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Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses
scientific journal article
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instance of
scholarly article
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
title
Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses
(English)
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
main subject
phosphorylation
0 references
author name string
S. Souchelnytskyi
series ordinal
1
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
P. ten Dijke
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
K. Miyazono
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
C. H. Heldin
series ordinal
4
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
language of work or name
English
0 references
publication date
15 November 1996
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
published in
The EMBO Journal
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stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
volume
15
1 reference
stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
issue
22
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stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
page(s)
6231–6240
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stated in
PubMed
PubMed ID
8947046
retrieved
3 February 2017
cites work
Interaction of the transforming growth factor-beta type I receptor with farnesyl-protein transferase-alpha
1 reference
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PubMed Central
reference URL
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17 March 2017
Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta
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PubMed Central
reference URL
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17 March 2017
A transforming growth factor beta type I receptor that signals to activate gene expression
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PubMed Central
reference URL
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17 March 2017
Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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17 March 2017
Mechanism of activation of the TGF-beta receptor
1 reference
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PubMed Central
reference URL
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retrieved
17 March 2017
A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor
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stated in
PubMed Central
reference URL
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17 March 2017
Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12
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PubMed Central
reference URL
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17 March 2017
Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
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PubMed Central
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17 March 2017
TGF beta signals through a heteromeric protein kinase receptor complex
1 reference
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PubMed Central
reference URL
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17 March 2017
Signaling via hetero-oligomeric complexes of type I and type II serine/threonine kinase receptors
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Complementation between kinase-defective and activation-defective TGF-beta receptors reveals a novel form of receptor cooperativity essential for signaling.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Identification of important regions in the cytoplasmic juxtamembrane domain of type I receptor that separate signaling pathways of transforming growth factor-beta
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PubMed Central
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3 June 2018
Signaling activity of transforming growth factor beta type II receptors lacking specific domains in the cytoplasmic region
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PubMed Central
reference URL
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3 June 2018
Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta.
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PubMed Central
reference URL
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3 June 2018
The types II and III transforming growth factor-beta receptors form homo-oligomers
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Reconstitution and transphosphorylation of TGF-beta receptor complexes
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
The GS domain of the transforming growth factor-beta type I receptor is important in signal transduction
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Disruption of transforming growth factor beta signaling by a mutation that prevents transphosphorylation within the receptor complex.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
TGF-beta-receptor-mediated signaling
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Homomeric interactions between type II transforming growth factor-beta receptors.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Signaling by the transforming growth factor-beta receptors
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
New class of transforming growth factors potentiated by epidermal growth factor: isolation from non-neoplastic tissues
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PubMed Central
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3 June 2018
TGF-beta stimulation and inhibition of cell proliferation: new mechanistic insights
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PubMed Central
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3 June 2018
Concomitant loss of transforming growth factor (TGF)-beta receptor types I and II in TGF-beta-resistant cell mutants implicates both receptor types in signal transduction.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
TGF-beta receptors and TGF-beta binding proteoglycans: recent progress in identifying their functional properties
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PubMed Central
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3 June 2018
Control of junB and extracellular matrix protein expression by transforming growth factor-beta 1 is independent of simian virus 40 T antigen-sensitive growth-sensitive growth-inhibitory events
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
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3 June 2018
Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=452446
retrieved
3 June 2018
Receptors for the TGF-beta superfamily: multiple polypeptides and serine/threonine kinases
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8947046
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The TGF-beta family and its composite receptors
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/8947046
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1038/SJ.EMBOJ.7590578D
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2958752
OpenCitations bibliographic resource ID
2958752
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2958752
PMCID
452446
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2958752
PubMed ID
8947046
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2958752
ResearchGate publication ID
14260461
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