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

Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymes

12 Nov 2024

Abstract excerpt

Ubiquitin-conjugating enzymes (E2) play a crucial role in the attachment of ubiquitin to proteins. Together with ubiquitin ligases (E3), they catalyze the transfer of ubiquitin (Ub) onto lysines with high chemoselectivity. A subfamily of E2s, including yeast Ubc6 and human Ube2J2, also mediates noncanonical modification of serines, but the structural determinants for this chemical versatility remain unknown....

Read the complete abstract on PubMed

Topics

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

Share to Autophagy in Disease and Therapy
Share to Cancer, Hypoxia, and Metabolism
Share to Ubiquitin and proteasome pathways

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

Source

Identifiers

PMID: 39533056
DOI: 10.1038/s44318-024-00301-3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 22 Oct 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

Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymesPMID 39533056Read ↗

Structural and biophysical characterisation of ubiquitin variants that specifically inhibit the ubiquitin conjugating enzyme Ube2d2Semantic proximity Read ↗

Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases.Semantic proximity Read ↗

E2 enzymes: more than just middle menSemantic proximity Read ↗

Biochemical and structural characterization of the ubiquitin-conjugating enzyme UBE2W reveals the formation of a noncovalent homodimer.Semantic proximity Read ↗

A comprehensive framework of E2-RING E3 interactions of the human ubiquitin-proteasome system.Semantic proximity Read ↗

Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer.Semantic proximity Read ↗

The unifying catalytic mechanism of the RING-between-RING E3 ubiquitin ligase familySemantic proximity Read ↗

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.Semantic proximity Read ↗

RING E3-Catalyzed E2 Self-Ubiquitination Attenuates the Activity of Ube2E Ubiquitin-Conjugating Enzymes.Semantic proximity Read ↗

A General Strategy for Discovery of Inhibitors and Activators of RING and U-box E3 Ligases with Ubiquitin VariantsSemantic proximity Read ↗

Dimerization regulates the human APC/C-associated ubiquitin-conjugating enzyme UBE2S.Semantic proximity Read ↗

Dimeric Ube2g2 simultaneously engages donor and acceptor ubiquitins to form Lys48‐linked ubiquitin chainsSemantic proximity Read ↗

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