Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Timothy P. C. Rooney"'
Autor:
Simon R. Stockwell, Duncan E. Scott, Gerhard Fischer, Estrella Guarino, Timothy P. C. Rooney, Tzu-Shean Feng, Tommaso Moschetti, Rajavel Srinivasan, Esther Alza, Alice Asteian, Claudio Dagostin, Anna Alcaide, Mathieu Rocaboy, Beata Blaszczyk, Alicia Higueruelo, Xuelu Wang, Maxim Rossmann, Trevor R. Perrior, Tom L. Blundell, David R. Spring, Grahame McKenzie, Chris Abell, John Skidmore, Marko Hyvönen, Ashok R. Venkitaraman
The protein kinase Aurora A, and its close relative, Aurora B, regulate human cell division. Aurora A is frequently overexpressed in cancers of the breast, ovary, pancreas and blood, provoking genome instability and resistance to anti-mitotic chemoth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d989dbb8823cab17b2cfdce4dae22a7b
https://doi.org/10.1101/2023.03.22.533679
https://doi.org/10.1101/2023.03.22.533679
Autor:
Timothy P. C. Rooney, Gregory G. Aldred, Helen K. Boffey, Henriëtte M. G. Willems, Simon Edwards, Stephen J. Chawner, Duncan E. Scott, Christopher Green, David Winpenny, John Skidmore, Jonathan H. Clarke, Stephen P. Andrews
Owing to their central role in regulating cell signaling pathways, the phosphatidylinositol 5-phosphate 4-kinases (PI5P4Ks) are attractive therapeutic targets in diseases such as cancer, neurodegeneration, and immunological disorders. Until now, tool
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d160b7c900b0f29940d1fd8d175c7fc
Autor:
John Skidmore, Jonathan H. Clarke, Elliott D. Bayle, Tashfina Mirza, Stephen P. Andrews, Henriëtte M. G. Willems, Duncan Scott, Timothy P. C. Rooney
Publikováno v:
ACS Med Chem Lett
[Image: see text] Bifunctional molecules known as PROTACs simultaneously bind an E3 ligase and a protein of interest to direct ubiquitination and clearance of that protein, and they have emerged in the past decade as an exciting new paradigm in drug
Autor:
Helen K. Boffey, Timothy P. C. Rooney, Henriette M. G. Willems, Simon Edwards, Christopher Green, Tina Howard, Derek Ogg, Tamara Romero, Duncan E. Scott, David Winpenny, James Duce, John Skidmore, Jonathan H. Clarke, Stephen P. Andrews
Phosphatidylinositol 5-phosphate 4-kinases (PI5P4Ks) are emerging as attractive therapeutic targets in diseases, such as cancer, immunological disorders, and neurodegeneration, owing to their central role in regulating cell signaling pathways that ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3436caf3f254cd663c0a8c1e1751a60
https://www.repository.cam.ac.uk/handle/1810/334446
https://www.repository.cam.ac.uk/handle/1810/334446
Autor:
Matthias Schiedel, Katrina H. Andrews, Corentine M.C. Laurin, Joseph P. Bluck, Stuart J. Conway, Prakriti Kalra, Panagis Filippakopoulos, James Clayton, Anthony K. N. Chan, Amy R. Scorah, Oleg Fedorov, Ester M. Hammond, Mustafa Moroglu, Kayla B. Vinh, William C. K. Pomerantz, Richard I. Cooper, Wilian A. Cortopassi, Pascal Heitel, Robert S. Paton, Anna Skwarska, Gabriella T. Perell, Kirsten E. Christensen, Larissa See, Hannah Bolland, Timothy P. C. Rooney, Sarah Picaud, Philip C. Biggin, Michael Brand
Publikováno v:
Journal of Medicinal Chemistry
CREBBP (CBP/KAT3A) and its paralogue EP300 (KAT3B) are lysine acetyltransferases (KATs) that are essential for human development. They each comprise 10 domains through which they interact with >400 proteins, making them important transcriptional co-a
Autor:
Lukass Jursins, David S. Hewings, Katie R. Lewendon, Angelina R Measures, Tom D. Heightman, Timothy P. C. Rooney, Natalie H. Theodoulou, Stuart J. Conway, Laura E. Jennings
Publikováno v:
Angewandte Chemie (International Ed. in English)
A range of isoxazole‐containing amino acids was synthesized that displaced acetyl‐lysine‐containing peptides from the BAZ2A, BRD4(1), and BRD9 bromodomains. Three of these amino acids were incorporated into a histone H4‐mimicking peptide and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23ee6b52f1c8d152bc0e0746b02fd79a
Autor:
Michael, Brand, Angelina R, Measures, Angelina M, Measures, Brian G, Wilson, Wilian A, Cortopassi, Rikki, Alexander, Matthias, Höss, David S, Hewings, Timothy P C, Rooney, Robert S, Paton, Stuart J, Conway
Publikováno v:
ACS Chemical Biology. 10:22-39
Bromodomains are protein modules that bind to acetylated lysine residues. Their interaction with histone proteins suggests that they function as "readers" of histone lysine acetylation, a component of the proposed "histone code". Bromodomain-containi
Autor:
Amber L. Thompson, David C. Pryde, Wilian A. Cortopassi, Martin Philpott, Oleg Fedorov, Panagis Filippakopoulos, Sarah Martin, Timothy P. C. Rooney, Minghua Wang, Anthony Tumber, Duncan Hay, Sarah Picaud, Susanne Müller, Stuart J. Conway, Andrew Simon Cook, Stefan Knapp, Paul Brennan, Robert S. Paton, Catherine M. Rogers, Tom D. Heightman
Publikováno v:
Angewandte Chemie (International Ed. in English)
The benzoxazinone and dihydroquinoxalinone fragments were employed as novel acetyl lysine mimics in the development of CREBBP bromodomain ligands. While the benzoxazinone series showed low affinity for the CREBBP bromodomain, expansion of the dihydro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ddd6664f2aa25ee6845d93868b7b689
https://doi.org/10.1002/anie.201402750
https://doi.org/10.1002/anie.201402750
Lysine acetylation is known to play an important role in processes that relate to cancer. Consequently, there has been much interest in developing inhibitors of the enzymes that add an acetyl group to the e-nitrogen atom of lysine, lysine/histone ace
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06404bbfcceca9f2240e72357a9f61e9
https://doi.org/10.1016/b978-0-12-800206-3.00022-7
https://doi.org/10.1016/b978-0-12-800206-3.00022-7
Autor:
Michael Brand, David S. Hewings, Brian G Wilson, Angelina R Measures, Robert S. Paton, Wilian A. Cortopassi, Rikki Alexander, Timothy P. C. Rooney, Stuart J. Conway, Matthias Höss
Publikováno v:
ACS Chemical Biology. 11:1148-1148