Author

P. H. Godoi

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· 2 Cell Biology· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:drug response / drug discovery· 3 Organism:human· 2 Assay:protein structure· 2 Research Focus:protein structure prediction· 1

Frequent Co-Authors

J. M. Elkins· 3 shared W. J. Zuercher· 3 shared C. I. Wells· 2 shared C. R. M. Asquith· 2 shared J. M. Bennett· 2 shared K. B. Massirer· 2 shared O. Gileadi· 2 shared R. M. Counago· 2 shared

Activity by Year

2017-2019 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiochemistry

J. M. Elkins

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Author profile →

4 papers

Recent·Most cited

Structural and binding studies of human CAMKK2 kinase domain bound to small molecule ligands

G. S. Profeta, C. V. dos Reis, P. H. Godoi, A. M. Fala, R. Satori, A. P. Salmazo, P. Z. Ramos, K. B. Massirer, J. M. Elkins, D. H. Drewry, O. Gileadi, R. M. Counago

This study presents six novel co-structures of CAMKK2 bound to small molecule ligands and shows some ligand binding is enthalpy driven.

bioRxiv · Feb 1, 2019 · PreprintBiochemistry

SGC-GAK-1: a chemical probe for cyclin G associated kinase (GAK)

C. R. M. Asquith, B.-T. Berger, J. Wan, J. M. Bennett, M. P. East, J. M. Elkins, O. Fedorov, P. H. Godoi, D. M. Hunter, S. Knapp, S. Mueller, C. I. Wells, H. S. Earp, T. M. Willson, W. J. Zuercher

The paper describes SGC-GAK-1, a selective GAK inhibitor, and identifies a related compound that inhibits RIPK2 without GAK activity, providing tools to study GAK and RIPK2 biology.

bioRxiv · Jul 25, 2018Cell Biology

Identification and Optimization of 4-Anilinoquinolines as Inhibitors of Cyclin G Associated Kinase

C. R. M. Asquith, T. Laitinen, J. M. Bennett, P. H. Godoi, G. J. Tizzard, J. M. Elkins, T. M. Willson, W. J. Zuercher

The paper identifies 4-anilinoquinolines as potent GAK inhibitors with high selectivity and suggests their potential as tools for studying GAK's role in infectious diseases.

bioRxiv · Apr 11, 2017Pharmacology & Toxicology

Structural characterization of human Vaccinia-Related Kinases (VRK) bound to small-molecule inhibitors identifies different P-loop conformations

R. M. Counago, C. K. Allerston, P. Savitsky, H. Azevedo, P. H. Godoi, C. I. Wells, A. Mascarello, F. H. de Souza Gama, K. B. Massirer, W. J. Zuercher, C. R. W. Guimaraes, O. Gileadi

The paper identifies BI-D1870 as a starting point for VRK inhibitors and reports co-crystal structures revealing different P-loop conformations in VRK1 and VRK2.

bioRxiv · Mar 2, 2017Biochemistry