Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Suvana S. Lam"'
Publikováno v:
Journal of Biological Chemistry. 282:11365-11376
The family of Smad proteins mediates transforming growth factor-beta (TGF-beta) signaling in cell growth and differentiation. Smads repress or activate TGF-beta signaling by interacting with corepressors (e.g. Ski) or coactivators (e.g. CREB-binding
Autor:
Kai Lin, Genbin Shi, B.M. Chacko, Mark P. de Caestecker, Ashutosh Tiwari, Suvana S. Lam, Bin Y. Qin, Lawrence J. Hayward
Publikováno v:
Molecular Cell. 15(5):813-823
The formation of protein complexes between phosphorylated R-Smads and Smad4 is a central event in the TGF-beta signaling pathway. We have determined the crystal structure of two R-Smad/Smad4 complexes, Smad3/Smad4 to 2.5 angstroms, and Smad2/Smad4 to
Autor:
John J. Correia, Kai Lin, Rachel Delston, Hema Srinath, Suvana S. Lam, Bin Y. Qin, Rik Derynck, Cheng Liu
Publikováno v:
Nature Structural & Molecular Biology. 10:913-921
IRF-3, a member of the interferon regulatory factor (IRF) family of transcription factors, functions as a molecular switch for antiviral activity. IRF-3 uses an autoinhibitory mechanism to suppress its transactivation potential in uninfected cells, a
Publikováno v:
Genes & Development. 16:1950-1963
Smad3 transduces the signals of TGF-βs, coupling transmembrane receptor kinase activation to transcriptional control. The membrane-associated molecule SARA (Smad Anchor for Receptor Activation) recruits Smad3 for phosphorylation by the receptor kina
Publikováno v:
Nature Structural Biology. 8:248-253
Smad proteins mediate the transforming growth factor beta responses. C-terminal phosphorylation of R-Smads leads to the recruitment of Smad4 and the formation of active signaling complexes. We investigated the mechanism of phosphorylation-induced Sma
Publikováno v:
Structure. 7(12):1493-1503
Background: Smad4 functions as a common mediator of transforming growth factor β (TGF- β ) signaling by forming complexes with the phosphorylated state of pathway-restricted SMAD proteins that act in specific signaling pathways to activate transcri
Autor:
Katherine A. Fitzgerald, Celia A. Schiffer, John J. Correia, Kai Lin, William E. Royer, Suvana S. Lam, Weijun Chen, Zhaozhao Jiang, Hema Srinath
Publikováno v:
Nature structuralmolecular biology. 15(11)
Interferon regulatory factors (IRFs) are essential in the innate immune response and other physiological processes. Activation of these proteins in the cytoplasm is triggered by phosphorylation of serine and threonine residues in a C-terminal autoinh
Publikováno v:
Journal of molecular biology. 379(2)
IRF-3, a member of the interferon regulatory factor (IRF) family of transcription factors, functions in innate immune defense against viral infection. Upon infection, host cell IRF-3 is activated by phosphorylation at its seven C-terminal Ser/Thr res
Publikováno v:
Molecular cell. 8(6)
Phosphorylation of Smad1 at the conserved carboxyl terminal SVS sequence activates BMP signaling. Here we report the crystal structure of the Smad1 MH2 domain in a conformation that reveals the structural effects of phosphorylation and a molecular me
Autor:
Hema Srinath, Katherine A. Fitzgerald, Kai Lin, John J. Correia, Celia A. Schiffer, Zhaozhao Jiang, Weijun Chen, William E. Royer, Suvana S. Lam
Publikováno v:
Biophysical Journal. (3):586a-587a
Members of the Interferon Regulatory Factor (IRF) family of proteins play important roles in development of the immune system, host defense, inflammation and apoptosis. Activation of these proteins in the cytoplasm is triggered by phosphorylation of