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

Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38.

The Biochemical journal - 1 Nov 2004

Takagaki Kentaro, Satoh Takeshi, Tanuma Nobuhiro, Masuda Kouhei, Takekawa Mutsuhiro, Shima Hiroshi, Kikuchi Kunimi

Abstract excerpt

We have isolated a mouse cDNA for a novel dual-specificity phosphatase designated LDP-3 (low-molecular-mass dual-specificity phosphatase 3). The 450 bp open reading frame encodes a protein of 150 amino acids with a predicted molecular mass of 16 kDa. Northern blot and reverse transcription-PCR analyses show that LDP-3 transcripts are expressed in almost all mouse tissues examined. In vitro analyses using several...

Read the complete abstract on PubMed

Topics

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

Share to Chlorocebus aethiops
Share to COS Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dual-Specificity Phosphatases

Share to JNK Mitogen-Activated Protein Kinases

Share to Molecular Weight

Share to Osmotic Pressure

Share to p38 Mitogen-Activated Protein Kinases

Share to Protein Tyrosine Phosphatases

Source

Open in PubMed Open full text

Identifiers

PMID: 15281913
DOI: 10.1042/BJ20040498
PMCID: PMC1133737

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

Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38.PMID 15281913Read ↗

Molecular identification and functional characterization of a Drosophila dual-specificity phosphatase DMKP-4 which is involved in PGN-induced activation of the JNK pathway.Semantic proximity Read ↗

MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein.Semantic proximity Read ↗

Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase.Semantic proximity Read ↗

Biochemical and biological characterization of a neuroendocrine-associated phosphatase.Semantic proximity Read ↗

Molecular mechanisms involved in regulating protein activity and biological function of MST3Semantic proximity Read ↗

Conserved cross-interactions in Drosophila and Xenopus between Ras/MAPK signaling and the dual-specificity phosphatase MKP3.Semantic proximity Read ↗

The Drosophila dual-specificity ERK phosphatase DMKP3 cooperates with the ERK tyrosine phosphatase PTP-ER.Semantic proximity Read ↗

The dual specificity JKAP specifically activates the c-Jun N-terminal kinase pathway.Semantic proximity Read ↗

A one-step method to identify MAP kinase residues involved in inactivation by tyrosine- and dual-specificity protein phosphatases.Semantic proximity Read ↗

Role and regulation of MKP-1 in airway inflammationSemantic proximity Read ↗

Isolation and characterization of pmk-(1-3): three p38 homologs in Caenorhabditis elegans.Semantic proximity Read ↗

The isoform‐specific functions of the c‐Jun N‐terminal Kinases (JNKs): differences revealed by gene targetingSemantic proximity Read ↗

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