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The hepatitis B virus encoded oncoprotein pX amplifies TGF-beta family signaling through direct interaction with Smad4: potential mechanism of hepatitis B virus-induced liver fibrosis

Article Abstract:

Results show that hepatitis B virus encoded oncoprotein pX, regulates cytokine transforming growth factor-beta (TGF-beta) signaling implicated in the pathogenesis of liver fibrosis. Data indicate that signal amplification of TGF-beta is accomplished by its complexing with the signal transduer Smad4 and an oncoprotein.

Author: Parks, W. Tony, Roberts, Anita B., Lee, Dug Keum, Park, Seok Hee, Yi, Youngsuk, Choi, Shin-Geon, Lee, Cecile, Cho, HyeSeong, de Caestecker, Mark P., Shaul, Yosef, Kim, Seong-Jin
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2001
South Korea, Israel, Liver diseases, Hepatitis B virus

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Smad3 recruits the anaphase-promoting complex for ubiquitination and degradation of SnoN

Article Abstract:

Results show that the Smad proteins, Smad2 and Smad3 degrade the transforming growth factor beta regulator protein SnoN, which is mediated by the anaphase-promoting complex and ubiquitin-conjugating enzymes. Data reveal that ubiquitination and degradation of SnoN requires the Smad3 binding site in SnoN and lysine residues of SnoN.

Author: Wrana, Jeffrey L., Luo, Kunxin, Stroschein, Shannon L., Bonni, Shirin
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 2001
Canada, Enzymes, Ubiquitin, Enzyme regulation

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Smad2 transduces common signals from receptor serine-threonine and tyrosine kinases

Article Abstract:

Hepatocyte growth factor and epidermal growth factor signal through transmembrane receptor tyrosine kinases and facilitate gene activation. This activation is normally induced by Smad proteins through receptor serine-threonine kinases of the TGF-B superfamily. Experiments with mutations indicate that Smad2 may be a common factor in both processes and therefore in the process of phosphorylation.

Author: Parks, W. Tony, Lechleider, Robert J., Roberts, Anita B., Bottaro, Donald P., Caestecker, Mark P. de, Frank, Chistopher J., Castagnino, Paola
Publisher: Cold Spring Harbor Laboratory Press
Publication Name: Genes & Development
Subject: Biological sciences
ISSN: 0890-9369
Year: 1998
Analysis, Genetic aspects, Proteins, Phosphorylation, Transduction, Transduction (Genetics)

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Subjects list: United States, Physiological aspects, Cellular signal transduction, Transforming growth factors
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