Phosphorylation motifs in the nonhelical domains of myosin heavy chain and paramyosin may negatively regulate assembly inCaenorhabditis elegansstriated muscle
Author:
Publisher
Wiley
Subject
Cell Biology,Structural Biology
Reference31 articles.
1. Rod phosphorylation favors folding in a catch muscle myosin;Castellani;Proc Natl Acad Sci USA,1987
2. Thick filament substructures in Caenorhabditis elegans: Evidence for two populations of paramyosin;Deitiker;J Cell Biol,1993
3. Assembly-dependent phosphorylation of myosin and paramyosin of native thick filaments in Caenorhabditis elegans;Dey;Biochem Biophys Res Commun,1992
4. Sequence analysis of the complete Caernohabditis elegans myosin heavy chain gene family;Dibb;J Mol Biol,1989
5. Myosin and paramyosin of Caenorhabditis elegans embryos assemble into nascent structures distinct from thick filaments and multi-filament assemblages;Epstein;J Cell Biol,1993
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2. UNC‐82/NUAK kinase is required by myosin A, but not myosin B, to assemble and function in the thick filament arms of C. elegans striated muscle;Cytoskeleton;2023-11-20
3. Protein phosphatase 2A is crucial for sarcomere organization in Caenorhabditis elegans striated muscle;Molecular Biology of the Cell;2018-08-15
4. The Role of the UNC-82 Protein Kinase in Organizing Myosin Filaments in Striated Muscle of Caenorhabditis elegans;Genetics;2017-03-01
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