Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Kelly Le Riche"'
Autor:
Mark D. Carr, Mariusz Muzylak, David McMillan, Richard J. Franklin, Vaclav Veverka, Daniel Christopher Brookings, Joanne E. Compson, Kelly Le Riche, Laura Ellen Newnham, Carl Brendan Doyle, Thomas A Ceska, Rachael Garlish, James Petrie Turner, Jiye Shi, Bernadette Sweeney, Alistair James Henry, Patrick M. Slocombe, Jeffery Kennedy, Gill Holdsworth, Martyn K. Robinson
Publikováno v:
The Journal of biological chemistry. 287(32)
LRP5 and LRP6 are proteins predicted to contain four six-bladed β-propeller domains and both bind the bone-specific Wnt signaling antagonist sclerostin. Here, we report the crystal structure of the amino-terminal region of LRP6 and using NMR show th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::264cb99223c5808bb96a9f6cf30f0c4e
https://pubmed.ncbi.nlm.nih.gov/22696217
https://pubmed.ncbi.nlm.nih.gov/22696217
Autor:
John Robert Porter, Mark James Batchelor, Fabien Lecomte, Christoph Meier, Jean Keyaerts, Lloyd King, Jose M. Gascon-Simorte, James Thomas Reuberson, Alison Maloney, Kelly Le Riche, Jean Delgado, Mark Daniel Calmiano, Bénédicte Lallemand, Simon Lumb, Anne Marie Foley, Richard J. Franklin, Helen Edwards
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(10)
A series of 4-azaindole inhibitors of c-Met kinase is described. The postulated binding mode was confirmed by an X-ray crystal structure and series optimisation was performed on the basis of this structure. Future directions for series development ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3985a39d17773e1b2ec299ad573ae58
https://pubmed.ncbi.nlm.nih.gov/19369077
https://pubmed.ncbi.nlm.nih.gov/19369077
Autor:
Jose M. Gascon-Simorte, Mark Daniel Calmiano, James Thomas Reuberson, John B. Porter, Richard J. Franklin, Helen Edwards, Jean Delgado, Alison Maloney, Kelly Le Riche, Mark James Batchelor, Fabien Lecomte, Christoph Meier, Simon Lumb, Anne Marie Foley
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(2)
A series of quinoxaline inhibitors of c-Met kinase is described. The postulated binding mode was confirmed by an X-ray crystal structure and optimisation of the series was performed on the basis of this structure. Future directions for development of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f65a04dc5225bc746bbd873d5d54a69
https://pubmed.ncbi.nlm.nih.gov/19059779
https://pubmed.ncbi.nlm.nih.gov/19059779