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

Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization.

Biochemistry - 2 Jul 1996

Ghosh M, Jacques P S, Rodgers D W, Ottman M, Darlix J L, Le Grice S F

Abstract excerpt

Alanine scanning mutagenesis was undertaken to evaluate the structural significance of Met230-His235 of the 66 kDa subunit of p66/p51 human immunodeficiency virus reverse transcriptase (HIV-1 RT). Together with Glu224-Trp229, these residues provide the framework of the p66 "primer grip", whose proposed role is maintaining the primer terminus in an orientation appropriate for nucleophilic attack on an incoming...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to DNA Primers

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

Share to Molecular Sequence Data

Share to Mutation

Share to Recombination, Genetic

Share to Sequence Deletion

Source

Identifiers

PMID: 8679616
DOI: 10.1021/bi952773j

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

Alterations to the primer grip of p66 HIV-1 reverse transcriptase and their consequences for template-primer utilization.PMID 8679616Read ↗

Kinetic analysis of four HIV-1 reverse transcriptase enzymes mutated in the primer grip region of p66. Implications for DNA synthesis and dimerization.Semantic proximity Read ↗

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

Alanine-scanning mutations in the "primer grip" of p66 HIV-1 reverse transcriptase result in selective loss of RNA priming activity.Semantic proximity Read ↗

Structure/function studies of human immunodeficiency virus type 1 reverse transcriptase. Alanine scanning mutagenesis of an alpha-helix in the thumb subdomain.Semantic proximity Read ↗

Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.Semantic proximity Read ↗

Insertion of a small peptide of six amino acids into the beta7-beta8 loop of the p51 subunit of HIV-1 reverse transcriptase perturbs the heterodimer and affects its activities.Semantic proximity Read ↗

Analysis of amino acids in the beta7-beta8 loop of human immunodeficiency virus type 1 reverse transcriptase for their role in virus replication.Semantic proximity Read ↗

Relationship between enzyme activity and dimeric structure of recombinant HIV-1 reverse transcriptase.Semantic proximity Read ↗

Probing contacts between the ribonuclease H domain of HIV-1 reverse transcriptase and nucleic acid by site-specific photocross-linking.Semantic proximity Read ↗

Proteolytic processing of an HIV-1 pol polyprotein precursor: insights into the mechanism of reverse transcriptase p66/p51 heterodimer formation.Semantic proximity Read ↗

HIV-1 reverse transcriptase: polymerization properties of the p51 homodimer compared to the p66/p51 heterodimer.Semantic proximity Read ↗

Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase.Semantic proximity Read ↗

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