease inhibitors on evolution of resistance to the maturation inhibitor bevirimat (PA-457)Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites.Resistance-associated loss of viral fitness in human immunodeficiency virus type 1: phenotypic analysis of protease and gag coevolution in protease inhibitor-treated patients.Changes in human immunodeficiency virus type 1 Gag at positions L449 and P453 are linked to I50V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro.A structurally disordered region at the C terminus of capsid plays essential roles in multimerization and membrane binding of the gag protein of human immunodeficiency virus type 1.The spacer peptide between human immunodeficiency virus capsid and nucleocapsid proteins is essential for ordered assembly and viral infectivityHuman immunodeficiency virus type 1 (HIV-1) protein Vif inhibits the activity of HIV-1 protease in bacteria and in vitro.
P2860
Q24563651-BD8E3ADF-FBEC-4836-8D83-30E6C5BF6106Q24614498-CFAFC256-3CDC-4519-BC39-4BC80B18B174Q24642446-25525907-3A1C-44A9-BC79-622D13D6AB6DQ26771739-C1DF15F7-5CCC-4F73-85F6-DC3D4ACDECC2Q27009643-872B4B87-7A11-4B90-8CCD-F9D30A50034AQ27324263-0D3043E1-9165-45F5-B2B2-B8313040649AQ27486202-E50F38B7-2782-4C5D-BF1E-51B107D3E28EQ28485054-BC497BB8-E78A-4119-A816-C9AEEBC6A39EQ28828191-EE29CCFD-0D25-49B0-B6FB-A78C2CADA24DQ30423782-2D03142F-FA53-400D-8478-F8D972525124Q30832180-A1CCBCC6-276B-41A8-8C7C-9A7B16555DF2Q30850215-CAADD15C-54E6-4199-9649-B5C7B91BE64BQ33624690-894E793D-E4A8-459F-A9F9-66F1B5072C62Q33724969-ED78B390-5240-48C9-A87F-2D5B563671D5Q33727091-AD4FFB72-BB72-4987-B3A9-B12B81FDF7F9Q33781019-5C2A059D-00C4-4A37-A9DF-D4F322B2573EQ33864444-C11F5FA8-127F-4704-93B1-62617CD1B63BQ34288376-E183AAA5-CFC2-46EB-9A68-3213D8A35ABFQ35010631-F6AC426E-07B2-4CD1-AF2D-1B7418934A7EQ35104668-E0AEF866-718C-457A-83D7-F8168E71B541Q35135963-8D04570A-1190-4D47-AAB3-CE4F9A1DD98AQ35139703-CBE6BBBC-E0CC-4CFD-BBB9-F075F118AABBQ35212464-66D0FAF5-5AC7-46B1-9301-198FCCC51D90Q35841323-567ED7D8-97AB-4D89-BBB0-FF4C7EDCC086Q35842465-A37F1F02-6337-4056-9266-49F275A42907Q35848720-BDD99494-94E8-4FE9-A4F6-F2C40B2BE1CEQ35889311-8DB454CC-6985-4F85-A95E-1446A737590EQ35921690-19166CB0-415E-46D7-BE42-865100774F09Q36085386-CA7EC04A-3773-4999-9EC8-CC692D022AAAQ36635813-59DFE0FA-CA0C-46B9-9993-3CB9D8B3C5F5Q36653886-9DB7BF12-5E1C-41AF-919F-CC6EB7AB505CQ36667876-CED4D668-4812-4DAF-B65C-DD8F0015B831Q37059742-54237071-A88C-46B3-A486-D39164A5836BQ37192174-8518A3FA-003B-4D11-9A6C-48A19B7ECAEAQ39579012-E527C3F6-16DF-4FF5-BE87-AB88E00B3D33Q39580564-D639F7DE-2C3D-407D-922D-3C94F4558043Q39684211-F762E962-4F1E-4E35-82B2-4FC7B8338481Q39699793-43870B7C-9DCF-4F27-BAC7-E5B7E856A536Q39870242-29252566-80B8-4A68-99D7-1C94AF8C8F18Q39880472-DF7724AC-4FCA-4F6D-B605-ADC8D26EA77D
P2860
Mutagenesis of protease cleavage sites in the human immunodeficiency virus type 1 gag polyprotein.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Mutagenesis of protease cleava ...... virus type 1 gag polyprotein.
@en
type
label
Mutagenesis of protease cleava ...... virus type 1 gag polyprotein.
@en
prefLabel
Mutagenesis of protease cleava ...... virus type 1 gag polyprotein.
@en
P2093
P2860
P1433
P1476
Mutagenesis of protease cleava ...... virus type 1 gag polyprotein.
@en
P2093
Erickson-Viitanen S
P2860
P304
P407
P577
1991-02-01T00:00:00Z