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TGFBR3 wt Allele

Known as: ALK-5, TGFBR3, Transforming Growth Factor, Beta Receptor III (Betaglycan, 300kDa) wt Allele 
Human TGFBR3 wild-type allele is located within 1p33-p32 and is approximately 217 kb in length. This allele, which encodes TGF-beta receptor type III… 
National Institutes of Health

Related topics

Related topics

12 relations
1p33-p32ALK PathwayCTCF PathwayLigand Binding

Broader (1)

TGFBR3 gene

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Attenuation of pulmonary fibrosis in type I collagen-targeted reporter mice with ALK-5 inhibitors.
2016
2016
Effect of Transforming Growth Factor-Beta signalling on SHED cultured in keratinocytes differentiation medium treated with TGF-B1 and ALK-5 inhibitor
2015
2015
Activation of the ALK-5 Pathway is not per se Sufficient for the Antiproliferative Effect of TGF-β1 on Renal Tubule Epithelial Cells
Background/Aims: Defective tissue repair underlies renal tissue degeneration during chronic kidney disease (CKD) progression… 
2013
2013
Evaluation of Dose Effect of ALK-5 Inhibitor and Controlled Delivery with Novel Pentablock Polymer in Glaucoma Filtration Surgery
2010
2010
[Platelet-derived growth factor-BB inhibited p21(WAF1) expression partially through transforming growth factor-beta signalling system in vascular smooth muscle cell].
OBJECTIVE To assess if the modulating effect of platelet-derived growth factor (PDGF)-BB on p21(WAF1) was mediated by… 
2003
2003
ACE inhibition modulates transforming growth factor-beta receptors in the young rat.
The renin-angiotensin system plays an important role in renal growth and development. Exposure of the neonate to angiotensin… 
1998
1998
The conventional transforming growth factor-beta (TGF-beta) receptor type I is not required for TGF-beta 1 signaling in a human prostate cancer cell line, LNCaP.
LNCaP is an androgen-responsive human prostate cancer cell line that has a defective gene for ALK-5, the conventional TGF-beta… 
1996
1996
Truncated activin type II receptors inhibit bioactivity by the formation of heteromeric complexes with activin type I. receptors.
Truncated activin type II receptors have been reported to inhibit activin receptor signaling in Xenopus embryos, although the… 
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