Author

R. M. Counago

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· 3 Cancer Biology· 2 Pharmacology & Toxicology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 7 Research Focus:drug response / drug discovery· 5 Assay:protein structure· 3 Organism:human· 2 Organism:Arabidopsis· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1 Organism:rat· 1

Frequent Co-Authors

C. I. Wells· 5 shared D. H. Drewry· 5 shared O. Gileadi· 4 shared P. Zonzini Ramos· 3 shared A. d. S. Santiago· 2 shared C. G. Langendorf· 2 shared J. M. Elkins· 2 shared J. S. Oakhill· 2 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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5 shared papersCancer Biology

C. I. Wells

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

SGC-CAMKK2-1: A chemical probe for CAMKK2

C. I. Wells, Y. Liang, T. L. Pulliam, C. Lin, D. Awad, B. Eduful, S. O Byrne, M. A. Hossain, C. Catta-Preta, P. Zonzini Ramos, O. Gileadi, C. Gileadi, R. M. Counago, B. Stork, C. G. Langendorf, , D. H. Drewry

This paper introduces SGC-CAMKK2-1, a selective chemical probe for CAMKK2, demonstrating its potential as a tool to study the therapeutic benefits of CAMKK2 inhibition.

Cells · Jan 11, 2023Peer-reviewedCancer Biology

An open source plant kinase chemogenomics set

M. F. Ercoli, P. Zonzini Ramos, R. Jain, J. Pilotte, O. X. Dong, T. Thompson, C. I. Wells, J. M. Elkins, A. M. Edwards, R. M. Counago, D. H. Drewry, P. C. Ronald

The paper presents a plant kinase chemogenomics set, identifying compounds that affect root development in Arabidopsis and rice, with implications for understanding plant kinase function.

bioRxiv · Jun 18, 2022Plant Biology

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

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

Structural Analysis of Inhibitor Binding to CAMKK1 Identifies Features Necessary for Design of Specific Inhibitors

A. d. S. Santiago, R. M. Counago, P. Zonzini Ramos, P. H. C. Godoi, K. B. B. Massirer, O. Gileadi, J. Elkins

The paper determines the crystal structure of CAMKK1 with inhibitors and identifies structural differences from CAMKK2 to guide the design of specific inhibitors.

bioRxiv · Mar 31, 2018Biochemistry

In depth analysis of kinase cross screening data to identify chemical starting points for inhibition of the Nek family of kinases

C. I. Wells, N. R. Kapadia, R. M. Counago, D. H. Drewry

The paper analyzes kinase cross-screening data to identify potential chemical starting points for inhibiting Nek kinases, aiming to advance drug discovery for these understudied targets.

bioRxiv · May 14, 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