Title : Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking.

Pub. Date : 1985 Jul 2

PMID : 2994715






6 Functional Relationships(s)
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1 In this paper, the interactions with actin of the ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) stable 1:1 gelsolin-actin complexes are compared with those of free gelsolin. Egtazic Acid gelsolin Homo sapiens
2 In this paper, the interactions with actin of the ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) stable 1:1 gelsolin-actin complexes are compared with those of free gelsolin. Egtazic Acid gelsolin Homo sapiens
3 In this paper, the interactions with actin of the ethylene glycol bis(beta-aminoethyl ether)-N,N,N",N"-tetraacetic acid (EGTA) stable 1:1 gelsolin-actin complexes are compared with those of free gelsolin. Egtazic Acid gelsolin Homo sapiens
4 The abilities of free or complexed gelsolin to sever actin filaments, nucleate filament assembly, bind to the fast growing (+) filament ends, and lower the filament size distribution in the presence of either Ca2+ or EGTA were examined. Egtazic Acid gelsolin Homo sapiens
5 The gelsolin-actin complexes, however, differ from free gelsolin in that they have a higher affinity for (+) filament ends in EGTA and they cannot sever filaments in calcium. Egtazic Acid gelsolin Homo sapiens
6 The gelsolin-actin complexes, however, differ from free gelsolin in that they have a higher affinity for (+) filament ends in EGTA and they cannot sever filaments in calcium. Egtazic Acid gelsolin Homo sapiens