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A new family of covalent inhibitors block nucleotide binding to the active site of pyruvate kinase

DOI: 10.1042/BJ20121014 DOI Help

Authors: Hugh Morgan (University of Edinburgh) , Martin J. Walsh (NIH Center for Translational Therapeutics, National Human Genome Research Institute, Rockville, USA) , Elizabeth Blackburn (The University of Edinburgh) , Martin Wear (The University of Edinburgh) , Matthew Boxer (NIH Center for Translational Therapeutics, National Human Genome Research Institute, Rockville, USA) , Min Shen (NIH Center for Translational Therapeutics, National Human Genome Research Institute, Rockville, USA) , Iain Mcnae (University of Edinburgh) , Matthew Nowicki (University of Edinburgh) , Paul A.m. Michels (Université catholique de Louvain, Brussels, Belgium) , Douglas Auld (NIH Center for Translational Therapeutics, National Human Genome Research Institute, Rockville, USA) , Linda Fothergill-gilmore (The University of Edinburgh) , Malcolm Walkinshaw (University of Edinburgh) , Henrike Veith (NIH Center for Translational Therapeutics, National Human Genome Research Institute, Rockville, USA)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical Journal

State: Published (Approved)
Published: September 2012
Diamond Proposal Number(s): 7613

Abstract: Leishmania mexicana, lysine covalent modification, nucleotide binding, pyruvate kinase, Covalent inhibition, covalent inhibitors block nucleotide

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography