Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Sequential Mechanism of HIV Reverse Transcriptase RNase H

1 Dec 2000

Abstract excerpt

Synthesis of the minus strand of viral DNA by human immunodeficiency virus, type 1 (HIV-1) reverse transcriptase is accompanied by RNase H degradation of the viral RNA genome. RNA fragments remain after synthesis and are degraded by the polymerase-independent mode of RNase H cleavage. Recently, we showed that this mode of cleavage occurs by a specific ordered mechanism in which primary cuts are first, secondary...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA and Nucleic Acid Chemistry
Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 10956669
DOI: 10.1074/jbc.m007381200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Sequential Mechanism of HIV Reverse Transcriptase RNase HPMID 10956669Read ↗

Mutations in the RNase H domain of HIV-1 reverse transcriptase affect the initiation of DNA synthesis and the specificity of RNase H cleavage in vivo.Semantic proximity Read ↗

Mutations within the primer grip region of HIV-1 reverse transcriptase result in loss of RNase H function.Semantic proximity Read ↗

Temporal Coordination between Initiation of HIV (+)-Strand DNA Synthesis and Primer RemovalSemantic proximity Read ↗

Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase.Semantic proximity Read ↗

Mutants of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase resistant to nonnucleoside reverse transcriptase inhibitors demonstrate altered rates of RNase H cleavage that correlate with HIV-1 replication fitness in cell culture.Semantic proximity Read ↗

Mechanism and fidelity of HIV reverse transcriptase.Semantic proximity Read ↗

Determinants of the RNase H cleavage specificity of human immunodeficiency virus reverse transcriptase.Semantic proximity Read ↗

Effects on DNA synthesis and translocation caused by mutations in the RNase H domain of Moloney murine leukemia virus reverse transcriptase.Semantic proximity Read ↗

Mutating a Conserved Motif of the HIV-1 Reverse Transcriptase Palm Subdomain Alters Primer UtilizationSemantic proximity Read ↗

Arm-specific cleavage and mutation during reverse transcription of 2΄,5΄-branched RNA by Moloney murine leukemia virus reverse transcriptase.Semantic proximity Read ↗

Residues in the alphaH and alphaI helices of the HIV-1 reverse transcriptase thumb subdomain required for the specificity of RNase H-catalyzed removal of the polypurine tract primer.Semantic proximity Read ↗

In vitro analysis of the effects of mutations in the G-tract of the human immunodeficiency virus type 1 polypurine tract on RNase H cleavage specificity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.