The Role of Tubulin Isotypes in Neuronal Microtubule Growth and Transport Processes
- Alternative title
-
Die Rolle von Tubulin Isotypen in neuronalem Mikrotubuliwachstum und in Transportprozessen
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Hamburg, Universität Hamburg, Dissertation, 2021
- Event
-
Veröffentlichung
- (where)
-
Hamburg
- (who)
-
Staats- und Universitätsbibliothek Hamburg Carl von Ossietzky
- (when)
-
2021
- Creator
-
Radwitz, Jennifer
- Contributor
-
Kneussel, Matthias
Rübhausen, Michael
- URN
-
urn:nbn:de:gbv:18-ediss-103809
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:34 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
- Radwitz, Jennifer
- Kneussel, Matthias
- Rübhausen, Michael
- Staats- und Universitätsbibliothek Hamburg Carl von Ossietzky
Time of origin
- 2021
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Mechanical communication within the microtubule through network-based analysis of tubulin dynamics
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Tubulin biochemistry confers intrinsic differences in microtubule dynamics and drug sensitivity between species
Atomistic molecular dynamics simulations of tubulin heterodimers explain the motion of a microtubule
Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins
α-tubulin detyrosination fine-tunes kinetochore-microtubule attachments
Microtubule nucleation by γ-tubulin [gamma-tubulin] in the cell cycle of Saccharomyces cerevisiae
CLIPs regulate neuronal polarization through microtubule and growth cone dynamics
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
Mechanical communication within the microtubule through network-based analysis of tubulin dynamics
Microtubule minus-end aster organization is driven by processive HSET-tubulin clusters
The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail
Tubulin biochemistry confers intrinsic differences in microtubule dynamics and drug sensitivity between species
Atomistic molecular dynamics simulations of tubulin heterodimers explain the motion of a microtubule
Tubulin polyglutamylation differentially regulates microtubule‐interacting proteins
α-tubulin detyrosination fine-tunes kinetochore-microtubule attachments
Microtubule nucleation by γ-tubulin [gamma-tubulin] in the cell cycle of Saccharomyces cerevisiae
CLIPs regulate neuronal polarization through microtubule and growth cone dynamics
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
Mechanical communication within the microtubule through network-based analysis of tubulin dynamics
Microtubule minus-end aster organization is driven by processive HSET-tubulin clusters
The force required to remove tubulin from the microtubule lattice by pulling on its α-tubulin C-terminal tail
Tubulin biochemistry confers intrinsic differences in microtubule dynamics and drug sensitivity between species