(Q41048740)

English

Ligand-dependent and -independent interactions with the transforming growth factor type II and I receptor subunits reside in the aminoterminal portion of the ectodomain of the type III subunit

scientific article published on March 1998

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Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

Ligand-dependent and -independent interactions with the transforming growth factor type II and I receptor subunits reside in the aminoterminal portion of the ectodomain of the type III subunit (English)

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

author name string

Taniguchi A

1

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

Matsuzaki K

2

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

Nakano K

3

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

Kan M

4

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

McKeehan WL

5

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

language of work or name

1 reference

based on heuristic

inferred from title

publication date

1 March 1998

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

In Vitro Cellular & Developmental Biology - Animal

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

34

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

232-238

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

https://scigraph.springernature.com/pub.10.1007/s11626-998-0129-3

0 references

Betaglycan has multiple binding sites for transforming growth factor-beta 1.

1 reference

https://api.crossref.org/works/10.1007%2FS11626-998-0129-3

21 January 2018

Localization of transforming growth factor beta binding site in betaglycan. Comparison with small extracellular matrix proteoglycans

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transforming growth factor-beta activity is potentiated by heparin via dissociation of the transforming growth factor-beta/alpha 2-macroglobulin inactive complex

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reconstitution of a pentameric complex of dimeric transforming growth factor beta ligand and a type I, II, III receptor in baculoviral-infected insect cells

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mapping of the ligand binding domain of the transforming growth factor beta receptor type III by deletion mutagenesis

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Fibroblast Growth Factor Receptors from Liver Vary in Three Structural Domains

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transforming growth factor-beta 1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-beta 1.

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Transforming growth factor-beta (TGF-beta) receptor proteoglycan. Cell surface expression and ligand binding in the absence of glycosaminoglycan chains

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta.

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

TGF beta signals through a heteromeric protein kinase receptor complex

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Endoglin forms a heteromeric complex with the signaling receptors for transforming growth factor-beta

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Mutagenesis analysis of the membrane-proximal ligand binding site of the TGF-beta receptor type III extracellular domain

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Signaling by chimeric erythropoietin-TGF-beta receptors: homodimerization of the cytoplasmic domain of the type I TGF-beta receptor and heterodimerization with the type II receptor are both required for intracellular signal transduction.

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Complementation between kinase-defective and activation-defective TGF-beta receptors reveals a novel form of receptor cooperativity essential for signaling.

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Betaglycan presents ligand to the TGF beta signaling receptor.

1 reference

https://pubmed.ncbi.nlm.nih.gov/9557941

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1007/S11626-998-0129-3

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

Dimensions Publication ID

0 references

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

26 September 2017

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