Two Low-Affinity Ca2+-Binding Sites of Gelsolin that Regulate Association with Actin
- 1 April 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 229 (2) , 512-516
- https://doi.org/10.1111/j.1432-1033.1995.tb20492.x
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Nucleation of Actin Polymerization by GelsolinEuropean Journal of Biochemistry, 1994
- Rate constants and equilibrium constants for binding of actin to the 1:1 gelsolin‐actin complexEuropean Journal of Biochemistry, 1991
- Weak binding of divalent cations to plasma gelsolinBiochemistry, 1990
- pH-dependent rate of formation of the gelsolin-actin complex from gelsolin and monomeric actinEuropean Journal of Biochemistry, 1987
- Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphateNature, 1987
- Rate constants and equilibrium constants for binding of the gelsolin‐actin complex to the barbed ends of actin filaments in the presence and absence of calciumEuropean Journal of Biochemistry, 1986
- Rate of treadmilling of actin filaments in vitroJournal of Molecular Biology, 1986
- Fluorescence study of brevin, the Mr 92000 actin-capping and -fragmenting protein isolated from serum. Effect of calcium on protein conformationBiochemistry, 1985
- Actin filament disassembly in blood plasmaFEBS Letters, 1980
- Head to tail polymerization of actinJournal of Molecular Biology, 1976