The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Regulation of calmodulin-binding myosins
Open accessAbstract
Myosins constitute a diverse superfamily of actin-based mechanoenzymes that are involved in many essential cellular motilities. In addition to conventional muscle myosin II, ten other classes of unconventional myosins are known. Many unconventional myosins bind multiple calmodulin light chains and Ca2+, which can dramatically alter their mechanochemical and enzymatic activity. Calmodulin-binding myosins can also be regulated by phospholipid binding, phosphorylation of the heavy chain and actin-binding proteins. The molecular details linking unconventional-myosin regulation and function are just beginning to emerge.
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“In others, changes in the Ca2+ concentration affect the light chain calmodulin and lead to motor activation (Wolenski, 1995).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Wolenski, 1995
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Cites
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Brain myosin-V is a two-headed unconventional myosin with motor activity
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An active motor model for adaptation by vertebrate hair cells
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Cited by
Cell Migration: A Physically Integrated Molecular Process
Lauffenburger, D. A., & Horwitz, A. F. (1996) · Cell · doi:10.1016/s0092-8674(00)81280-5 · Cited by 3,915
Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules
Verhey, K. J., Lizotte, D. L., Abramson, T., Barenboim, L., Schnapp, B. J., & Rapoport, T. A. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.4.1053 · Cited by 266
“In others, changes in the Ca21 concentration affect the light chain calmodulin and lead to motor activation (Wolenski, 1995).”
BackgroundA Plant-Specific Protein Essential for Blue-Light-Induced Chloroplast Movements
DeBlasio, S. L., Luesse, D. L., & Hangarter, R. P. (2005) · Plant Physiology · doi:10.1104/pp.105.061887 · Cited by 102
Actin-based motor properties of native myosin VIIa
Udovichenko, I. P., Gibbs, D., & Williams, D. S. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.445 · Cited by 82
Unconventional Myosins, Actin Dynamics and Endocytosis: A Ménage à Trois?
Soldati, T. (2003) · Traffic · doi:10.1034/j.1600-0854.2003.t01-1-00095.x · Cited by 53
Metadata
- Authors
- Wolenski, J. S.
- Affiliations
- Yale University (US)
- Corresponding author
- Wolenski, Joseph S.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 1995-08
- Volume
- 5
- Issue
- 8
- Pages
- 310-316
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W1999525967
- Cited by
- 114
- References
- 47
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 1 · 2022: 1 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 3 · 2015: 2 · 2012: 1
- FWCI
- 5.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by-nc-nd/4.0/ (vor, 1827 d)
- Locations
- Trends in Cell Biology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- unconventional myosins, calcium regulation, myosin heavy chain phosphorylation, phospholipid binding, actin-binding proteins, myosin regulation, cell motility
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- Wolenski, J. S. (1995). Regulation of calmodulin-binding myosins. Trends in Cell Biology. https://doi.org/10.1016/s0962-8924(00)89053-4
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
