Title : Drebrin-induced stabilization of actin filaments.

Pub. Date : 2013 Jul 5

PMID : 23696644






2 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 The actin binding domain of drebrin decreases the intrastrand disulfide cross-linking of Cys-41 (in the DNase I binding loop) to Cys-374 (C-terminal) but increases the interstrand disulfide cross-linking of Cys-265 (hydrophobic loop) to Cys-374 in the yeast mutants Q41C and S265C, respectively. Disulfides drebrin 1 Homo sapiens
2 The actin binding domain of drebrin decreases the intrastrand disulfide cross-linking of Cys-41 (in the DNase I binding loop) to Cys-374 (C-terminal) but increases the interstrand disulfide cross-linking of Cys-265 (hydrophobic loop) to Cys-374 in the yeast mutants Q41C and S265C, respectively. Disulfides drebrin 1 Homo sapiens