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

TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin‐RING ligase complexes

27 Sept 2013

Abstract excerpt

RING (Really Interesting New Gene)-in-between-RING (RBR) enzymes are a distinct class of E3 ubiquitin ligases possessing a cluster of three zinc-binding domains that cooperate to catalyse ubiquitin transfer. The regulation and biological function for most members of the RBR ligases is not known, and all RBR E3s characterized to date are auto-inhibited for in vitro ubiquitylation. Here, we show that TRIAD1 and...

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 Endoplasmic Reticulum Stress and Disease
Share to Ubiquitin and proteasome pathways

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 24076655
DOI: 10.1038/emboj.2013.209

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin‐RING ligase complexesPMID 24076655Read ↗

The acidic N-terminus of HHARI and neddylation are essential for the activation and maintenance of RIG-I-mediated type I interferon responseSemantic proximity Read ↗

Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation.Semantic proximity Read ↗

The emerging family of CULLIN3‐RING ubiquitin ligases (CRL3s): cellular functions and disease implicationsSemantic proximity Read ↗

DCAF1 (VprBP): emerging physiological roles for a unique dual-service E3 ubiquitin ligase substrate receptorSemantic proximity Read ↗

Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF function.Semantic proximity Read ↗

Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7.Semantic proximity Read ↗

CRL Ubiquitin Ligases and DNA Damage ResponseSemantic proximity Read ↗

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

Ariadne-1: a vital Drosophila gene is required in development and defines a new conserved family of ring-finger proteins.Semantic proximity Read ↗

The ring between ring fingers (RBR) protein familySemantic proximity Read ↗

CRL4s: the CUL4-RING E3 ubiquitin ligases.Semantic proximity Read ↗

The TFIIH subunit Tfb3 regulates cullin neddylation.Semantic proximity Read ↗

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