Mutation of amino acids in the connection domain of human immunodeficiency virus type 1 reverse transcriptase that contact the template-primer affects RNase H activity.
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The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate bindingRNase H activity: structure, specificity, and function in reverse transcriptionRibonuclease H: properties, substrate specificity and roles in retroviral reverse transcriptionConservation of functional domains and limited heterogeneity of HIV-1 reverse transcriptase gene following vertical transmissionConservation patterns of HIV-1 RT connection and RNase H domains: identification of new mutations in NRTI-treated patientsVirtual screening models for prediction of HIV-1 RT associated RNase H inhibitionVinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activityMultiple nucleotide preferences determine cleavage-site recognition by the HIV-1 and M-MuLV RNases H.A novel molecular mechanism of dual resistance to nucleoside and nonnucleoside reverse transcriptase inhibitors.HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors.The "Connection" Between HIV Drug Resistance and RNase HRevisiting plus-strand DNA synthesis in retroviruses and long terminal repeat retrotransposons: dynamics of enzyme: substrate interactions.SiRNA-induced mutation in HIV-1 polypurine tract region and its influence on viral fitness.Mutations in the connection domain of HIV-1 reverse transcriptase increase 3'-azido-3'-deoxythymidine resistanceMutations in human immunodeficiency virus type 1 RNase H primer grip enhance 3'-azido-3'-deoxythymidine resistance.Selection of mutations in the connection and RNase H domains of human immunodeficiency virus type 1 reverse transcriptase that increase resistance to 3'-azido-3'-dideoxythymidine.Changes in simian immunodeficiency virus reverse transcriptase alleles that appear during infection of macaques enhance infectivity and replication in CD4+ T cells.Human immunodeficiency virus reverse transcriptase: 25 years of research, drug discovery, and promise.Effect of translocation defective reverse transcriptase inhibitors on the activity of N348I, a connection subdomain drug resistant HIV-1 reverse transcriptase mutant.Inhibitors of HIV-1 Reverse Transcriptase-Associated Ribonuclease H Activity.Tighter binding of HIV reverse transcriptase to RNA-DNA versus DNA-DNA results mostly from interactions in the polymerase domain and requires just a small stretch of RNA-DNA.Examining the role of the HIV-1 reverse transcriptase p51 subunit in positioning and hydrolysis of RNA/DNA hybridsAlizarine derivatives as new dual inhibitors of the HIV-1 reverse transcriptase-associated DNA polymerase and RNase H activities effective also on the RNase H activity of non-nucleoside resistant reverse transcriptases.Examining the ribonuclease H primer grip of HIV-1 reverse transcriptase by charge neutralization of RNA/DNA hybridsMolecular mechanism of HIV-1 resistance to 3'-azido-2',3'-dideoxyguanosine.Interaction of the Ty3 reverse transcriptase thumb subdomain with template-primer.Two modes of HIV-1 polypurine tract cleavage are affected by introducing locked nucleic acid analogs into the (-) DNA template.Insights into the structure and activity of prototype foamy virus RNase H.Structural requirements for enzymatic activities of foamy virus protease-reverse transcriptase.Evolutionary Analysis of HIV-1 Pol Proteins Reveals Representative Residues for Viral Subtype Differentiation.
P2860
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P2860
Mutation of amino acids in the connection domain of human immunodeficiency virus type 1 reverse transcriptase that contact the template-primer affects RNase H activity.
description
2003 nî lūn-bûn
@nan
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Mutation of amino acids in the ...... imer affects RNase H activity.
@ast
Mutation of amino acids in the ...... imer affects RNase H activity.
@en
type
label
Mutation of amino acids in the ...... imer affects RNase H activity.
@ast
Mutation of amino acids in the ...... imer affects RNase H activity.
@en
prefLabel
Mutation of amino acids in the ...... imer affects RNase H activity.
@ast
Mutation of amino acids in the ...... imer affects RNase H activity.
@en
P2093
P2860
P50
P1433
P1476
Mutation of amino acids in the ...... rimer affects RNase H activity
@en
P2093
Edward Arnold
John G Julias
W Gregory Alvord
P2860
P304
P356
10.1128/JVI.77.15.8548-8554.2003
P407
P577
2003-08-01T00:00:00Z