Isoform-specific Interaction of the Myosin-binding Proteins (MyBPs) with Skeletal and Cardiac Myosin Is a Property of the C-terminal Immunoglobulin Domain
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference51 articles.
1. Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intracellular member of the immunoglobulin superfamily.
2. The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif.
3. Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs.
4. Human Myosin-Binding Protein H (MyBP-H): Complete Primary Sequence, Genomic Organization, and Chromospinal Localization
5. Complete sequence of human fast-type and slow-type muscle myosin-binding-protein C (MyBP-C). Differential expression, conserved domain structure and chromosome assignment
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1. Implications of S-glutathionylation of sarcomere proteins in cardiac disorders, therapies, and diagnosis;Frontiers in Cardiovascular Medicine;2023-01-24
2. Nanosurfer assay dissects β-cardiac myosin and cardiac myosin-binding protein C interactions;Biophysical Journal;2022-06
3. Molecular characterization of linker and loop-mediated structural modulation and hinge motion in the C4-C5 domains of cMyBPC;Journal of Structural Biology;2022-06
4. Dissecting β-Cardiac Myosin and Cardiac Myosin-Binding Protein C Interactions using a Nanosurf Assay;2022-03-12
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