Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase.
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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 transcriptionPreclinical Characterization of PF-00868554, a Potent Nonnucleoside Inhibitor of the Hepatitis C Virus RNA-Dependent RNA PolymeraseInfluence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domainsDicaffeoylquinic and dicaffeoyltartaric acids are selective inhibitors of human immunodeficiency virus type 1 integrase.Combinatorial selection, inhibition, and antiviral activity of DNA thioaptamers targeting the RNase H domain of HIV-1 reverse transcriptaseCoordination between the polymerase and RNase H activity of HIV-1 reverse transcriptaseMultiple nucleotide preferences determine cleavage-site recognition by the HIV-1 and M-MuLV RNases H.Inhibition of foamy virus reverse transcriptase by human immunodeficiency virus type 1 RNase H inhibitorsReplication of phenotypically mixed human immunodeficiency virus type 1 virions containing catalytically active and catalytically inactive reverse transcriptase.Cleavage of double-stranded RNA by RNase HI from a thermoacidophilic archaeon, Sulfolobus tokodaii 7.Substitution of a highly basic helix/loop sequence into the RNase H domain of human immunodeficiency virus reverse transcriptase restores its Mn(2+)-dependent RNase H activity.Fusion with an RNA binding domain to confer target RNA specificity to an RNase: design and engineering of Tat-RNase H that specifically recognizes and cleaves HIV-1 RNA in vitro.HIV-1 integrase and RNase H activities as therapeutic targets.Crystal structure of the moloney murine leukemia virus RNase H domainReverse transcriptase--a general discussion.RNase H domain of Moloney murine leukemia virus reverse transcriptase retains activity but requires the polymerase domain for specificity.RNase D, a reported new activity associated with HIV-1 reverse transcriptase, displays the same cleavage specificity as Escherichia coli RNase IIISequence-independent RNA cleavages generate the primers for plus strand DNA synthesis in hepatitis B viruses: implications for other reverse transcribing elements.Contributions of DNA polymerase subdomains to the RNase H activity of human immunodeficiency virus type 1 reverse transcriptasePurification 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.RNase H activity associated with reverse transcriptase from feline immunodeficiency virusHuman immunodeficiency virus type 1 reverse transcriptase: spatial and temporal relationship between the polymerase and RNase H activitiesInhibition of HIV-1 reverse transcriptase by defined template/primer DNA oligonucleotides: effect of template length and binding characteristics.The Y181C substitution in 3'-azido-3'-deoxythymidine-resistant human immunodeficiency virus, type 1, reverse transcriptase suppresses the ATP-mediated repair of the 3'-azido-3'-deoxythymidine 5'-monophosphate-terminated primer.HIV-1 Reverse Transcriptase Polymerase and RNase H (Ribonuclease H) Active Sites Work Simultaneously and Independently.Characterization of the protease of a fish retrovirus, walleye dermal sarcoma virus.Mutations of the RNase H C helix of the Moloney murine leukemia virus reverse transcriptase reveal defects in polypurine tract recognition.Defects in Moloney murine leukemia virus replication caused by a reverse transcriptase mutation modeled on the structure of Escherichia coli RNase H.Reverse transcriptase of human immunodeficiency virus type 1: functionality of subunits of the heterodimer in DNA synthesis.Characterization of the double stranded RNA dependent RNase activity associated with recombinant reverse transcriptases.Viral gene products and replication of the human immunodeficiency type 1 virus.Functional organization of repeat addition processivity and DNA synthesis determinants in the human telomerase multimer.Two defective forms of reverse transcriptase can complement to restore retroviral infectivityTargeted RNases: a feasibility study for use in HIV gene therapy.Targeted Reconstitution of Cytokine Activity upon Antigen Binding using Split Cytokine Antibody Fusion Proteins.Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase
P2860
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P2860
Reconstitution in vitro of RNase H activity by using purified N-terminal and C-terminal domains of human immunodeficiency virus type 1 reverse transcriptase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@en
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@nl
type
label
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@en
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@nl
prefLabel
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@en
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@nl
P2093
P2860
P356
P1476
Reconstitution in vitro of RNa ...... type 1 reverse transcriptase.
@en
P2093
E W Moomaw
G O Hudson
Z Hostomska
Z Hostomsky
P2860
P304
P356
10.1073/PNAS.88.4.1148
P407
P577
1991-02-01T00:00:00Z