| Full text | |
| Author(s): Show less - |
O'Byrne, Sean N.
[1]
;
Scott, John W.
[2, 3, 4, 5]
;
Pilotte, Joseph R.
[1]
;
Santiago, Andre da S.
[6, 7]
;
Langendorf, Christopher G.
[3, 4]
;
Oakhill, Jonathan S.
[2, 3, 4]
;
Eduful, Benjamin J.
[1]
;
Counago, Rafael M.
[6, 7]
;
Wells, Carrow I.
[1]
;
Zuercher, William J.
[1]
;
Willson, Timothy M.
[1]
;
Drewry, David H.
[1]
Total Authors: 12
|
| Affiliation: | [1] Univ North Carolina Chapel Hill, Struct Genom Consortium, UNC Eshelman Sch Pharm, Chapel Hill, NC 27599 - USA
[2] Australian Catholic Univ, Mary MacKillop Inst Hlth Res, 215 Spring St, Melbourne, Vic 3000 - Australia
[3] Univ Melbourne, St Vincents Inst, 41 Victoria Parade, Fitzroy, Vic 3065 - Australia
[4] Univ Melbourne, Dept Med, 41 Victoria Parade, Fitzroy, Vic 3065 - Australia
[5] Florey Inst Neurosci & Mental Hlth, 30 Royal Parade, Parkville, Vic 3052 - Australia
[6] Univ Estadual Campinas, Inst Biol, Dept Genet & Evolucao, Struct Genom Consortium, BR-13083886 Campinas, SP - Brazil
[7] Univ Estadual Campinas UNICAMP, Ctr Quim Med CQMED, CBMEG, BR-13083875 Campinas, SP - Brazil
Total Affiliations: 7
|
| Document type: | Journal article |
| Source: | Molecules; v. 25, n. 2 JAN 2 2020. |
| Web of Science Citations: | 1 |
| Abstract | |
The calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2) activates CAMK1, CAMK4, AMPK, and AKT, leading to numerous physiological responses. The deregulation of CAMKK2 is linked to several diseases, suggesting the utility of CAMKK2 inhibitors for oncological, metabolic and inflammatory indications. In this work, we demonstrate that STO-609, frequently described as a selective inhibitor for CAMKK2, potently inhibits a significant number of other kinases. Through an analysis of literature and public databases, we have identified other potent CAMKK2 inhibitors and verified their activities in differential scanning fluorimetry and enzyme inhibition assays. These inhibitors are potential starting points for the development of selective CAMKK2 inhibitors and will lead to tools that delineate the roles of this kinase in disease biology. (AU) | |
| FAPESP's process: | 13/50724-5 - Protein Kinase Chemical Biology Center: supporting drug development through open-access research |
| Grantee: | Paulo Arruda |
| Support Opportunities: | Research Grants - Research Partnership for Technological Innovation - PITE |
| FAPESP's process: | 19/14275-8 - Structural analysis of the kinase proteins PRPF4 and DYRK1B, from the CMGC family, and identification of small compound inhibitors |
| Grantee: | André da Silva Santiago |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 14/50897-0 - INCT 2014: Open-acess Medicinal Chemistry Centre (OpenMedChem) |
| Grantee: | Katlin Brauer Massirer |
| Support Opportunities: | Research Projects - Thematic Grants |