Author

K. B. Massirer

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 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:protein structure· 3 Organism:human· 2 Research Focus:drug response / drug discovery· 1 Organism:plant (other)· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

O. Gileadi· 3 shared P. H. Godoi· 2 shared R. M. Counago· 2 shared A. M. Fala· 1 shared A. Mascarello· 1 shared A. P. Salmazo· 1 shared C. Gottschald Chiodi· 1 shared C. I. Wells· 1 shared

Activity by Year

2017-2019 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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3 shared papersBiochemistry

O. Gileadi

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Author profile →

3 papers

Recent·Most cited

The C-terminal domains SnRK2-box and ABA-box have a role in sugarcane SnRK2s auto-activation and activity

G. L. Righetto, D. Sriranganadane, L. Halabelian, C. Gottschald Chiodi, J. Elkins, K. B. Massirer, O. Gileadi, M. Menossi, R. Counago

This study investigates the role of SnRK2-box and ABA-box domains in sugarcane SnRK2s auto-activation and activity, revealing distinct regulatory mechanisms compared to Arabidopsis.

bioRxiv · Mar 26, 2019Plant 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 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