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

Identification and characterization of constitutively active Smad2 mutants: evaluation of formation of Smad complex and subcellular distribution.

Molecular endocrinology (Baltimore, Md.) - 1 Oct 2000

Funaba M, Mathews L S

Abstract excerpt

Smads mediate activin, transforming growth factor beta (TGFbeta), and bone morphogenetic protein signaling from receptors to nuclei. According to the current model, activated activin/TGFbeta receptors phosphorylate the carboxyl-terminal serines of Smad2 and Smad3 (SSMS-COOH); phosphorylated Smad2...

Read the complete abstract on PubMed

Topics

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

Share to Mink
Share to Nerve Growth Factors
Share to Phosphoserine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Smad Proteins

Share to Smad2 Protein

Share to Smad4 Protein

Share to Xenopus

Share to Xenopus Proteins

Source

Identifiers

PMID: 11043574
DOI: 10.1210/mend.14.10.0537

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11043574-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification and characterization of constitutively active Smad2 mutants: evaluation of formation of Smad complex and subcellular distribution.PMID 11043574Read ↗

Smad2 phosphorylation by type I receptor: contribution of arginine 462 and cysteine 463 In the C terminus of Smad2 for specificity.Semantic proximity Read ↗

Mechanism for mutational inactivation of the tumor suppressor Smad2.Semantic proximity Read ↗

Identification of Smad2, a Human Mad-related Protein in the Transforming Growth Factor β Signaling PathwaySemantic proximity Read ↗

Novel mutations in Smad proteins that inhibit signaling by the transforming growth factor beta in mammalian cells.Semantic proximity Read ↗

Novel dominant negative Smad antagonists to TGFbeta signaling.Semantic proximity Read ↗

Evidence for a role of Smad3 and Smad2 in stabilization of the tumor-derived mutant Smad2.Q407R.Semantic proximity Read ↗

A tale of two proteins: Differential roles and regulation of Smad2 and Smad3 in TGF‐β signalingSemantic proximity Read ↗

Unraveling the biological functions of Smad7 with mouse modelsSemantic proximity Read ↗

Identification of novel Smad2 and Smad3 associated proteins in response to TGF‐β1Semantic proximity Read ↗

Mutations in the tumor suppressors Smad2 and Smad4 inactivate transforming growth factor β signaling by targeting Smads to the ubiquitin–proteasome pathwaySemantic proximity Read ↗

Interaction with Smad4 is indispensable for suppression of BMP signaling by c-Ski.Semantic proximity Read ↗

Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.Semantic proximity Read ↗

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