Author

C. W. Yu

University of Toronto

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

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Genetics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Approach:biophysical modeling· 1 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:differential expression· 1 Assay:DNA methylation· 1 Organism:Drosophila· 1

Frequent Co-Authors

S. H. McLaughlin· 2 shared S. M. Freund· 2 shared A. J. Heck· 1 shared Baskar BakthavachaluiD· 1 shared Camilla RoselliiD· 1 shared D. Barford· 1 shared D. Kureisaite-Ciziene· 1 shared E. S. Fischer· 1 shared

Activity by Year

2021-2025 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiochemistry

S. H. McLaughlin

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Ataxin-2 preserves oocyte genome integrity by promoting timely premeiotic DNA replication

Vernon Monteiro, C. W. Yu, Camilla Roselli, Baskar Bakthavachalu, Mani Ramaswami, Thomas R. Hurd

This study identifies Ataxin-2 as a regulator of meiotic entry in Drosophila by downregulating Dacapo, leading to timely premeiotic DNA replication and preventing genomic damage in oocytes.

bioRxiv · Jun 13, 2025 · PreprintGenetics

Juxtaposition of Bub1 and Cdc20 on phosphorylated Mad1 during catalytic mitotic checkpoint complex assembly

E. S. Fischer, C. W. Yu, J. F. Hevler, S. H. McLaughlin, S. L. Maslen, A. J. Heck, S. M. Freund, D. Barford

This study investigates how Mps1 phosphorylation of Mad1 facilitates the assembly of the mitotic checkpoint complex by promoting interactions between Mad1, Cdc20, and Bub1.

bioRxiv · May 16, 2022Biochemistry

The bacterial actin-like cell division protein FtsA forms curved antiparallel double filaments upon binding of FtsN

T. Nierhaus, S. H. McLaughlin, F. Bürmann, D. Kureisaite-Ciziene, S. Maslen, M. J. Skehel, C. W. Yu, S. M. Freund, L. F. Funke, J. W. Chin, J. Löwe

This study shows that FtsA forms curved antiparallel double filaments when bound to FtsN, similar to MreB, and suggests these structures orient septal PG synthesis during bacterial division.

bioRxiv · Nov 8, 2021 · PreprintMicrobiology