The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule
- 1 August 1993
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 65 (2) , 799-805
- https://doi.org/10.1016/s0006-3495(93)81121-4
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Molecular Shape of Vinculin in Aqueous SolutionJournal of Molecular Biology, 1993
- Severin is a gelsolin prototypeFEBS Letters, 1990
- Loss of calcium sensitivity of plasma gelsolin is associated with the presence of calcium ions during preparationFEBS Letters, 1989
- Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis.The Journal of cell biology, 1989
- Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity.The Journal of cell biology, 1988
- Nucleotide sequence of pig plasma gelsolin: Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeatsJournal of Molecular Biology, 1988
- Gelsolin has three actin-binding sites.The Journal of cell biology, 1988
- Fluorescence study of brevin, the Mr 92000 actin-capping and -fragmenting protein isolated from serum. Effect of calcium on protein conformationBiochemistry, 1985
- Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blockingBiochemistry, 1985
- A Ca2+‐dependent actin modulator from vertebrate smooth muscleFEBS Letters, 1984