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

Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase.

Science (New York, N.Y.) - 1 Jul 2005

Cadwell Ken, Coscoy Laurent

Abstract excerpt

Ubiquitination controls a broad range of cellular functions. The last step of the ubiquitination pathway is regulated by enzyme type 3 (E3) ubiquitin ligases. E3 enzymes are responsible for substrate specificity and catalyze the formation of an isopeptide bond between a lysine residue of the substrate (or the N terminus of the substrate) and ubiquitin. MIR1 and MIR2 are two E3 ubiquitin ligases encoded by...

Read the complete abstract on PubMed

Topics

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

Share to CHO Cells
Share to Endocytosis
Share to Herpesvirus 8, Human

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HLA-B7 Antigen

Share to Lysine

Share to Serine

Share to Transduction, Genetic

Share to Ubiquitin

Source

Identifiers

PMID: 15994556
DOI: 10.1126/science.1110340

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase.PMID 15994556Read ↗

The Ubiquitin System and Kaposi’s Sarcoma-Associated HerpesvirusSemantic proximity Read ↗

c-MIR, a Human E3 Ubiquitin Ligase, Is a Functional Homolog of Herpesvirus Proteins MIR1 and MIR2 and Has Similar ActivitySemantic proximity Read ↗

Immune regulation by protein ubiquitination: roles of the E3 ligases VHL and ItchSemantic proximity Read ↗

MHC class I ubiquitination by a viral PHD/LAP finger protein.Semantic proximity Read ↗

Emerging Roles of Non-proteolytic Ubiquitination in TumorigenesisSemantic proximity Read ↗

The Viral E3 Ubiquitin Ligase mK3 Uses the Derlin/p97 Endoplasmic Reticulum-associated Degradation Pathway to Mediate Down-regulation of Major Histocompatibility Complex Class I ProteinsSemantic proximity Read ↗

Degradation of the epstein-barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue.Semantic proximity Read ↗

Efficient internalization of MHC I requires lysine-11 and lysine-63 mixed linkage polyubiquitin chains.Semantic proximity Read ↗

Regulation of HPV-16 infection by ubiquitination of the L1 major capsid protein.Semantic proximity Read ↗

The Kaposi's sarcoma-associated herpesvirus K5 E3 ubiquitin ligase modulates targets by multiple molecular mechanisms.Semantic proximity Read ↗

Analysis of the ubiquitin-modified proteome identifies novel host factors in Kaposi’s sarcoma herpesvirus lytic reactivationSemantic proximity Read ↗

Ubiquitination of the transcription factor c-MAF is mediated by multiple lysine residues.Semantic proximity Read ↗

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