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Details on Person Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.

Class:IdLiteratureReference:208162
_displayNameCrystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.
_timestamp2007-12-18 11:48:37
author[Person:207888] Wu, JW
[Person:207589] Hu, M
[Person:207156] Chai, J
[Person:207735] Seoane, J
[Person:200869] Huse, M
[Person:207295] Li, C
[Person:207837] Rigotti, DJ
[Person:207116] Kyin, S
[Person:207886] Muir, TW
[Person:207451] Fairman, R
[Person:173487] Massague, J
[Person:141951] Shi, Y
created[InstanceEdit:205608] Williams, MG, 2007-03-27 14:11:11
journalMol Cell
pages1277-89
pubMedIdentifier11779503
titleCrystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.
volume8
year2001
(literatureReference)[Reaction:170847] Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4 [Homo sapiens]
[Reaction:208983] Phosphorylated SMAD2 forms a homotrimeric complex [Homo sapiens]
[Reaction:209015] Phosphorylated SMAD2 dissociates from SARA and Phospho TGFBR1 dimer [Homo sapiens]
[Reaction:9846183] GOCAM Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4 [Homo sapiens]
[Reaction:9846552] GOCAM Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4 [Homo sapiens]
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No pathways have been reviewed or authored by Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling. (208162)