subject area of
- Altered expression of high-molecular-weight calmodulin-binding protein in human ischaemic myocardium Academic Article
- Binding of NAP-22, a Calmodulin-Binding Neuronal Protein, to Raft-like Domains in Model Membranes† Academic Article
- Biological significance of phosphorylation and myristoylation in the regulation of cardiac muscle proteins. Academic Article
- Ca2+-calmodulin binding to caldesmon and the caldesmon-actin-tropomyosin complex. Its role in Ca2+ regulation of the activity of synthetic smooth-muscle thin filaments Academic Article
- Ca2+-dependent regulation of vascular smooth-muscle caldesmon by S.100 and related smooth-muscle proteins Academic Article
- Caldesmon mRNA splicing and isoform expression in mammalian smooth-muscle and non-muscle tissues Academic Article
- Cardiac High Molecular Weight Calmodulin Binding Protein Contains Calpastatin Activity† Academic Article
- Decreased expression of high-molecular-weight calmodulin-binding protein and its correlation with apoptosis in ischemia-reperfused rat heart Academic Article
- Induction of raft-like domains by a myristoylated NAP-22 peptide and its Tyr mutant Academic Article
- Lipid binding activity of a neuron-specific protein NAP-22 studied in vivo and in vitro Academic Article
- Location of two contact sites between human smooth muscle caldesmon and Ca(2+)-calmodulin. Academic Article
- Primitive Neuroectodermal Tumors of the Female Genital Tract Academic Article
- Protein-Induced Formation of Cholesterol-Rich Domains† Academic Article
- Quaternary structure of the neuronal protein NAP-22 in aqueous solution Academic Article
- Specificity of Membrane Binding of the Neuronal Protein NAP-22 Academic Article
- The Ca2+-Sensitizing Component of Smooth Muscle Thin Filaments: Properties of Regulatory Factors That Interact with Caldesmon Academic Article
- The arrangement of cholesterol in membranes and binding of NAP-22 Academic Article
- The mechanism of Ca2+ regulation of vascular smooth muscle thin filaments by caldesmon and calmodulin. Academic Article
- Tracking peptide–membrane interactions: Insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly Academic Article