Hydroxyl radical footprint analysis of human immunodeficiency virus reverse transcriptase-template.primer complexes.
about
Functional roles of carboxylate residues comprising the DNA polymerase active site triad of Ty3 reverse transcriptaseTruncating alpha-helix E' of p66 human immunodeficiency virus reverse transcriptase modulates RNase H function and impairs DNA strand transferStructures of complexes formed by HIV-1 reverse transcriptase at a termination site of DNA synthesis.Interactions between HIV-1 reverse transcriptase and the downstream template strand in stable complexes with primer-templateStructural basis for the specificity of the initiation of HIV-1 reverse transcription.Sequence-specific inhibition of human immunodeficiency virus (HIV) reverse transcription by antisense oligonucleotides: comparative study in cell-free assays and in HIV-infected cells.RuvC protein resolves Holliday junctions via cleavage of the continuous (noncrossover) strands.The tRNA primer activation signal in the human immunodeficiency virus type 1 genome is important for initiation and processive elongation of reverse transcriptionSpecific cleavages by RNase H facilitate initiation of plus-strand RNA synthesis by Moloney murine leukemia virus.What is the orientation of DNA polymerases on their templates?Mutations in HIV reverse transcriptase which alter RNase H activity and decrease strand transfer efficiency are suppressed by HIV nucleocapsid proteinBinding of RNA template to a complex of HIV-1 reverse transcriptase/primer/templateStrand displacement synthesis capability of Moloney murine leukemia virus reverse transcriptase.Dynamic binding orientations direct activity of HIV reverse transcriptaseSlide into action: dynamic shuttling of HIV reverse transcriptase on nucleic acid substrates.HIV-1 reverse transcriptase-associated RNase H cleaves RNA/RNA in arrested complexes: implications for the mechanism by which RNase H discriminates between RNA/RNA and RNA/DNAInterference footprinting analysis of telomerase elongation complexes.Broad-spectrum aptamer inhibitors of HIV reverse transcriptase closely mimic natural substrates.Mutating a region of HIV-1 reverse transcriptase implicated in tRNA(Lys-3) binding and the consequences for (-)-strand DNA synthesis.DNA-thumb interactions and processivity of T7 DNA polymerase in comparison to yeast polymerase eta.Differential tolerance to DNA polymerization by HIV-1 reverse transcriptase on N6 adenine C10R and C10S benzo[a]pyrene-7,8-dihydrodiol 9,10-epoxide-adducted templates.Localization of the active site of HIV-1 reverse transcriptase-associated RNase H domain on a DNA template using site-specific generated hydroxyl radicals.Sequence requirements for removal of tRNA by an isolated human immunodeficiency virus type 1 RNase H domainThe 'helix clamp' in HIV-1 reverse transcriptase: a new nucleic acid binding motif common in nucleic acid polymerases.Pausing kinetics dominates strand-displacement polymerization by reverse transcriptase.Interaction of p55 reverse transcriptase from the Saccharomyces cerevisiae retrotransposon Ty3 with conformationally distinct nucleic acid duplexes.Substitutions of Phe61 located in the vicinity of template 5'-overhang influence polymerase fidelity and nucleoside analog sensitivity of HIV-1 reverse transcriptase.Cleavage specificities of Moloney murine leukemia virus RNase H implicated in the second strand transfer during reverse transcription.Site-specific footprinting reveals differences in the translocation status of HIV-1 reverse transcriptase. Implications for polymerase translocation and drug resistance.Probing contacts between the ribonuclease H domain of HIV-1 reverse transcriptase and nucleic acid by site-specific photocross-linking.
P2860
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P2860
Hydroxyl radical footprint analysis of human immunodeficiency virus reverse transcriptase-template.primer complexes.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
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@zh
1993年學術文章
@zh-hant
name
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@ast
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@en
type
label
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@ast
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@en
prefLabel
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@ast
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@en
P2093
P2860
P356
P1476
Hydroxyl radical footprint ana ...... ase-template.primer complexes.
@en
P2093
P2860
P304
P356
10.1073/PNAS.90.13.5909
P407
P577
1993-07-01T00:00:00Z