The structure of an actin-crosslinking domain from human fimbrin.
- 1 September 1997
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 4 (9) , 708-712
- https://doi.org/10.1038/nsb0997-708
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Crystal structure of a calponin homology domainNature Structural & Molecular Biology, 1997
- Actin crosslinking proteins at the leading edgeSeminars in Cell Biology, 1994
- Deletion analysis of the dystrophin‐actin binding domainFEBS Letters, 1994
- Projection Image of Smooth Muscle α-Actinin from Two-dimensional Crystals Formed on Positively Charged Lipid LayersJournal of Molecular Biology, 1993
- Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping.The Journal of cell biology, 1992
- Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain.The Journal of cell biology, 1992
- Binding sites involved in the interaction of actin with the N‐terminal region of dystrophinFEBS Letters, 1992
- Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins.The Journal of cell biology, 1990
- The interaction of actin with dystrophinFEBS Letters, 1990
- Automatic indexing of rotation diffraction patternsJournal of Applied Crystallography, 1988