Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Matthew D. Cheeseman"'
Autor:
A. Elisa Pasqua, Swee Y. Sharp, Nicola E. A. Chessum, Angela Hayes, Loredana Pellegrino, Michael J. Tucker, Asadh Miah, Birgit Wilding, Lindsay E. Evans, Carl S. Rye, N. Yi Mok, Manjuan Liu, Alan T. Henley, Sharon Gowan, Emmanuel De Billy, Robert te Poele, Marissa Powers, Suzanne A. Eccles, Paul A. Clarke, Florence I. Raynaud, Paul Workman, Keith Jones, Matthew D. Cheeseman
Publikováno v:
Journal of Medicinal Chemistry. 66:5907-5936
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0140006 (2015)
The use of chemical tools to validate clinical targets has gained in popularity over recent years and the importance of understanding the activity, selectivity and mechanism of action of these compounds is well recognized. Dysregulation of the HSP70
Externí odkaz:
https://doaj.org/article/bfb80fbdb5aa490dbfd1aeaa0e6dea26
Autor:
G. Meirion Richards, Arjun Thapaliya, Esther N. Arwert, Gary Newton, Bradleigh Whitton, Kathy Tomlin, Rosemary Burke, Rajesh Chopra, A. Elisa Pasqua, Matthew D. Cheeseman, Rob L. M. van Montfort, Erald Shehu, Angela Hayes, Agi Skawinska, Tamas Hahner, Keith Jones, Ramya Salimraj, Birgit Wilding, Florence I. Raynaud, Olivier A. Pierrat, Nicola E. A. Chessum
Publikováno v:
Bioorganic & Medicinal Chemistry Letters
Graphical abstract
ERAP1 is a zinc-dependent M1-aminopeptidase that trims lipophilic amino acids from the N-terminus of peptides. Owing to its importance in the processing of antigens and regulation of the adaptive immune response, dysregulation
ERAP1 is a zinc-dependent M1-aminopeptidase that trims lipophilic amino acids from the N-terminus of peptides. Owing to its importance in the processing of antigens and regulation of the adaptive immune response, dysregulation
Publikováno v:
Angewandte Chemie. 129:15398-15408
Autor:
Jonathan Pettinger, Yann‐Vaï Le Bihan, Marcella Widya, Rob L. M. van Montfort, Keith Jones, Matthew D. Cheeseman
Publikováno v:
Angewandte Chemie (International Ed. in English)
The stress‐inducible molecular chaperone, HSP72, is an important therapeutic target in oncology, but inhibiting this protein with small molecules has proven particularly challenging. Validating HSP72 inhibitors in cells is difficult owing to compet
Autor:
Nicola E A, Chessum, Swee Y, Sharp, John J, Caldwell, A Elisa, Pasqua, Birgit, Wilding, Giampiero, Colombano, Ian, Collins, Bugra, Ozer, Meirion, Richards, Martin, Rowlands, Mark, Stubbs, Rosemary, Burke, P Craig, McAndrew, Paul A, Clarke, Paul, Workman, Matthew D, Cheeseman, Keith, Jones
Publikováno v:
Journal of Medicinal Chemistry
Demonstrating intracellular protein target engagement is an essential step in the development and progression of new chemical probes and potential small molecule therapeutics. However, this can be particularly challenging for poorly studied and nonca
Publikováno v:
Angewandte Chemie (International ed. in English). 56(48)
Targeted covalent inhibitors have gained widespread attention in drug discovery as a validated method to circumvent acquired resistance in oncology. This strategy exploits small-molecule/protein crystal structures to design tightly binding ligands wi
Cancer cells are heavily dependent on maintaining protein homeostasis in order to support their uncontrolled growth and proliferation. Consequently, cancer cells are vulnerable to inhibition of the various processes involved in protein homeostasis in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f55cf4f02f9faedb71c0b5bcb0910375
https://doi.org/10.1016/b978-0-12-409547-2.12395-9
https://doi.org/10.1016/b978-0-12-409547-2.12395-9
Autor:
Isaac M. Westwood, Matthew D. Cheeseman, Ian Collins, James Osborne, Rob L. M. van Montfort, Fiona Jeganathan, Martin G. Rowlands, Nadia Kadi, Keith Jones, Manjuan Liu, Norhakim Yahya, Craig McAndrew, Thomas P. Matthews, Paul Workman, Meirion Richards, Alan M. Jones, Diane Frances Lee, S.E. Dobson, Rosemary Burke
Publikováno v:
'Scientific Reports ', vol: 6, pages: 34701-1-34701-13 (2016)
Scientific Reports
Scientific Reports
The heat shock protein 70s (HSP70s) are molecular chaperones implicated in many cancers and of significant interest as targets for novel cancer therapies. Several HSP70 inhibitors have been reported, but because the majority have poor physicochemical
Autor:
Matthew D, Cheeseman, Isaac M, Westwood, Olivier, Barbeau, Martin, Rowlands, Sarah, Dobson, Alan M, Jones, Fiona, Jeganathan, Rosemary, Burke, Nadia, Kadi, Paul, Workman, Ian, Collins, Rob L M, van Montfort, Keith, Jones
Publikováno v:
Journal of Medicinal Chemistry
HSP70 is a molecular chaperone and a key component of the heat-shock response. Because of its proposed importance in oncology, this protein has become a popular target for drug discovery, efforts which have as yet brought little success. This study d