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

Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer.

The Journal of biological chemistry - 25 Sept 2009

Qian Shu-Bing, Waldron Lauren, Choudhary Neelima, Klevit Rachel E, Chazin Walter J, Patterson Cam

Abstract excerpt

Protein ubiquitination regulates numerous cellular functions in eukaryotes. The prevailing view about the role of RING or U-box ubiquitin ligases (E3) is to provide precise positioning between the attached substrate and the ubiquitin-conjugating enzyme (E2). However, the mechanism of ubiquitin transfer remains obscure. Using the carboxyl terminus of Hsc70-interacting protein as a model E3, we show herein that...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Crystallization

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

Share to Protein Engineering

Share to Protein Multimerization

Share to Ubiquitin

Share to Ubiquitin-Conjugating Enzymes

Share to Ubiquitin-Protein Ligases

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 19648119
DOI: 10.1074/jbc.M109.032334
PMCID: PMC2785368

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

Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer.PMID 19648119Read ↗

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

Determinants of chemoselectivity in ubiquitination by the J2 family of ubiquitin-conjugating enzymesSemantic proximity Read ↗

Core structures of ubiquitin dictate its dynamics and function.Semantic proximity Read ↗

HECT and RING finger families of E3 ubiquitin ligases at a glanceSemantic proximity Read ↗

E2 enzymes: more than just middle menSemantic proximity Read ↗

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

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

Structural biology of ubiquitin-protein ligases.Semantic proximity Read ↗

Engineering the orthogonal ubiquitin E1-E2 pairs for identification of K27 chain linkage substrates.Semantic proximity Read ↗

Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B.Semantic proximity Read ↗

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

Mutations of Rad6 E2 ubiquitin-conjugating enzymes at alanine-126 in helix-3 affect ubiquitination activity and decrease enzyme stability.Semantic proximity Read ↗

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