Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2041-1723
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate ; volume:9 ; number:1 ; day:6 ; month:7 ; year:2018 ; pages:1-13 ; date:12.2018
Nature Communications ; 9, Heft 1 (6.7.2018), 1-13, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Trofimova, Daria
- Contributor
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Paydar, Mohammadjavad
Zara, Anthony
Talje, Lama
Kwok, Benjamin H.
Allingham, John S.
SpringerLink (Online service)
- DOI
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10.1038/s41467-018-05025-7
- URN
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urn:nbn:de:101:1-2018091221411674560595
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:28 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Trofimova, Daria
- Paydar, Mohammadjavad
- Zara, Anthony
- Talje, Lama
- Kwok, Benjamin H.
- Allingham, John S.
- SpringerLink (Online service)
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Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
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Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
Author Correction: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
Tubulin islands containing slowly hydrolyzable GTP analogs regulate the mechanism and kinetics of microtubule depolymerization
Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins
α-tubulin detyrosination fine-tunes kinetochore-microtubule attachments
Kinesin motor density and dynamics in gliding microtubule motility
Microtubule nucleation by γ-tubulin [gamma-tubulin] in the cell cycle of Saccharomyces cerevisiae
Influence of tubulin tyrosination on the localization of microtubule plus end tracking proteins and microtubule dynamics
Influence of tubulin tyrosination on the localization of microtubule plus end tracking proteins and microtubule dynamics
Tubulin posttranslational modifications as regulators of microtubule-based functions in cells
Ensconsin, a Par-1 regulated microtubule associated protein, regulates kinesin dependent transport
Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
Author Correction: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
Tubulin islands containing slowly hydrolyzable GTP analogs regulate the mechanism and kinetics of microtubule depolymerization
Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin
Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins
α-tubulin detyrosination fine-tunes kinetochore-microtubule attachments
Kinesin motor density and dynamics in gliding microtubule motility
Microtubule nucleation by γ-tubulin [gamma-tubulin] in the cell cycle of Saccharomyces cerevisiae
Influence of tubulin tyrosination on the localization of microtubule plus end tracking proteins and microtubule dynamics
Influence of tubulin tyrosination on the localization of microtubule plus end tracking proteins and microtubule dynamics
Tubulin posttranslational modifications as regulators of microtubule-based functions in cells