(Q24313061)

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The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands

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The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands (English)

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Transforming growth factor beta receptor 2

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GOA release 2020-03-11

transforming growth factor beta 2

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GOA release 2020-03-11

type III transforming growth factor beta receptor binding

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GOA release 2020-03-11

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inferred from title

6

object named as

H F Lodish

author given names

H F

author last names

Lodish

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PubMed publication ID

9 December 2023

author name string

H Y Lin

1

author given names

H Y

author last names

Lin

1 reference

PubMed publication ID

9 December 2023

A Moustakas

2

author given names

A

author last names

Moustakas

1 reference

PubMed publication ID

9 December 2023

P Knaus

3

author given names

P

author last names

Knaus

1 reference

PubMed publication ID

9 December 2023

R G Wells

4

author given names

R G

author last names

Wells

1 reference

PubMed publication ID

9 December 2023

Y I Henis

5

author given names

Y I

author last names

Henis

1 reference

PubMed publication ID

9 December 2023

language of work or name

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publication date

10 February 1995

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Journal of Biological Chemistry

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270

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6

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2747-54

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Transforming growth factors type beta 1 and beta 2 are equipotent growth inhibitors of human breast cancer cell lines.

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The transforming growth factor-beta system, a complex pattern of cross-reactive ligands and receptors

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Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system

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Expression cloning and characterization of the TGF-beta type III receptor

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Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinase

1 reference

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TGF beta signals through a heteromeric protein kinase receptor complex

1 reference

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Receptors for the TGF-β family

1 reference

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Betaglycan presents ligand to the TGF beta signaling receptor.

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Identification of human activin and TGF beta type I receptors that form heteromeric kinase complexes with type II receptors

1 reference

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Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor

1 reference

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Receptors for the TGF-beta superfamily: multiple polypeptides and serine/threonine kinases

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The TGF-beta family and its composite receptors

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Transforming growth factor beta 1: secondary structure as determined by heteronuclear magnetic resonance spectroscopy

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An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2

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DNA sequencing with chain-terminating inhibitors

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Type beta transforming growth factor is an inhibitor of myogenic differentiation

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Growth inhibition by transforming growth factor beta (TGF-beta) type I is restored in TGF-beta-resistant hepatoma cells after expression of TGF-beta receptor type II cDNA

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Cloning and characterization of a transmembrane serine kinase that acts as an activin type I receptor

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

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The types II and III transforming growth factor-beta receptors form homo-oligomers

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Oxidized redox state of glutathione in the endoplasmic reticulum

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Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily

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Direct cloning and sequence analysis of enzymatically amplified genomic sequences

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Characterization of type I receptors for transforming growth factor-beta and activin

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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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A transforming growth factor beta type I receptor that signals to activate gene expression

1 reference

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Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor

1 reference

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Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin

1 reference

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The transforming growth factor beta type II receptor can replace the activin type II receptor in inducing mesoderm

1 reference

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High-efficiency transformation of mammalian cells by plasmid DNA

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10.1074/JBC.270.6.2747

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release_p4cfyicky5ee5l6oxqnvzmz3bq

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