Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sean N O'Byrne"'
Autor:
Sean N. O’Byrne, John W. Scott, Joseph R. Pilotte, André da S. Santiago, Christopher G. Langendorf, Jonathan S. Oakhill, Benjamin J. Eduful, Rafael M. Couñago, Carrow I. Wells, William J. Zuercher, Timothy M. Willson, David H. Drewry
Publikováno v:
Molecules, Vol 25, Iss 2, p 325 (2020)
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 inhibitor
Externí odkaz:
https://doaj.org/article/d806b3ec018a4bf9b9a5cb50cf8208cc
Autor:
Filip Cvetko, John G. McCarron, Calum Wilson, Sean N O'Byrne, Michael P. Murphy, Stuart T. Caldwell, Richard C. Hartley
Publikováno v:
Chemical Communications (Cambridge, England)
Photouncaging delivers compounds with high spatial and temporal control to induce or inhibit biological processes but the released compounds may diffuse out. We here demonstrate that sulfonate anions can be photocaged so that a membrane impermeable c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97c523af5d2b80a73cbb82446ba2c85a
Autor:
William J. Zuercher, Christopher G. Langendorf, Rafael M. Couñago, Chenchu Lin, Alfredo Picado, Mohammad Anwar Hossain, Jonathan S. Oakhill, Dominik Awad, Joseph R. Pilotte, David H. Drewry, Carolina M. C. Catta-Preta, Daniel E. Frigo, Carrow I. Wells, P.Z. Ramos, Christopher R. M. Asquith, Sean N. O’Byrne, Timothy M. Willson, Louisa Temme, A.S. Santiago, Kevin Nay, Thomas L. Pulliam, John W. Scott, Yi Liang, Benjamin J. Eduful
Publikováno v:
Journal of Medicinal Chemistry
CAMKK2 is a serine/threonine kinase and an activator of AMPK whose dysregulation is linked with multiple diseases. Unfortunately, STO-609, the tool inhibitor commonly used to probe CAMKK2 signaling, has limitations. To identify promising scaffolds as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1dbcff8ed683ad253b52fbd8a7704dcb
https://acuresearchbank.acu.edu.au/item/8x148/hinge-binder-scaffold-hopping-identifies-potent-calcium-calmodulin-dependent-protein-kinase-kinase-2-camkk2-inhibitor-chemotypes
https://acuresearchbank.acu.edu.au/item/8x148/hinge-binder-scaffold-hopping-identifies-potent-calcium-calmodulin-dependent-protein-kinase-kinase-2-camkk2-inhibitor-chemotypes
Autor:
Chenchu Lin, David H. Drewry, Carrow I. Wells, Joseph R. Pilotte, John W. Scott, Benjamin J. Eduful, Yi Liang, Rafael M. Couñago, Carolina M. C. Catta-Preta, Alfredo Picado, Sean N. O’Byrne, Jonathan S. Oakhill, Dominik Awad, Christopher G. Langendorf, Christopher R. M. Asquith, Timothy M. Willson, Thomas L. Pulliam, Louisa Temme, Daniel E. Frigo, William J. Zuercher, P.Z. Ramos, A.S. Santiago, Kevin Nay
CAMKK2 is a serine/threonine kinase and an activator of AMPK whose dysregulation is linked with multiple diseases. Unfortunately, STO-609, the tool inhibitor commonly used to probe CAMKK2 signaling, has limitations. To identify promising scaffolds as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::103f4b3c66ec89afbef05608bfa9d132
https://doi.org/10.26434/chemrxiv.13484763
https://doi.org/10.26434/chemrxiv.13484763
Publikováno v:
Tetrahedron Lett
A concise 4-step synthesis of furo[2,3-b]pyridines, with handles in the 3- and 5-positions for palladium mediated cross-coupling reactions, is described. The synthetic route has been optimized, with only one step requiring purification by column chro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21db8426125c3444dc4f33c8ce2e0949
https://europepmc.org/articles/PMC7526865/
https://europepmc.org/articles/PMC7526865/
Autor:
Joseph R. Pilotte, Sean N. O’Byrne, Timothy M. Willson, David H. Drewry, Carrow I. Wells, Jonathan S. Oakhill, A.S. Santiago, John W. Scott, Benjamin J. Eduful, Rafael M. Couñago, William J. Zuercher, Christopher G. Langendorf
Publikováno v:
Molecules
Volume 25
Issue 2
Molecules, Vol 25, Iss 2, p 325 (2020)
Volume 25
Issue 2
Molecules, Vol 25, Iss 2, p 325 (2020)
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 inhibitor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::142293ff7edf6c8bd589a1054205cec4
https://acuresearchbank.acu.edu.au/item/8vy63/in-depth-analysis-of-kinase-cross-screening-data-to-identify-camkk2-inhibitory-scaffolds
https://acuresearchbank.acu.edu.au/item/8vy63/in-depth-analysis-of-kinase-cross-screening-data-to-identify-camkk2-inhibitory-scaffolds