Transforming growth factor beta-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth (Q39939459)

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scientific article published on 15 September 2008

Language	Label	Description	Also known as
English	Transforming growth factor beta-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth	scientific article published on 15 September 2008

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

Transforming growth factor beta-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth (English)

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

phosphorylation

1 reference

based on heuristic

inferred from title

Caroline S. Hill

3

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

author name string

Amanda C Daly

1

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

Rebecca A Randall

2

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

language of work or name

0 references

publication date

15 September 2008

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

Molecular and Cellular Biology

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Europe PubMed Central

PMC publication ID

15 September 2017

28

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

22

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

6889-6902

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

Cancer-associated transforming growth factor beta type II receptor gene mutant causes activation of bone morphogenic protein-Smads and invasive phenotype

1 reference

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22 September 2017

Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding

1 reference

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22 September 2017

How the Smads regulate transcription

1 reference

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Dorsomorphin inhibits BMP signals required for embryogenesis and iron metabolism

1 reference

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TGFbeta-SMAD signal transduction: molecular specificity and functional flexibility

1 reference

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Arkadia activates Smad3/Smad4-dependent transcription by triggering signal-induced SnoN degradation

1 reference

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BMP-9 signals via ALK1 and inhibits bFGF-induced endothelial cell proliferation and VEGF-stimulated angiogenesis

1 reference

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Identification of BMP9 and BMP10 as functional activators of the orphan activin receptor-like kinase 1 (ALK1) in endothelial cells

1 reference

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Kinetic analysis of Smad nucleocytoplasmic shuttling reveals a mechanism for transforming growth factor beta-dependent nuclear accumulation of Smads

1 reference

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Specificity and versatility in tgf-beta signaling through Smads

1 reference

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Smad4 dependency defines two classes of transforming growth factor {beta} (TGF-{beta}) target genes and distinguishes TGF-{beta}-induced epithelial-mesenchymal transition from its antiproliferative and migratory responses

1 reference

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Endoglin promotes endothelial cell proliferation and TGF-beta/ALK1 signal transduction

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A simple molecular complex mediates widespread BMP-induced repression during Drosophila development.

1 reference

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Lateral signaling enhances TGF-beta response complexity

1 reference

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Activin receptor-like kinase (ALK)1 is an antagonistic mediator of lateral TGFbeta/ALK5 signaling

1 reference

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1 reference

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Morphogenesis and oncogenesis of MCF-10A mammary epithelial acini grown in three-dimensional basement membrane cultures

1 reference

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SB-431542 is a potent and specific inhibitor of transforming growth factor-beta superfamily type I activin receptor-like kinase (ALK) receptors ALK4, ALK5, and ALK7

1 reference

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1 reference

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Identification and functional characterization of distinct critically important bone morphogenetic protein-specific response elements in the Id1 promoter

1 reference

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22 September 2017

How cells read TGF-beta signals

1 reference

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TGF-beta inhibits p70 S6 kinase via protein phosphatase 2A to induce G(1) arrest

1 reference

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TGFbeta signaling in growth control, cancer, and heritable disorders

1 reference

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Homeodomain and winged-helix transcription factors recruit activated Smads to distinct promoter elements via a common Smad interaction motif

1 reference

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Specific activation of Smad1 signaling pathways by the BMP7 type I receptor, ALK2

1 reference

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Determinants of specificity in TGF-beta signal transduction.

1 reference

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Direct binding of Smad3 and Smad4 to critical TGF beta-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene

1 reference

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A kinase subdomain of transforming growth factor-beta (TGF-beta) type I receptor determines the TGF-beta intracellular signaling specificity

1 reference

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A transcriptional partner for MAD proteins in TGF-beta signalling

1 reference

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Determination of type I receptor specificity by the type II receptors for TGF-beta or activin

1 reference

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1 reference

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1 reference

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Smad1 recognition and activation by the ALK1 group of transforming growth factor-beta family receptors

1 reference

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1 reference

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Nucleocytoplasmic shuttling of Smads 2, 3, and 4 permits sensing of TGF-beta receptor activity

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1 reference

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Analysis of Smad nucleocytoplasmic shuttling in living cells.

1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/18794361

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https://pubmed.ncbi.nlm.nih.gov/18794361

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Transforming growth factor beta signaling through Smad1 in human breast cancer cells

1 reference

https://pubmed.ncbi.nlm.nih.gov/18794361

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/MCB.01192-08

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

ResearchGate publication ID

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