Author

W. Zuercher

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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Pharmacology & Toxicology· 3 Biochemistry· 2 Cancer Biology· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 8 Research Focus:drug response / drug discovery· 7 Organism:human· 3 Assay:proteomics· 2 Organism:C. elegans· 1

Frequent Co-Authors

C. I. Wells· 3 shared D. Drewry· 3 shared A. Picado· 2 shared C. Eyers· 2 shared C. R. M. Asquith· 2 shared C. Wells· 2 shared D. Fernig· 2 shared D. H. Drewry· 2 shared

Activity by Year

2018-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersCancer Biology

C. I. Wells

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

SGC-CLK-1 (CAF-170) a chemical probe for the Cdc2-Like kinases CLK1, CLK2, and CLK4

D. Tiek, C. I. Wells, M. Schroder, X. Song, C. A. Ferrer, A. Goenka, R. Iglesia, M. Lu, B. Hu, F. Kwarcinski, P. Sintha, C. de Silva, M. A. Hossain, A. Picado, W. Zuercher, , D. Drewry

This paper identifies and characterizes SGC-CLK-1, a potent inhibitor of CLK1, CLK2, and CLK4, showing its selectivity and effects on SR protein phosphorylation and localization.

bioRxiv · Dec 15, 2022 · PreprintCancer Biology

A Survey of the Kinome Pharmacopeia Reveals Multiple Scaffolds and Targets for the Development of Novel Anthelmintics

J. Knox, W. Zuercher, P. J. Roy

The paper identifies nematode-specific kinase targets and small molecule scaffolds for developing novel anthelmintics by screening vertebrate kinase inhibitors in C. elegans.

bioRxiv · Aug 20, 2020Pharmacology & Toxicology

In depth analysis of kinase cross screening data to identify CAMKK2 inhibitory scaffolds

S. O'Byrne, J. W. Scott, J. R. Pilotte, A. d. S. Santiago, C. G. Langendorf, J. S. Oakhill, B. J. Eduful, R. M. Counago, C. I. Wells, W. Zuercher, T. Willson, D. H. Drewry

This paper reviews CAMKK2's role in biology and disease, identifies starting points for inhibitor development using literature and databases, and highlights potential for selective inhibitors in oncology, metabolism, and inflammation.

bioRxiv · Jan 8, 2020Cancer Biology

The Kinase Chemogenomic Set (KCGS): An open science resource for kinase vulnerability identification

C. I. Wells, H. Al-Ali, D. M. Andrews, C. R. M. Asquith, A. D. Axtman, M. Chung, I. Dikic, D. Ebner, J. Elkins, P. Ettmayer, C. Fischer, M. Frederiksen, N. S. Gray, S. B. Hatch, S. Knapp, , D. H. Drewry

The paper introduces the Kinase Chemogenomic Set (KCGS), a curated collection of 187 selective kinase inhibitors covering 215 human kinases, for use in cell-based screens.

bioRxiv · Dec 22, 2019Cell Biology

Design and evaluation of novel 4-anilinoquinolines and quinazolines as EGFR inhibitors in lung cancer and chordoma

C. R. M. Asquith, K. A. Maffuid, T. Laitinen, C. D. Torrice, G. J. Tizzard, C. Alamillo-Ferrer, K. M. Koshlap, D. J. Crona, W. Zuercher

The paper designs and evaluates novel 4-anilinoquinolines and quinazolines as EGFR inhibitors, identifying a potent compound for lung cancer and chordoma treatment.

bioRxiv · Feb 11, 2019 · PreprintPharmacology & Toxicology

Utilizing comprehensive and mini-kinome panels to optimize the selectivity of quinoline inhibitors for cyclin G associated kinase (GAK)

C. Asquith, C. Hopkins, D. K. Treiber, W. Zuercher

The paper demonstrates using kinase mini-panels and kinome-wide panels to develop a selective quinoline inhibitor for cyclin G associated kinase (GAK).

bioRxiv · Nov 17, 2018Pharmacology & Toxicology

New tools for carbohydrate sulphation analysis: Heparan Sulphate 2-O-sulphotranserase (HS2ST) is a target for small molecule protein kinase inhibitors

D. P. Byrne, Y. Li, K. Ramakrishnan, I. Barsukov, E. Yates, C. Eyers, D. Papy-Garcia, S. Chantepie, V. Pagadala, J. Liu, C. Wells, D. Drewry, W. Zuercher, N. Berry, D. Fernig, P. A. Eyers

This paper introduces a new non-radioactive assay for HS2ST activity using a synthetic fluorescent substrate and identifies protein kinase inhibitors that inhibit HS2ST-catalyzed sulphation.

bioRxiv · Apr 6, 2018Biochemistry

New tools for evaluating protein tyrosine sulphation: Tyrosyl Protein Sulphotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors

P. Eyers, D. Byrne, P. Ngamlert, Y. Li, K. Ramakrishnan, C. Eyers, C. Wells, D. Drewry, W. Zuercher, N. Berry, D. Fernig

The paper develops a non-radioactive assay to quantify tyrosine sulphation by TPST1 and TPST2 and identifies RAF kinase inhibitors as potential TPST inhibitors.

bioRxiv · Apr 6, 2018Biochemistry