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 R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27.

FEBS letters - 19 Jun 2003

Chabaud Stéphane, Lambert Herman, Sasseville A Marie-Josée, Lavoie Hugo, Guilbault Claire, Massie Bernard, Landry Jacques, Langelier Yves

Abstract excerpt

HSV-2 R1, the R1 subunit of herpes simplex virus (HSV) ribonucleotide reductase, protects cells against apoptosis. Here, we report the presence in HSV-2 R1 of a stretch exhibiting similarity to the alpha-crystallin domain of the small heat shock proteins, a domain known to be important for oligomerization and cytoprotective activities of these proteins. Also, the HSV-2 R1 protein, which forms multimeric...

Read the complete abstract on PubMed

Topics

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

Share to Citrate (si)-Synthase
Share to Consensus Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Herpesvirus 1, Human

Share to Hot Temperature

Share to Molecular Weight

Share to Protein Denaturation

Share to Ribonucleotide Reductases

Source

Identifiers

PMID: 12804778
DOI: 10.1016/s0014-5793(03)00547-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 9 closest

The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27.PMID 12804778Read ↗

The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function.Semantic proximity Read ↗

Modification and Reorganization of the Cytoprotective Cellular Chaperone Hsp27 during Herpes Simplex Virus Type 1 InfectionSemantic proximity Read ↗

The small heat-shock protein HspL is a VirB8 chaperone promoting type IV secretion-mediated DNA transfer.Semantic proximity Read ↗

An N-terminal 33-amino-acid-deletion variant of hsp25 retains oligomerization and functional properties.Semantic proximity Read ↗

YrhB is a highly stable small protein with unique chaperone-like activity in Escherichia coli BL21(DE3).Semantic proximity Read ↗

Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein.Semantic proximity Read ↗

Chaperone-Mediated In Vitro Disassembly of Polyoma- and PapillomavirusesSemantic proximity Read ↗

Transcription antitermination by translation initiation factor IF1.Semantic proximity Read ↗

Structure and properties of K141E mutant of small heat shock protein HSP22 (HspB8, H11) that is expressed in human neuromuscular disorders.Semantic proximity Read ↗

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