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

Processing of the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase.

1 Jun 1990

Abstract excerpt

We have analyzed the processing of the RNA primer for (+) strand DNA synthesis by reverse transcriptase of the human immunodeficiency virus 1. To test for specific RNA cleavage and primer usage, we constructed a 99-base pair RNA-DNA hybrid containing the viral polypurine tract and flanking viral sequences. Although the RNase H activity of reverse transcriptase cleaves the RNA strand into multiple fragments, only...

Read the complete abstract on PubMed

Topics

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

Share to HIV/AIDS drug development and treatment
Share to HIV Research and Treatment
Share to T-cell and Retrovirus Studies

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 1693920
DOI: 10.1016/s0021-9258(18)86984-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Processing of the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase.PMID 1693920Read ↗

The sequence features important for plus strand priming by human immunodeficiency virus type 1 reverse transcriptase.Semantic proximity Read ↗

Human Immunodeficiency Virus Reverse Transcriptase: 25 Years of Research, Drug Discovery, and PromiseSemantic 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 ↗

Effects of HIV-1 reverse transcriptase connection subdomain mutations on polypurine tract removal and initiation of (+)-strand DNA synthesis.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 ↗

Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Can Prevent Self-Priming of Minus-Strand Strong Stop DNA by Promoting the Annealing of Short Oligonucleotides to Hairpin SequencesSemantic proximity Read ↗

RNA abasic sites: preparation and trans-lesion synthesis by HIV-1 reverse transcriptase.Semantic proximity Read ↗

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

Sequences in the 5' and 3' R elements of human immunodeficiency virus type 1 critical for efficient reverse transcription.Semantic proximity Read ↗

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 ↗

A second origin of DNA plus-strand synthesis is required for optimal human immunodeficiency virus replication.Semantic proximity Read ↗

Mutations in the 5' end of the human immunodeficiency virus type 1 polypurine tract affect RNase H cleavage specificity and virus titer.Semantic proximity Read ↗

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