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

The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.

Journal of molecular biology - 3 Sept 1999

Wilkinson K D, Laleli-Sahin E, Urbauer J, Larsen C N, Shih G H, Haas A L, Walsh S T, Wand A J

Abstract excerpt

The ubiquitin fold is a versatile and widely used targeting signal that is added post-translationally to a variety of proteins. Covalent attachment of one or more ubiquitin domains results in localization of the target protein to the proteasome, the nucleus, the cytoskeleton or the endocytotic machinery. Recognition of the ubiquitin domain by a variety of enzymes and receptors is vital to the targeting function...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Papain

Share to Static Electricity

Share to Thiolester Hydrolases

Share to Ubiquitin Thiolesterase

Share to Ubiquitins

Source

Identifiers

PMID: 10518943
DOI: 10.1006/jmbi.1999.3038

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The binding site for UCH-L3 on ubiquitin: mutagenesis and NMR studies on the complex between ubiquitin and UCH-L3.PMID 10518943Read ↗

Development of Ubiquitin Variants with Selectivity for Ubiquitin C-Terminal Hydrolase Deubiquitinases.Semantic proximity Read ↗

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

Mechanism of UCH-L5 activation and inhibition by DEUBAD domains in RPN13 and INO80G.Semantic proximity Read ↗

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

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

Mutations in the hydrophobic core of ubiquitin differentially affect its recognition by receptor proteins.Semantic proximity Read ↗

Structural Complexity in Ubiquitin RecognitionSemantic proximity Read ↗

The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders.Semantic proximity Read ↗

Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1.Semantic proximity Read ↗

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde.Semantic proximity Read ↗

The effect of Parkinson's-disease-associated mutations on the deubiquitinating enzyme UCH-L1.Semantic proximity Read ↗

Structural Elucidation of Peptide Binding to KLHL-12, a Substrate Specific Adapter Protein in a Cul3-Ring E3 Ligase Complex.Semantic proximity Read ↗

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