S
Su Wen Qian
Researcher at National Institutes of Health
Publications - 12
Citations - 1154
Su Wen Qian is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Transforming growth factor beta & Amino acid. The author has an hindex of 12, co-authored 12 publications receiving 1127 citations.
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Journal ArticleDOI
cDNA cloning by PCR of rat transforming growth factor β-1
Journal ArticleDOI
Hypoxia upregulates the synthesis of tgf-β1 by human dermal fibroblasts
Vincent Falanga,Su Wen Qian,David Danielpour,Matthew H. Katz,Anita B. Roberts,Michael B. Sporn +5 more
TL;DR: It is concluded that low oxygen tension upregulates the synthesis of TGF-β1 by human dermal fibroblasts, and leads to increased secretion of this peptide.
Journal ArticleDOI
Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2.
Andrew P. Hinck,Sharon J. Archer,Su Wen Qian,Anita B. Roberts,Michael B. Sporn,James A. Weatherbee,Monica L.-S. Tsang,Roger C. Lucas,Bo Ling Zhang,Jeff Wenker,Dennis A. Torchia +10 more
TL;DR: The three-dimensional solution structure of human transforming growth factor beta 1 (TGF-beta 1) has been determined using multinuclear magnetic resonance spectroscopy and a hybrid distance geometry/ simulated annealing algorithm, providing the first opportunity to examine structural differences between the two isoforms at the molecular level.
Journal ArticleDOI
The recombinant proregion of transforming growth factor beta1 (latency-associated peptide) inhibits active transforming growth factor beta1 in transgenic mice
Erwin P. Bottinger,Valentina M. Factor,Monica L.-S. Tsang,James A. Weatherbee,Jeffrey B. Kopp,Su Wen Qian,Lalage M. Wakefield,Anita B. Roberts,Snorri S. Thorgeirsson,Michael B. Sporn +9 more
TL;DR: Recombinant LAP should be a useful tool for novel approaches to study and therapeutically modulate pathophysiological processes mediated by TGF-beta3, both in vitro and in vivo, after intraperitoneal administration.
Journal ArticleDOI
Binding Affinity of Transforming Growth Factor-β for Its Type II Receptor Is Determined by the C-terminal Region of the Molecule
Su Wen Qian,James K. Burmester,Monica L.-S. Tsang,James A. Weatherbee,Andrew P. Hinck,Dennis J. Ohlsen,Michael B. Sporn,Anita B. Roberts +7 more
TL;DR: Observations clearly indicate that the domain in TGF-β1 responsible for its high affinity binding to TβRII, both the soluble and membrane-bound forms, is located at C terminus of the molecule.