Title : Interaction of Smads with collagen types I, III, and V.

Pub. Date : 2003 Oct 31

PMID : 14559231






1 Functional Relationships(s)
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1 These interactions were confirmed by glutathione S-transferase (GST) pull-down assays in which the MH2 domain of Smad 3 fused to GST interacted strongly with in vitro translated, 35S-labeled collagen types I, III, and V. Each collagen also bound to the MH2 domains of Smads 4 and 7 and, to a lesser extent, full-length Smads 1, 2, 3, and 4. Sulfur-35 SMAD family member 3 Homo sapiens