How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices
- 1 February 1990
- journal article
- review article
- Published by Elsevier BV in Trends in Biochemical Sciences
- Vol. 15 (2), 59-64
- https://doi.org/10.1016/0968-0004(90)90177-d
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- The γ-Subunit of Skeletal Muscle Phosphorylase Kinase Contains Two Noncontiguous Domains That Act in Concert to Bind CalmodulinPublished by Elsevier BV ,1989
- Design of Peptides and ProteinsAdvances in protein chemistry, 1988
- Fluorescence Properties of Calmodulin-Binding Peptides Reflect Alpha-Helical PeriodicityScience, 1987
- Predicted calmodulin-binding sequence in the γ subunit of phosphorylase b kinaseProteins-Structure Function and Bioinformatics, 1987
- Calmodulin binding domains: characterization of a phosphorylation and calmodulin binding site from myosin light chain kinaseBiochemistry, 1986
- Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formationBiochemistry, 1985
- Probable role of amphiphilicity in the binding of mastoparan to calmodulinBiochemistry, 1985
- The design, synthesis, and characterization of tight‐binding inhibitors of calmodulinJournal of Cellular Biochemistry, 1985
- Identification of .beta.-endorphin residues 14-25 as a region involved in the inhibition of calmodulin-stimulated phosphodiesterase activityBiochemistry, 1983
- CalmodulinAdvances in protein chemistry, 1982