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

UbMES and UbFluor: Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN.

The Journal of biological chemistry - 6 Oct 2017

Park Sungjin, Foote Peter K, Krist David T, Rice Sarah E, Statsyuk Alexander V

Abstract excerpt

Ring-between-ring (RBR) E3 ligases have been implicated in autoimmune disorders and neurodegenerative diseases. The functions of many RBR E3s are poorly defined, and their regulation is complex, involving post-translational modifications and allosteric regulation with other protein partners. The functional complexity of RBRs, coupled with the complexity of the native ubiquitination reaction that requires ATP and...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Fluorescence Polarization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Probes

Share to Mutation

Share to Polyubiquitin

Share to Ubiquitin-Protein Ligases

Share to Ubiquitination

Source

Open in PubMed Open full text

Identifiers

PMID: 28710279
DOI: 10.1074/jbc.M116.773200
PMCID: PMC5633118

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

UbMES and UbFluor: Novel probes for ring-between-ring (RBR) E3 ubiquitin ligase PARKIN.PMID 28710279Read ↗

Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation.Semantic proximity Read ↗

Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation.Semantic proximity Read ↗

Mechanism of phospho-Ubls' specificity and conformational changes that regulate Parkin activity.Semantic proximity Read ↗

Selective localization of Mfn2 near PINK1 enable its preferential ubiquitination by Parkin on mitochondriaSemantic proximity Read ↗

Engineering a Cell-Based Orthogonal Ubiquitin Transfer Cascade for Profiling the Substrates of RBR E3 ParkinSemantic proximity Read ↗

A Ubl/ubiquitin switch in the activation of ParkinSemantic proximity Read ↗

A mechanistic review of Parkin activation.Semantic proximity Read ↗

Activation of parkin by a molecular glue.Semantic proximity Read ↗

Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases.Semantic proximity Read ↗

Mechanism of phospho-ubiquitin-induced PARKIN activation.Semantic proximity Read ↗

Structure of the human Parkin ligase domain in an autoinhibited state.Semantic proximity Read ↗

Structure of parkin reveals mechanisms for ubiquitin ligase activation.Semantic proximity Read ↗

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