The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Arginylation of ß-Actin Regulates Actin Cytoskeleton and Cell Motility
Abstract
Posttranslational arginylation is critical for mouse embryogenesis, cardiovascular development, and angiogenesis, but its molecular effects and the identity of proteins arginylated in vivo are unknown. We found that β-actin was arginylated in vivo to regulate actin filament properties, β-actin localization, and lamella formation in motile cells. Arginylation of β-actin apparently represents a critical step in the actin N-terminal processing needed for actin functioning in vivo. Thus, posttranslational arginylation of a single protein target can regulate its intracellular function, inducing global changes on the cellular level, and may contribute to cardiovascular development and angiogenesis.
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β-Actin specifically controls cell growth, migration, and the G-actin pool
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Remote Control of Gene Function by Local Translation
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Smooth Muscle α Actin (Acta2) and Myofibroblast Function during Hepatic Wound Healing
Rockey, D. C., Weymouth, N., & Shi, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077166 · Cited by 188
Chemical basis for minimal cognition
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Metadata
- Authors
- Karakozova, M., Kozak, M., Wong, C. C. L., Bailey, A. O., Yates, J. R., Mogilner, A., Zebroski, H., & Kashina, A.
- Venue
- Science
- Published
- 2006-07-14
- Volume
- 313
- Issue
- 5784
- Pages
- 192-196
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2029422324
- Cited by
- 271
- References
- 17
- FWCI
- 5.49
- Type
- journal article
- Language
- en
- Open access
- closed
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- Karakozova, M., Kozak, M., Wong, C. C. L., Bailey, A. O., Yates, J. R., Mogilner, A., Zebroski, H., & Kashina, A. (2006). Arginylation of ß-Actin Regulates Actin Cytoskeleton and Cell Motility. Science. https://doi.org/10.1126/science.1129344
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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