Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid.
about
The choreography of HIV-1 proteolytic processing and virion assemblyInvestigation by atomic force microscopy of the structure of Ty3 retrotransposon particles.In vitro selection and characterization of human immunodeficiency virus type 1 variants with increased resistance to ABT-378, a novel protease inhibitor.Second locus involved in human immunodeficiency virus type 1 resistance to protease inhibitorsA look inside HIV resistance through retroviral protease interaction mapsIdentification of the protease cleavage sites in a reconstituted Gag polyprotein of an HERV-K(HML-2) elementMolecular basis for the relative substrate specificity of human immunodeficiency virus type 1 and feline immunodeficiency virus proteases.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 proteaseHelical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packagingAltered substrate specificity of drug-resistant human immunodeficiency virus type 1 protease.Local and spatial factors determining HIV-1 protease substrate recognition.Feline Immunodeficiency Virus Evolutionarily Acquires Two Proteins, Vif and Protease, Capable of Antagonizing Feline APOBEC3The initial step in human immunodeficiency virus type 1 GagProPol processing can be regulated by reversible oxidationA putative alpha-helical structure which overlaps the capsid-p2 boundary in the human immunodeficiency virus type 1 Gag precursor is crucial for viral particle assemblyFeline immunodeficiency virus (FIV) as a model for study of lentivirus infections: parallels with HIV.Sequences in the cytoplasmic tail of the gibbon ape leukemia virus envelope protein that prevent its incorporation into lentivirus vectorsProteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation.Complementation of integrase function in HIV-1 virions.Comprehensive bioinformatic analysis of the specificity of human immunodeficiency virus type 1 protease.Virion 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.The TY3 Gag3 spacer controls intracellular condensation and uncoatingCooperative cleavage of the R peptide in the Env trimer of Moloney murine leukemia virus facilitates its maturation for fusion competence.Coevolutionary analysis of resistance-evading peptidomimetic inhibitors of HIV-1 protease.A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.Context-Dependent Cleavage of the Capsid Protein by the West Nile Virus Protease Modulates the Efficiency of Virus AssemblyContext 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.A proposal for a new HIV-1 DLS structural model.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.Effect of linker insertion mutations in the human immunodeficiency virus type 1 gag gene on activation of viral protease expressed in bacteriaMutational analysis of the major homology region of Mason-Pfizer monkey virus by use of saturation mutagenesisMolecular mechanisms of FIV infection.A viral protease-mediated cleavage of the transmembrane glycoprotein of Mason-Pfizer monkey virus can be suppressed by mutations within the matrix protein.Nucleocapsid protein function in early infection processes.How to find simple and accurate rules for viral protease cleavage specificities.Comparative studies on retroviral proteases: substrate specificity.Sequential steps in human immunodeficiency virus particle maturation revealed by alterations of individual Gag polyprotein cleavage sites.Compensatory point mutations in the human immunodeficiency virus type 1 Gag region that are distal from deletion mutations in the dimerization initiation site can restore viral replicationCleavage of human immunodeficiency virus type 1 proteinase from the N-terminally adjacent p6* protein is essential for efficient Gag polyprotein processing and viral infectivity.Evidence for a stable interaction of gp41 with Pr55(Gag) in immature human immunodeficiency virus type 1 particles.Ty1 proteolytic cleavage sites are required for transposition: all sites are not created equal.
P2860
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P2860
Analysis of retroviral protease cleavage sites reveals two types of cleavage sites and the structural requirements of the P1 amino acid.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh-hant
name
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@en
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@nl
type
label
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@en
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@nl
prefLabel
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@en
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@nl
P2093
P1476
Analysis of retroviral proteas ...... irements of the P1 amino acid.
@en
P2093
Hutchison CA 3rd
Swanstrom R
P304
14539-14547
P407
P577
1991-08-01T00:00:00Z