Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention.
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Insertion of a small peptide of six amino acids into the beta7-beta8 loop of the p51 subunit of HIV-1 reverse transcriptase perturbs the heterodimer and affects its activities.Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formationStructural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic InstabilityPotent nonnucleoside reverse transcriptase inhibitors target HIV-1 Gag-PolThe y271 and i274 amino acids in reverse transcriptase of human immunodeficiency virus-1 are critical to protein stabilityRNA-protein interactions govern antiviral specificity and encapsidation of broad spectrum anti-HIV reverse transcriptase aptamersAnalysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation.Construction and characterization of a temperature-sensitive human immunodeficiency virus type 1 reverse transcriptase mutantMutations that abrogate human immunodeficiency virus type 1 reverse transcriptase dimerization affect maturation of the reverse transcriptase heterodimer.Analysis of human immunodeficiency virus type 1 reverse transcriptase subunit structure/function in the context of infectious virions and human target cells.Domain structure of the human immunodeficiency virus reverse transcriptase.Functional multimerization of the human telomerase reverse transcriptase.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.Conformational changes in HIV-1 reverse transcriptase induced by nonnucleoside reverse transcriptase inhibitor binding.Selective killing of human immunodeficiency virus infected cells by non-nucleoside reverse transcriptase inhibitor-induced activation of HIV protease.Subunit-specific analysis of the human immunodeficiency virus type 1 reverse transcriptase in vivo.Multiparameter single-molecule fluorescence spectroscopy reveals heterogeneity of HIV-1 reverse transcriptase:primer/template complexes.Structural basis of asymmetry in the human immunodeficiency virus type 1 reverse transcriptase heterodimerThe p66 immature precursor of HIV-1 reverse transcriptase.Analysis of mutations and suppressors affecting interactions between the subunits of the HIV type 1 reverse transcriptaseHuman immunodeficiency virus-1 reverse transcriptase heterodimer stability.Molecular matchmaking: NNRTIs can enhance the dimerization of HIV type 1 reverse transcriptase.Hydroxyl radical footprint analysis of human immunodeficiency virus reverse transcriptase-template.primer complexes.Structure-activity relationships in HIV-1 reverse transcriptase revealed by radiation target analysisUnfolding the HIV-1 reverse transcriptase RNase H domain--how to lose a molecular tug-of-war.Purification and characterization of an active human immunodeficiency virus type 1 RNase H domain.Mutational analysis of the fingers domain of human immunodeficiency virus type 1 reverse transcriptase.Cassette mutagenesis of the reverse transcriptase of human immunodeficiency virus type 1.Two highly antigenic sites in the human immunodeficiency virus type 1 reverse transcriptase.HIV-1 protease dimer interface mutations that compensate for viral reverse transcriptase instability in infectious virions.Mutations in HIV-1 reverse transcriptase cause misfolding and miscleavage by the viral protease.Regulation of the reverse transcriptase of human immunodeficiency virus type 1 by dNTPs.Human immunodeficiency virus type 1 reverse transcriptase: spatial and temporal relationship between the polymerase and RNase H activitiesEnzyme activities in four different forms of human immunodeficiency virus 1 pol gene products.The p15 carboxyl-terminal proteolysis product of the human immunodeficiency virus type 1 reverse transcriptase p66 has DNA polymerase activityEndogenous expression of a high-affinity pseudoknot RNA aptamer suppresses replication of HIV-1.The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse transcriptase and inhibits its function during viral replication.Human T-cell leukemia virus type 1 reverse transcriptase (RT) originates from the pro and pol open reading frames and requires the presence of RT-RNase H (RH) and RT-RH-integrase proteins for its activity.Asymmetric subunit organization of heterodimeric Rous sarcoma virus reverse transcriptase alphabeta: localization of the polymerase and RNase H active sites in the alpha subunit.Functional multimerization of human telomerase requires an RNA interaction domain in the N terminus of the catalytic subunit.
P2860
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P2860
Dimerization of human immunodeficiency virus type 1 reverse transcriptase. A target for chemotherapeutic intervention.
description
1990 nî lūn-bûn
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1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
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1990年学术文章
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1990年学术文章
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1990年学术文章
@zh-my
1990年学术文章
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1990年學術文章
@zh-hant
name
Dimerization of human immunode ...... chemotherapeutic intervention.
@en
Dimerization of human immunode ...... chemotherapeutic intervention.
@nl
type
label
Dimerization of human immunode ...... chemotherapeutic intervention.
@en
Dimerization of human immunode ...... chemotherapeutic intervention.
@nl
prefLabel
Dimerization of human immunode ...... chemotherapeutic intervention.
@en
Dimerization of human immunode ...... chemotherapeutic intervention.
@nl
P1476
Dimerization of human immunode ...... chemotherapeutic intervention
@en
P2093
P304
P407
P577
1990-06-01T00:00:00Z