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

A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.

Journal of virology - 1 Aug 1996

Merkulov G V, Swiderek K M, Brachmann C B, Boeke J D

Abstract excerpt

Cleavage of the Gag and Gag-Pol polyprotein precursors is a critical step in proliferation of retroviruses and retroelements. The Ty1 retroelement of Saccharomyces cerevisiae forms virus-like particles (VLPs) made of the Gag protein. Ty1 Gag is not obviously homologous to the Gag proteins of retroviruses. The apparent molecular mass of Gag is reduced from 58 to 54 kDa during particle maturation. Antibodies raised...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies
Share to Base Sequence
Share to DNA Transposable Elements

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

Share to Gene Products, gag

Share to Molecular Sequence Data

Share to Mutation

Share to Plasmids

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 8764068
DOI: 10.1128/JVI.70.8.5548-5556.1996
PMCID: PMC190514

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

A critical proteolytic cleavage site near the C terminus of the yeast retrotransposon Ty1 Gag protein.PMID 8764068Read ↗

A nucleocapsid functionality contained within the amino terminus of the Ty1 protease that is distinct and separable from proteolytic activity.Semantic proximity Read ↗

Ty3 GAG3 and POL3 genes encode the components of intracellular particlesSemantic proximity Read ↗

Mutations in the Ty3 major homology region affect multiple steps in Ty3 retrotransposition.Semantic proximity Read ↗

Saccharomyces cerevisiae RNA lariat debranching enzyme, Dbr1p, is required for completion of reverse transcription by the retrovirus-like element Ty1 and cleaves branched Ty1 RNAs.Semantic proximity Read ↗

The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins.Semantic proximity Read ↗

BUD22 affects Ty1 retrotransposition and ribosome biogenesis in Saccharomyces cerevisiae.Semantic proximity Read ↗

RNA branching and debranching in the yeast retrovirus-like element Ty1.Semantic proximity Read ↗

The Ty1 Retrotransposon Restriction Factor p22 Targets Gag.Semantic proximity Read ↗

P-body components are required for Ty1 retrotransposition during assembly of retrotransposition-competent virus-like particles.Semantic proximity Read ↗

A tobacco etch virus protease with increased substrate tolerance at the P1' position.Semantic proximity Read ↗

Proteolytic processing of foamy virus Gag and Pol proteins.Semantic proximity Read ↗

Characterization of a transpositionally active Ty3 element and identification of the Ty3 integrase protein.Semantic proximity Read ↗

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