Author

A. K. Shiau

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· 1 Cancer Biology· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Organism:C. elegans· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:DNA methylation· 1

Frequent Co-Authors

A. Desai· 2 shared K. Oegema· 2 shared A. E. Leschziner· 1 shared A. Gerson-Gurwitz· 1 shared B. Davis· 1 shared C. de Groot· 1 shared C. K. Deniston· 1 shared D. M. Snead· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersCancer Biology

A. Desai

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Control of cell proliferation by memories of mitosis

F. Meitinger, R. L. Davis, M. B. Martinez, A. K. Shiau, K. Oegema, A. Desai

The paper shows that mitotic duration memories control cell proliferation through a p53-based pathway, halting proliferation after extended or successive mitoses.

bioRxiv · Nov 14, 2022Cancer Biology

The N-terminal Tail of C. elegans CENP-A Interacts with KNL-2 and is Essential for Centromeric Chromatin Assembly

C. de Groot, J. Houston, B. Davis, A. Gerson-Gurwitz, J. Monen, K. Oegema, A. K. Shiau, A. Desai

This study identifies the N-terminal tail of C. elegans CENP-A as essential for centromeric chromatin assembly through its interaction with KNL-2, compensating for the absence of Scm3/HJURP.

bioRxiv · Dec 28, 2020Cell Biology

Parkinson's Disease-linked LRRK2 structure and model for microtubule interaction

C. K. Deniston, J. Salogiannis, S. Mathea, D. M. Snead, I. Lahiri, O. Donosa, R. Watanabe, J. Böhning, A. K. Shiau, S. Knapp, E. Villa, S. L. Reck-Peterson, A. E. Leschziner

This study reports the structure of LRRK2 and its interaction with microtubules, showing that its conformation regulates binding and affects motor protein function.

bioRxiv · Jan 6, 2020Biophysics