Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Michelle L. Heathcote"'
Autor:
Heather Hobbs, Rick P. C. Cousins, Caroline Whitworth, Ruth R. Osborn, Cesar Ramirez-Molina, Giorgia Vicentini, Chris Ioannou, Chun-wa Chung, Jeremy John Payne, Michelle L. Heathcote, Michael David Barker, Sebastien Andre Campos, Paul Faulder, Mary A. Morse, William L. Rumsey, John Liddle, Daniel Terence Tape, John Martin Pritchard, Rick Williamson, Duncan S. Holmes, Paul Bamborough
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 22:5222-5226
The lead optimization of a series of potent azaindole IKK2 inhibitors is described. Optimization of the human whole blood activity and selectivity over IKK1 in parallel led to the discovery of 16, a potent and selective IKK2 inhibitor showing good ef
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66c01094b7cd1f9f02ade498d99ac86e
https://doi.org/10.1016/j.bmcl.2012.06.065
https://doi.org/10.1016/j.bmcl.2012.06.065
Autor:
Peter Francis, Bill Leavens, Michelle L. Heathcote, Melanie Leveridge, Chun-wa Chung, Paul Homes, Argyrides Argyrou, Jordi Munoz-Muriedas, Michelle Gee, Laura Williams, Stuart M. Baddeley, Sue Hutchinson, Anthony Shillings, Emma J. Jones, Angela Bridges
Publikováno v:
SLAS Discovery. 17:39-48
A high-throughput RapidFire mass spectrometry assay is described for the JMJD2 family of Fe(2+), O(2), and α-ketoglutarate-dependent histone lysine demethylases. The assay employs a short amino acid peptide substrate, corresponding to the first 15 a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::557947806d65ab6979c82184961e81b9
https://doi.org/10.1177/1087057111416660
https://doi.org/10.1177/1087057111416660
Autor:
Zoë A. Hughes-Thomas, Michelle A. Jones, Hui Hong, Peter F. Leadlay, Victor M. Bolanos-Garcia, Michelle L. Heathcote, Barbara M. Harvey, Rebecca M. Goss, Jonathan B. Spencer, Wolfgang Kroutil, James Staunton
Publikováno v:
Chembiochem : a European journal of chemical biology. 7(9)
Polyether ionophores, such as monensin A, are known to be biosynthesised, like many other antibiotic polyketides, on giant modular polyketide synthases (PKSs), but the intermediates and enzymes involved in the subsequent steps of oxidative cyclisatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a6734fc2154663f27d2b60874cf81bd
https://pubmed.ncbi.nlm.nih.gov/16897798
https://pubmed.ncbi.nlm.nih.gov/16897798
Publikováno v:
Chemistrybiology. 8(2)
Background: Modular polyketide synthases (PKSs) function as molecular assembly lines in which polyketide chains are assembled by successive addition of chain extension units. At the end of the assembly line, there is usually a covalently linked type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e72fb8951f77a1053405bfb7e258e65
https://pubmed.ncbi.nlm.nih.gov/11251294
https://pubmed.ncbi.nlm.nih.gov/11251294
Autor:
Barbara M. Harvey, Hui Hong, Michelle A. Jones, Zoë A. Hughes-Thomas, Rebecca M. Goss, Michelle L. Heathcote, Victor M. Bolanos-Garcia, Wolfgang Kroutil, James Staunton, Peter F. Leadlay, Jonathan B. Spencer
Publikováno v:
ChemBioChem; Sep2006, Vol. 7 Issue 9, p1435-1442, 8p