Author

S. Bechstedt

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:genetic perturbation / CRISPR· 1 Assay:imaging· 1 Assay:proteomics· 1

Frequent Co-Authors

T. S. McAlear· 3 shared A. A. Lopez· 1 shared A. A. Z. Khalifa· 1 shared B. Christensen· 1 shared C. Black· 1 shared D. A. Compton· 1 shared D. Dai· 1 shared I. Vlasac· 1 shared

Activity by Year

2019-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

T. S. McAlear

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Author profile →

4 papers

Recent·Most cited

An Aurora kinase A-BOD1L1-PP2A B56 Axis promotes chromosome segregation fidelity

T. Kucharski, I. Vlasac, M. Higgs, B. Christensen, S. Bechstedt, D. A. Compton

The paper identifies an Aurora kinase A-BOD1L1-PP2A axis that promotes chromosome segregation fidelity in cancer cells and shows its role in resistance to a MCAK agonist.

Cell Reports · Feb 1, 2025Peer-reviewedCell Biology

The spindle protein CKAP2 regulates microtubule dynamics and ensures faithful chromosome segregation.

L. M. G. Paim, T. S. McAlear, A. A. Lopez, S. Bechstedt

This study identifies CKAP2 as a microtubule growth factor that regulates microtubule dynamics and ensures accurate chromosome segregation, with its loss leading to segregation errors and aneuploidy.

bioRxiv · Oct 27, 2023Cell Biology

The mitotic spindle protein CKAP2 potently increases formation and stability of microtubules

S. Bechstedt, T. S. McAlear

This study shows CKAP2 enhances microtubule nucleation and stability by reducing critical tubulin concentration and suppressing catastrophes, identifying it as a potent microtubule growth factor.

bioRxiv · Jul 20, 2021Biophysics

The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications

A. A. Z. Khalifa, M. Ichikawa, D. Dai, C. Black, K. Peri, T. S. McAlear, S. Kubo, S. Veyron, S. K. Yang, J. Vargas, J.-F. Trempe, S. Bechstedt, K. H. Bui

The paper identifies new inner junction proteins in cilia and shows they form an interaction hub involving tubulin post-translational modifications.

bioRxiv · Oct 10, 2019Biophysics