(Q42546368)

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Biological activity differences between TGF-β1 and TGF-β3 correlate with differences in the rigidity and arrangement of their component monomers

scientific article published on 5 September 2014

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scholarly article

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Europe PubMed Central

2 November 2017

Biological activity differences between TGF-β1 and TGF-β3 correlate with differences in the rigidity and arrangement of their component monomers (English)

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Europe PubMed Central

2 November 2017

3

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5 June 2020

author name string

Tao Huang

1

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5 June 2020

Seth L Schor

2

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5 June 2020

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5 September 2014

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Europe PubMed Central

2 November 2017

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Europe PubMed Central

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5 June 2020

53

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5 June 2020

36

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5 June 2020

5737-5749

1 reference

Europe PubMed Central

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5 June 2020

Transforming growth factor-β3 (TGF-β3) knock-in ameliorates inflammation due to TGF-β1 deficiency while promoting glucose tolerance.

1 reference

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1 reference

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TGF-β signaling in fibrosis

1 reference

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TGF-β signalling is mediated by two autonomously functioning TβRI:TβRII pairs

1 reference

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Ternary Complex of Transforming Growth Factor- 1 Reveals Isoform-specific Ligand Recognition and Receptor Recruitment in the Superfamily

1 reference

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Betaglycan has two independent domains required for high affinity TGF-beta binding: proteolytic cleavage separates the domains and inactivates the neutralizing activity of the soluble receptor.

1 reference

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TbetaR-II discriminates the high- and low-affinity TGF-beta isoforms via two hydrogen-bonded ion pairs

1 reference

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A cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactions

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TGFbeta in Cancer

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

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Overexpression of human transforming growth factor-beta1 using a recombinant CHO cell expression system

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Solution structure and backbone dynamics of the TGFbeta type II receptor extracellular domain

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Mechanisms of TGF-beta signaling from cell membrane to the nucleus

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Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex

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Rapid structural fluctuations of the free HIV protease flaps in solution: relationship to crystal structures and comparison with predictions of dynamics calculations

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A method for efficient isotopic labeling of recombinant proteins

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28 May 2018

Pathogenesis of cleft palate in TGF-beta3 knockout mice

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4165442

28 May 2018

TGF-beta signal transduction

1 reference

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28 May 2018

TGFbeta2 knockout mice have multiple developmental defects that are non-overlapping with other TGFbeta knockout phenotypes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4165442

28 May 2018

The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4165442

28 May 2018

Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2

1 reference

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Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.

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Transforming growth factor beta 1 null mutation in mice causes excessive inflammatory response and early death

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4165442

28 May 2018

Betaglycan presents ligand to the TGF beta signaling receptor.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4165442

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Mechanism of activation of the TGF-beta receptor

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Transforming growth factor-beta 3 is required for secondary palate fusion

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Elucidating the folding problem of helical peptides using empirical parameters.

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12 December 2020

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1 reference

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based on heuristic

inferred from PubMed ID database lookup

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1 reference

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1 reference

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Identifiers

10.1021/BI500647D

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25153513%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25153513%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:25153513%20AND%20SRC:MED&resulttype=core&format=json

5 June 2020

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