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

Arabidopsis BRS1 is a secreted and active serine carboxypeptidase.

The Journal of biological chemistry - 21 Oct 2005

Zhou Aifen, Li Jia

Abstract excerpt

The Arabidopsis BRS1 gene encodes a serine carboxypeptidase II-like protein. Its biological role in the brassinosteroid signaling pathway was first established by its capability to specifically suppress a weak brassinosteroid insensitive 1 (bri1) allele, bri1-5, when overexpressed. To gain additional insights into the molecular mechanisms of BRS1 function, the subcellular localization and the biochemical...

Read the complete abstract on PubMed

Topics

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

Share to Carboxypeptidases
Share to Chromatography, Affinity
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glycosylation

Share to Hydrolysis

Share to Mass Spectrometry

Share to Microscopy, Confocal

Share to Transgenes

Source

Identifiers

PMID: 16123046
DOI: 10.1074/jbc.M503299200

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

Arabidopsis BRS1 is a secreted and active serine carboxypeptidase.PMID 16123046Read ↗

BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana.Semantic proximity Read ↗

BRS1 mediates plant redox regulation and cold responses.Semantic proximity Read ↗

Emerging roles for diverse intramembrane proteases in plant biology.Semantic proximity Read ↗

Plant proteases: from phenotypes to molecular mechanisms.Semantic proximity Read ↗

Serpin protease inhibitors in plant biology.Semantic proximity Read ↗

Arabidopsis SBT5.2 and SBT1.7 subtilases mediate C-terminal cleavage of flg22 epitope from bacterial flagellin.Semantic proximity Read ↗

Characterization of recombinant CDR1, an Arabidopsis aspartic proteinase involved in disease resistance.Semantic proximity Read ↗

Functional analyses of the chitin-binding domains and the catalytic domain of Brassica juncea chitinase BjCHI1.Semantic proximity Read ↗

A conserved asparagine residue in the inner surface of BRI1 superhelix is essential for protein native conformation.Semantic proximity Read ↗

Characterization of cp3 reveals a new bri1 allele, bri1-120, and the importance of the LRR domain of BRI1 mediating BR signaling.Semantic proximity Read ↗

The elongation defective1 mutant of Arabidopsis is impaired in the gene encoding a serine-rich secreted protein.Semantic proximity Read ↗

Plant-specific insertions in the soybean aspartic proteinases, soyAP1 and soyAP2, perform different functions of vacuolar targeting.Semantic proximity Read ↗

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