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

An exposed cysteine residue of human angiostatic mini tryptophanyl-tRNA synthetase.

Biochemistry - 13 Apr 2010

Wakasugi Keisuke

Abstract excerpt

Human tryptophanyl-tRNA synthetase (TrpRS) catalyzes the aminoacylation of tRNA(Trp). Human TrpRS exists in two forms: a major form that is the full-length protein and a truncated form (mini TrpRS) in which most of the N-terminal extension is absent. Human mini, but not full-length, TrpRS has angiostatic activity. Because the full-length protein, which lacks angiostatic activity, has all of the amino acid...

Read the complete abstract on PubMed

Topics

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

Share to Chromatography, Gel
Share to Circular Dichroism
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disulfides

Share to Electrophoresis, Polyacrylamide Gel

Share to Models, Molecular

Share to Protein Conformation

Share to Protein Multimerization

Source

Identifiers

PMID: 20225827
DOI: 10.1021/bi1000239

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

An exposed cysteine residue of human angiostatic mini tryptophanyl-tRNA synthetase.PMID 20225827Read ↗

A human aminoacyl-tRNA synthetase as a regulator of angiogenesisSemantic proximity Read ↗

An alternative conformation of human TrpRS suggests a role of zinc in activating non-enzymatic function.Semantic proximity Read ↗

Induction of Angiogenesis by a Fragment of Human Tyrosyl-tRNA SynthetaseSemantic proximity Read ↗

Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase.Semantic proximity Read ↗

Inhibition of mini-TyrRS-induced angiogenesis response in endothelial cells by VE-cadherin-dependent mini-TrpRS.Semantic proximity Read ↗

Species-specific differences in the regulation of the aminoacylation activity of mammalian tryptophanyl-tRNA synthetases.Semantic proximity Read ↗

The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis.Semantic proximity Read ↗

Improving Circulation Half-Life of Therapeutic Candidate N-TIMP2 by Unfolded Peptide ExtensionSemantic proximity Read ↗

Mini tryptophanyl-tRNA synthetase is required for a synthetic phenotype in vascular smooth muscle cells induced by IFN-γ-mediated β2-adrenoceptor signaling.Semantic proximity Read ↗

Interaction between the P14 residue and strand 2 of beta-sheet B is critical for reactive center loop insertion in plasminogen activator inhibitor-2.Semantic proximity Read ↗

Threonine 183 and adjacent flexible loop residues in the tryptophan synthase alpha subunit have critical roles in modulating the enzymatic activities of the beta subunit in the alpha 2 beta 2 complex.Semantic proximity Read ↗

Identification of thromboxane synthase amino acid residues involved in heme-propionate binding.Semantic proximity Read ↗

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