The DOI matches its Crossref record; 137 of the 137 references it cites were found in a registry or an index.
Microtubules and Microtubule-Associated Proteins
Open accessAbstract
Microtubules act as "railways" for motor-driven intracellular transport, interact with accessory proteins to assemble into larger structures such as the mitotic spindle, and provide an organizational framework to the rest of the cell. Key to these functions is the fact that microtubules are "dynamic." As with actin, the polymer dynamics are driven by nucleotide hydrolysis and influenced by a host of specialized regulatory proteins, including microtubule-associated proteins. However, microtubule turnover involves a surprising behavior-termed dynamic instability-in which individual polymers switch stochastically between growth and depolymerization. Dynamic instability allows microtubules to explore intracellular space and remodel in response to intracellular and extracellular cues. Here, we review how such instability is central to the assembly of many microtubule-based structures and to the robust functioning of the microtubule cytoskeleton.
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Cites
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Actin and Actin-Binding Proteins
Pollard, T. D. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018226 · Cited by 912
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The phenotypic landscape of essential human genes
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Mechanism of ribosome-associated mRNA degradation during tubulin autoregulation
Höpfler, M., Absmeier, E., Peak-Chew, S.-Y., Vartholomaiou, E., Passmore, L. A., Gasic, I., & Hegde, R. S. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.05.020 · Cited by 41
Metadata
- Authors
- Goodson, H. V., & Jonasson, E. M.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2018-06
- Volume
- 10
- Issue
- 6
- Pages
- a022608
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2806967619
- Cited by
- 579
- References
- 137
- Type
- posted content
- Language
- en
- Open access
- bronze
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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.