Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: Q9GZX9 and P13497 Pubmed SVM Score :0.0
Physical properties of Tld , Sog , Tsg and Dpp protein interactions are predicted to help create a sharp boundary in Bmp signals during dorsoventral patterning of the Drosophila embryo . ^^^ Previous genetic and biochemical studies have revealed that the Sog , Tsg and Tld proteins modify Dpp activity at the post transcriptional level . ^^^ The predominant view is that Sog and Tsg form a strong ternary complex with Dpp that prevents it from binding to its cognate receptors in lateral regions of the embryo , while in the dorsal most cells Tld is proposed to process Sog and thereby liberate Dpp for signaling . ^^^ In this study , additional genetic and biochemical assays were developed to further probe the relationships between the Sog , Tsg , Tld and Dpp proteins . ^^^ We propose that the strong Dpp concentration dependence exhibited by the processing reaction , together with movement of Dpp by Sog and Tsg protein can help explain how Tld activity is confined to the dorsal most region of the embryo through formation of a spatially dependent positive and negative reinforcement loop . ^^^
Interacting proteins: Q9GZX9 and P13497 Pubmed SVM Score :0.0
The ternary complex of Tsg / Chd / Bmp is cleaved by the metalloprotease Tolloid ( Tld ) / Xolloid ( Xld ) . ^^^
Interacting proteins: Q9GZX9 and P13497 Pubmed SVM Score :0.0
BMP signaling is modulated by a number of extracellular proteins , including the inhibitor Chordin , Tolloid related enzymes ( Tld ) , and the interacting protein Twisted Gastrulation ( Tsg ) . ^^^
Interacting proteins: Q9GZX9 and P13497 Pubmed SVM Score :0.0
This in vivo processing of Sog can be duplicated in vitro by treating Sog with a combination of the metalloprotease Tolloid ( Tld ) plus Twisted Gastrulation ( Tsg ) , another extracellular factor involved in Dpp signaling . ^^^
Interacting proteins: Q9GZX9 and P13497 Pubmed SVM Score :0.0
This refinement suggests that cells respond to the local transient morphogen distribution that results from interactions between bone morphogenetic proteins ( BMPs ) , their receptors , the BMP binding proteins Sog and Tsg , the metalloprotease Tld , and a putative , positively regulated component that locally enhances surface binding of BMPs within the region of high signaling . ^^^
Interacting proteins: Q9GZX9 and P13497 Pubmed SVM Score :0.0
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