Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.
about
Genome-wide screening, cloning, chromosomal assignment, and expression of full-length human endogenous retrovirus type KThe viruses in all of us: characteristics and biological significance of human endogenous retrovirus sequencesAssembly and processing of human immunodeficiency virus Gag mutants containing a partial replacement of the matrix domain by the viral protease domainVirion instability of human immunodeficiency virus type 1 reverse transcriptase (RT) mutated in the protease cleavage site between RT p51 and the RT RNase H domain.Reversal by dithiothreitol treatment of the block in murine leukemia virus maturation induced by disulfide cross-linkingProline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.Altered gag polyprotein cleavage specificity of feline immunodeficiency virus/human immunodeficiency virus mutant proteases as demonstrated in a cell-based expression system.The central globular domain of the nucleocapsid protein of human immunodeficiency virus type 1 is critical for virion structure and infectivityA critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.A p6Pol-protease fusion protein is present in mature particles of human immunodeficiency virus type 1.Altered Rous sarcoma virus Gag polyprotein processing and its effects on particle formation.HIV Assembly and Budding: Ca(2+) Signaling and Non-ESCRT Proteins Set the Stage.Human immunodeficiency virus type 1 protease regulation of tat activity is essential for efficient reverse transcription and replication.Uncoupling human immunodeficiency virus type 1 Gag and Pol reading frames: role of the transframe protein p6* in viral replication.Autoprocessing: an essential step for the activation of HIV-1 protease.Cleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity.Ty1 proteolytic cleavage sites are required for transposition: all sites are not created equal.Importance of the N terminus of rous sarcoma virus protease for structure and enzymatic function.HIV-1 protease inhibits its homologous reverse transcriptase by protein-protein interaction.Domains upstream of the protease (PR) in human immunodeficiency virus type 1 Gag-Pol influence PR autoprocessingAnalysis of cleavage site mutations between the NC and PR Gag domains of Rous sarcoma virusImportance of protease cleavage sites within and flanking human immunodeficiency virus type 1 transframe protein p6* for spatiotemporal regulation of protease activation.
P2860
Q24527314-5CE79321-8606-472C-BDD9-83AC608294E9Q24606140-67C5896A-DFF7-4E7D-9174-D21AAD2FEFE2Q33801779-786F347E-1E9A-4FDD-8B25-3B3A9016130CQ33987368-8D241F08-3930-44F2-A126-4514D043D730Q34347815-FF54E8BB-EB8C-44D2-A0B4-5A23EB536849Q34354549-B402DEA8-76B9-42F8-93F4-65E988F7E066Q35024024-72E8845C-CC4E-4DC3-960E-9C429AF3C7EFQ35834904-2BAE5DCA-DAC7-42E8-A2A1-FD9B7C8AF9E0Q35866466-9E370C71-63BE-4953-BF0E-55D7E44C1934Q35871101-EDD9FE84-27DD-448B-BE30-BBC894F5CDD0Q35878241-5548E834-4F0C-4728-9568-2A6FA392F569Q36063560-27434C2F-F3CF-47A6-8308-E4C2A1763B5AQ36464170-072B6006-8DEA-4384-A430-2C6A3B6F2FB2Q37248021-B797F435-2C3C-4A1B-9F8A-988705A59B16Q38357144-D5A980CD-B643-4793-8782-2B3E341E15DEQ39579642-128B0436-8139-4D0F-B7F2-8CD1E4252F83Q39601419-283F41D9-11EE-49F5-A4D9-AC5EAFE9E1F0Q39602769-3283A8A6-F995-4F25-B7B0-931843E318B6Q39719925-BBD0A373-1FAA-4630-86B6-782152A8E89FQ39870468-F9721DE2-4ACB-413C-A43D-45EFF4DEF4CDQ39877732-17C0C283-053A-48AA-9E0E-6B0C64B98E31Q40005589-5DD2A60F-53BC-4CDE-B9C1-CFF8E5E0A3DB
P2860
Proteolytic activity of novel human immunodeficiency virus type 1 proteinase proteins from a precursor with a blocking mutation at the N terminus of the PR domain.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Proteolytic activity of novel ...... e N terminus of the PR domain.
@ast
Proteolytic activity of novel ...... e N terminus of the PR domain.
@en
type
label
Proteolytic activity of novel ...... e N terminus of the PR domain.
@ast
Proteolytic activity of novel ...... e N terminus of the PR domain.
@en
prefLabel
Proteolytic activity of novel ...... e N terminus of the PR domain.
@ast
Proteolytic activity of novel ...... e N terminus of the PR domain.
@en
P2093
P2860
P1433
P1476
Proteolytic activity of novel ...... he N terminus of the PR domain
@en
P2093
H G Kräusslich
P2860
P304
P407
P577
1994-01-01T00:00:00Z