Author

K. W. Tan

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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Biochemistry· 4 Cell Biology· 3 Bioengineering· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:cell signaling & trafficking· 5 Assay:proteomics· 4 Research Focus:development & morphogenesis· 3 Research Focus:drug response / drug discovery· 3 Organism:human· 3 Research Focus:chromatin & epigenetic regulation· 2 Organism:yeast· 2

Frequent Co-Authors

C. T. Lim· 4 shared B. Canal· 3 shared F. Weissmann· 3 shared J. F. Diffley· 3 shared K. Labib· 3 shared M. Howell· 3 shared M. Wu· 3 shared R. Beale· 3 shared

Activity by Year

2018-2024 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiochemistry

C. T. Lim

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Cell Cycle Regulation has Shaped Budding Yeast Replication Origin Structure and Function

J. Diffley, C. T. Lim, T. C. Miller, K. W. Tan, s. Talele, A. Early, P. East, H. Sanchez, N. H. Dekker, A. Costa

The paper shows that CDK regulation influences MCM helicase loading at yeast origins, revealing how cell cycle control has shaped origin structure and function.

bioRxiv · Jan 10, 2024Biochemistry

ATPase activity of DFCP1 controls selective autophagy

V. Nähse, C. Raiborg, K. W. Tan, S. Mørk, M. L. Torgersen, E. M. Wenzel, M. Nager, V. T. Salo, T. Johansen, E. Ikonen, K. O. Schink, H. Stenmark

This study identifies DFCP1 as an ATPase essential for omegasome constriction and selective autophagy by facilitating autophagosome release.

bioRxiv · Feb 24, 2022Cell Biology

Dephosphorylation of the pre-initiation complex during S-phase is critical for origin firing

F. L. V. Jenkinson, K. W. Tan, B. Schöpf, M. M. Santos, I. Phanada, P. Zegerman

This study shows that dephosphorylation of Sld2 and Sld3 by PP2A and PP4 phosphatases is essential for replication origin firing in yeast.

bioRxiv · Nov 2, 2021 · PreprintCell Biology

Identifying SARS-CoV-2 Antiviral Compounds by Screening for Small Molecule Inhibitors of nsp5 Main Protease

C. Basier, R. Beale, G. Bineva-Todd, B. Canal, J. F. Curran, T. D. Deegan, J. F. Diffley, R. Fujisawa, M. Howell, D. Joshi, K. Labib, C. T. Lim, J. Milligan, H. Nagaraj, N. O'Reilly, , T. U. Zeisner

This study identifies small molecule inhibitors of SARS-CoV-2 nsp5 main protease, finding calpain inhibitor I and peptidyl fluoromethylketones with potent antiviral activity.

bioRxiv · Apr 7, 2021Biochemistry

Identifying SARS-CoV-2 Antiviral Compounds by Screening for Small Molecule Inhibitors of Nsp3 Papain-like Protease

L. A. Armstrong, R. Beale, G. Bineva-Todd, B. Canal, J. F. Diffley, L. S. Drury, M. Howell, Y. Kulathu, K. Labib, C. T. Lim, J. Milligan, N. O'Reilly, E. Ozono, K. W. Tan, R. Ulferts, , J. Zeng

This study identifies two small molecule inhibitors of SARS-CoV-2 Nsp3 PLpro that inhibit viral replication in cell culture.

bioRxiv · Apr 7, 2021Biochemistry

Identification of SARS-CoV-2 Antiviral Compounds by Screening for Small Molecule Inhibitors of the nsp14 RNA Cap Methyltransferase

C. Basier, S. Basu, R. Beale, B. Canal, V. H. Cowling, J. F. Curran, T. D. Deegan, J. F. Diffley, L. S. Drury, R. Fujisawa, M. Howell, K. Labib, C. T. Lim, T. Mak, A. W. McClure, , T. U. Zeisner

This study identifies four small molecule inhibitors of SARS-CoV-2 nsp14 RNA cap methyltransferase, with three showing synergy with remdesivir in antiviral assays.

bioRxiv · Apr 7, 2021Bioengineering

JIP4 is recruited by the phosphoinositide-binding protein Phafin2 to promote recycling tubules on macropinosomes

K. W. Tan, V. Nähse, C. Campsteijn, A. Brech, K. O. Schink, H. Stenmark

This study identifies JIP4 and Phafin2 as components of a tubular recycling pathway from macropinosomes, showing JIP4 recruitment via Phafin2's PtdIns3P binding.

bioRxiv · Sep 29, 2020Cell Biology

Molecular basis for the maintenance of lipid asymmetry in the outer membrane of Escherichia coli

J. Yeow, K. W. Tan, D. A. Holdbrook, Z.-S. Chong, J. K. Marzinek, P. J. Bond, S. S. Chng

The paper defines the molecular architecture of the OmpC-MlaA complex in E. coli and shows how it transports phospholipids across the outer membrane to maintain lipid asymmetry.

bioRxiv · Feb 8, 2018Biochemistry