Comparison of Three Members of the Cysteine-rich Protein Family Reveals Functional Conservation and Divergent Patterns of Gene Expression
Open Access
- 1 October 1997
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (43) , 27484-27491
- https://doi.org/10.1074/jbc.272.43.27484
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Two muscle-specific LIM proteins in Drosophila.The Journal of cell biology, 1996
- Structure of the Cysteine-Rich Intestinal Protein, CRIPJournal of Molecular Biology, 1996
- Specificity of single LIM motifs in targeting and LIM/LIM interactions in situ.Genes & Development, 1996
- The enigma of LIM domainsStructure, 1995
- The Cysteine-rich Protein Family of Highly Related LIM Domain ProteinsPublished by Elsevier ,1995
- The LIM/double zinc-finger motif functions as a protein dimerization domain.Proceedings of the National Academy of Sciences, 1994
- The LIM domain is a modular protein-binding interfaceCell, 1994
- Structure of the carboxy-terminal LIM domain from the cysteine rich protein CRPNature Structural & Molecular Biology, 1994
- Common metal ion coordination in LIM domain proteinsBiochemistry, 1994
- The LIM motif defines a specific zinc-binding protein domain.Proceedings of the National Academy of Sciences, 1993