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Article

Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II-C.

The Journal of biological chemistry - 17 Jun 2005

Kim Kye-Young, Kovács Mihály, Kawamoto Sachiyo, Sellers James R, Adelstein Robert S

Abstract excerpt

Human families with single amino acid mutations in nonmuscle myosin heavy chain (NMHC) II-A (MYH9) and II-C (MYH14) have been described as have mice generated with a point mutation in NMHC II-B (MYH10). These mutations (R702C and N93K in human NMHC II-A, R709C in murine NMHC II-B, and R726S in human NMHC II-C) result in phenotypes affecting kidneys, platelets, and leukocytes (II-A), heart and brain (II-B), and...

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Source

Identifiers

PMID: 15845534
DOI: 10.1074/jbc.M503488200

Genes

MYH10
MYH14
MYH9

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II-C.PMID 15845534Read ↗

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Research Advances in the Physiological and Pathological Function of MYH9 and NMIIA.Semantic proximity Read ↗

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The role of vertebrate nonmuscle Myosin II in development and human diseaseSemantic proximity Read ↗

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Linking the Landscape of MYH9-Related Diseases to the Molecular Mechanisms that Control Non-Muscle Myosin II-A Function in Cells.Semantic proximity Read ↗

MYH9 mutations differentially stabilize non-muscle myosin II filaments and induce distinct cellular aggregation phenotypes.Semantic proximity Read ↗

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