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Regulation of TGF-β receptor activity
scientific article published on 15 March 2012
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Europe PubMed Central
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3333473
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26 January 2020
title
Regulation of TGF-β receptor activity
(English)
1 reference
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Europe PubMed Central
PMC publication ID
3333473
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
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26 January 2020
author
Fei Huang
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1
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Europe PubMed Central
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3333473
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
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26 January 2020
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Ye-Guang Chen
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2
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3333473
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26 January 2020
publication date
15 March 2012
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3333473
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26 January 2020
published in
Cell & Bioscience
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PMC publication ID
3333473
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
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26 January 2020
volume
2
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3333473
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26 January 2020
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9
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Europe PubMed Central
PMC publication ID
3333473
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
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26 January 2020
exact match
https://scigraph.springernature.com/pub.10.1186/2045-3701-2-9
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TSC-22 promotes transforming growth factor β-mediated cardiac myofibroblast differentiation by antagonizing Smad7 activity.
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SNX25 regulates TGF-β signaling by enhancing the receptor degradation
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Monomeric type I and type III transforming growth factor-β receptors and their dimerization revealed by single-molecule imaging
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ALK5 phosphorylation of the endoglin cytoplasmic domain regulates Smad1/5/8 signaling and endothelial cell migration
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TACE-mediated ectodomain shedding of the type I TGF-beta receptor downregulates TGF-beta signaling
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The extracellular domain of the TGFbeta type II receptor regulates membrane raft partitioning.
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Specific activation of mitogen-activated protein kinase by transforming growth factor-beta receptors in lipid rafts is required for epithelial cell plasticity
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TRAF6 mediates Smad-independent activation of JNK and p38 by TGF-beta
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Transforming growth factor beta-induced Smad1/5 phosphorylation in epithelial cells is mediated by novel receptor complexes and is essential for anchorage-independent growth
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The type I TGF-beta receptor engages TRAF6 to activate TAK1 in a receptor kinase-independent manner
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TGF-beta activates Erk MAP kinase signalling through direct phosphorylation of ShcA
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The disintegrin and metalloproteinase ADAM12 contributes to TGF-beta signaling through interaction with the type II receptor
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Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-beta signaling
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The evolutionally conserved activity of Dapper2 in antagonizing TGF-beta signaling
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Smad transcription factors
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The ETV6-NTRK3 chimeric tyrosine kinase suppresses TGF-beta signaling by inactivating the TGF-beta type II receptor
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Histone modification in the TGFbetaRII gene promoter and its significance for responsiveness to HDAC inhibitor in lung cancer cell lines
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Non-Smad TGF-beta signals
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AIP4 restricts transforming growth factor-beta signaling through a ubiquitination-independent mechanism
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Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity
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GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I receptor
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Activin receptor-like kinase (ALK)1 is an antagonistic mediator of lateral TGFbeta/ALK5 signaling
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Smad-dependent and Smad-independent pathways in TGF-beta family signalling
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SARA, a FYVE domain protein, affects Rab5-mediated endocytosis.
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Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit
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TGF beta receptor internalization into EEA1-enriched early endosomes: role in signaling to Smad2
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Yes-associated protein (YAP65) interacts with Smad7 and potentiates its inhibitory activity against TGF-beta/Smad signaling
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Transforming growth factor beta activates Smad2 in the absence of receptor endocytosis
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reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3333473
retrieved
11 July 2018
The TGF beta receptor activation process: an inhibitor- to substrate-binding switch
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=3333473
retrieved
11 July 2018
Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation
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=3333473
retrieved
11 July 2018
MS-275, a histone deacetylase inhibitor, selectively induces transforming growth factor beta type II receptor expression in human breast cancer cells.
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=3333473
retrieved
11 July 2018
Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation
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=3333473
retrieved
11 July 2018
Caveolin-1 regulates transforming growth factor (TGF)-beta/SMAD signaling through an interaction with the TGF-beta type I 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=3333473
retrieved
11 July 2018
TGFbeta signaling in growth control, cancer, and heritable disorders
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=3333473
retrieved
11 July 2018
Controlling TGF-beta signaling
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=3333473
retrieved
11 July 2018
Silencing of TGF-beta signalling by the pseudoreceptor BAMBI.
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=3333473
retrieved
11 July 2018
Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12
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=3333473
retrieved
11 July 2018
SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta 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=3333473
retrieved
11 July 2018
Oligomeric structure of type I and type II transforming growth factor beta receptors: homodimers form in the ER and persist at the plasma membrane
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=3333473
retrieved
11 July 2018
Mechanism of TGFbeta receptor inhibition by FKBP12
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=3333473
retrieved
11 July 2018
The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling
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=3333473
retrieved
11 July 2018
The type II transforming growth factor-beta receptor autophosphorylates not only on serine and threonine but also on tyrosine residues
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=3333473
retrieved
11 July 2018
Positive and negative regulation of type II TGF-beta receptor signal transduction by autophosphorylation on multiple serine residues
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=3333473
retrieved
11 July 2018
Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses
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=3333473
retrieved
11 July 2018
Betaglycan presents ligand to the TGF beta signaling 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=3333473
retrieved
11 July 2018
Mechanism of activation of the TGF-beta 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=3333473
retrieved
11 July 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=3333473
retrieved
11 July 2018
GS domain mutations that constitutively activate T beta R-I, the downstream signaling component in the TGF-beta receptor complex
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=3333473
retrieved
11 July 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=3333473
retrieved
11 July 2018
Transforming Growth Factor {beta} Can Stimulate Smad1 Phosphorylation Independently of Bone Morphogenic Protein 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=3333473
retrieved
24 September 2018
Lateral diffusion of TGF-beta type I receptor studied by single-molecule imaging.
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=3333473
retrieved
24 September 2018
Cellular heparan sulfate negatively modulates transforming growth factor-beta1 (TGF-beta1) responsiveness in epithelial cells
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=3333473
retrieved
24 September 2018
Distinct endocytic pathways regulate TGF-β receptor signalling and turnover
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=3333473
retrieved
24 September 2018
Betaglycan inhibits TGF-beta signaling by preventing type I-type II receptor complex formation. Glycosaminoglycan modifications alter betaglycan function
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=3333473
retrieved
24 September 2018
Balancing BMP Signaling through Integrated Inputs into the Smad1 Linker
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22420375
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Src phosphorylates Tyr284 in TGF-beta type II receptor and regulates TGF-beta stimulation of p38 MAPK during breast cancer cell proliferation and invasion
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22420375
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Differential requirement for type I and type II transforming growth factor beta receptor kinase activity in ligand-mediated receptor endocytosis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22420375
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Ligand binding and functional properties of betaglycan, a co-receptor of the transforming growth factor-beta superfamily. Specialized binding regions for transforming growth factor-beta and inhibin A
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/22420375
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1186/2045-3701-2-9
1 reference
stated in
Europe PubMed Central
PMC publication ID
3333473
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 January 2020
Dimensions Publication ID
1011801271
0 references
PMC publication ID
3333473
1 reference
stated in
Europe PubMed Central
PMC publication ID
3333473
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 January 2020
PubMed publication ID
22420375
1 reference
stated in
Europe PubMed Central
PMC publication ID
3333473
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22420375%20AND%20SRC:MED&resulttype=core&format=json
retrieved
26 January 2020
ResearchGate publication ID
221897321
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