Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Neil Rankine"'
Autor:
Michael James, Gordon A. Hamlin, Stefan Gerhardt, David Ryan, Nash Ian Alun, Attilla Ting, Stephen J. Norris, Galith Karoutchi, Chris De Savi, Neil Rankine, David J. Hargreaves, Christine M. Wood, Sarah V. Baker, Philip A. MacFaul, Andrew David Morley, Kostas Karabelas
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 21:4215-4219
Directed screening has identified a novel series of MMP13 inhibitors that possess good levels of activity whilst possessing excellent selectivity over related MMPs. The binding mode of the series has been solved by co-crystallisation and demonstrates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edfdcf46848c274f3946020e4941981e
https://doi.org/10.1016/j.bmcl.2011.05.075
https://doi.org/10.1016/j.bmcl.2011.05.075
Autor:
Neil Rankine, Linda J. Wood, Galith Karoutchi, Michelle Coulson, Keith Oldham, Emma V. Jones, Paul A. Bethel, Stephan Krapp, Susannah J. Ford, Stefan Gerhardt, David Ryan, Matthew Grist, Peter W. Kenny, Hannes Simader, Andrew David Morley, Stuart L. Wells, Gordon A. Hamlin, Stefan Steinbacher, Jack E. Dawson, Nabil Asaad, Martin Augustin, Michael James
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:4280-4283
A series of potent Cathepsin L inhibitors with good selectivity with respect to other cysteine Cathepsins is described and SAR is discussed with reference to the crystal structure of a protein-ligand complex.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca39a993160acd7584b90a963ada1ade
https://doi.org/10.1016/j.bmcl.2009.05.071
https://doi.org/10.1016/j.bmcl.2009.05.071
Autor:
Peter Newham, Eleanor Henshaw, Philip A. MacFaul, Keith Oldham, Andrew David Morley, Neil Rankine, Christine M. Wood, David Elliot, Ken Page, Attilla Ting, Paul T. Sharpe
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 19:4832-4835
A novel approach to inhibition of the alphavbeta3 integrin is described, which uses compounds designed to generate nM potency without using the arginine binding site.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2c9ae033aabae6163e2ea27dfabe4eb
https://doi.org/10.1016/j.bmcl.2009.06.041
https://doi.org/10.1016/j.bmcl.2009.06.041
Autor:
Neil Rankine, Andrea M. Bamford, Daniel S. James, Vanessa Torr, Brown George Robert, Jonathan Bowyer, Eric J. Culbert, Eric Tang
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 10:575-579
Potent inhibition of Janus kinase 3 was found for a series of naphthyl(beta-aminoethyl)ketones (e.g. 7, pIC50 = 7.1+/-0.3). Further studies indicated that these compounds fragment in less than 1 h by retro-Michael reaction in the Jak3 in vitro ELISA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77fdff116215f7b24624a182edeea217
https://doi.org/10.1016/s0960-894x(00)00051-2
https://doi.org/10.1016/s0960-894x(00)00051-2
Autor:
Jonathan Bowyer, Vanessa Torr, Daniel S. James, Neil Rankine, Eric Tang, Brown George Robert, Andrea M. Bamford, Eric J. Culbert
Publikováno v:
ChemInform. 31
Potent inhibition of Janus kinase 3 was found for a series of naphthyl(beta-aminoethyl)ketones (e.g. 7, pIC50 = 7.1+/-0.3). Further studies indicated that these compounds fragment in less than 1 h by retro-Michael reaction in the Jak3 in vitro ELISA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3334f1fd6934daced8e044022580959f
https://doi.org/10.1002/chin.200028242
https://doi.org/10.1002/chin.200028242
Autor:
David, Elliot, Eleanor, Henshaw, Philip A, MacFaul, Andrew D, Morley, Peter, Newham, Keith, Oldham, Ken, Page, Neil, Rankine, Paul, Sharpe, Attilla, Ting, Christine M, Wood
Publikováno v:
Bioorganicmedicinal chemistry letters. 19(16)
A novel approach to inhibition of the alphavbeta3 integrin is described, which uses compounds designed to generate nM potency without using the arginine binding site.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::72cc3f3e671215a93c5c520ec608f8ec
https://pubmed.ncbi.nlm.nih.gov/19574045
https://pubmed.ncbi.nlm.nih.gov/19574045