M. Kirby

发表

Involvement of DPP‐IV catalytic residues in enzyme–saxagliptin complex formation

W. Metzler, J. Yanchunas, C. Weigelt, 2008, Protein science : a publication of the Protein Society.

Discovery of a Partial Glucokinase Activator Clinical Candidate: Diethyl ((3-(3-((5-(Azetidine-1-carbonyl)pyrazin-2-yl)oxy)-5-isopropoxybenzamido)-1H-pyrazol-1-yl)methyl)phosphonate (BMS-820132).

Steven A. Spronk, K. Behnia, J. Barrish, 2022, Journal of medicinal chemistry.

Potency, selectivity and prolonged binding of saxagliptin to DPP4: maintenance of DPP4 inhibition by saxagliptin in vitro and ex vivo when compared to a rapidly-dissociating DPP4 inhibitor

L. Hamann, M. Kirby, J. Marcinkeviciene, 2012, BMC pharmacology.

Liquid chromatography and tandem mass spectrometry method for the quantitative determination of saxagliptin and its major pharmacologically active 5-monohydroxy metabolite in human plasma: method validation and overcoming specific and non-specific binding at low concentrations.

W. Humphreys, M. Kirby, D. Boulton, 2012, Journal of chromatography. B, Analytical technologies in the biomedical and life sciences.

Design, synthesis, and SAR studies of novel polycyclic acids as potent and selective inhibitors of human 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD-1).

M. Kirby, R. Seethala, A. Nayeem, 2011, Bioorganic & medicinal chemistry letters.

Probing prime substrate binding sites of human dipeptidyl peptidase-IV using competitive substrate approach.

M. Kirby, J. Marcinkeviciene, Margaret A. Liu, 2005, Archives of biochemistry and biophysics.

Seco-prolinenitrile inhibitors of dipeptidyl peptidase IV define minimal pharmacophore requirements at P1.

L. Hamann, M. Kirby, J. Marcinkeviciene, 2006, Bioorganic & medicinal chemistry letters.

Diprolyl nitriles as potent dipeptidyl peptidase IV inhibitors.

R. Parker, L. Hamann, M. Kirby, 2005, Bioorganic & medicinal chemistry letters.

Synthesis and biological activity of 5-aryl-4-(4-(5-methyl-1H-imidazol-4-yl)piperidin-1-yl)pyrimidine analogs as potent, highly selective, and orally bioavailable NHE-1 inhibitors.

M. Kirby, Saleem Ahmad, R. Zahler, 2006, Bioorganic & medicinal chemistry letters.

Potent non-nitrile dipeptidic dipeptidyl peptidase IV inhibitors.

R. Parker, L. Hamann, M. Kirby, 2007, Bioorganic & medicinal chemistry letters.

Substituted piperidinyl glycinyl 2-cyano-4,5-methano pyrrolidines as potent and stable dipeptidyl peptidase IV inhibitors.

R. Parker, L. Hamann, M. Kirby, 2013, Bioorganic & medicinal chemistry letters.

Aminoimidazoles as bioisosteres of acylguanidines: novel, potent, selective and orally bioavailable inhibitors of the sodium hydrogen exchanger isoform-1.

M. Kirby, Saleem Ahmad, G. Chandrasena, 2004, Bioorganic & medicinal chemistry letters.

Arylcyclopropanecarboxyl guanidines as novel, potent, and selective inhibitors of the sodium hydrogen exchanger isoform-1.

K. J. Yost, M. Kirby, N. Grazier, 2001, Journal of medicinal chemistry.

DPP8 and DPP9 expression in cynomolgus monkey and Sprague Dawley rat tissues

M. Kirby, J. Rosenblum, M. Gorrell, 2013, Regulatory Peptides.

Synthesis and SAR of azolopyrimidines as potent and selective dipeptidyl peptidase-4 (DPP4) inhibitors for type 2 diabetes.

L. Hamann, M. Kirby, A. Fura, 2010, Bioorganic & medicinal chemistry letters.

Synthesis, SAR, and atropisomerism of imidazolopyrimidine DPP4 inhibitors.

C. Weigelt, L. Hamann, M. Kirby, 2010, Bioorganic & medicinal chemistry letters.

Discovery and preclinical profile of Saxagliptin (BMS-477118): a highly potent, long-acting, orally active dipeptidyl peptidase IV inhibitor for the treatment of type 2 diabetes.

R. Parker, L. Hamann, M. Kirby, 2005, Journal of medicinal chemistry.

7-Oxopyrrolopyridine-derived DPP4 inhibitors-mitigation of CYP and hERG liabilities via introduction of polar functionalities in the active site.

Wei Wang, C. Weigelt, K. Kish, 2011, Bioorganic & medicinal chemistry letters.

Optimization of activity, selectivity, and liability profiles in 5-oxopyrrolopyridine DPP4 inhibitors leading to clinical candidate (Sa)-2-(3-(aminomethyl)-4-(2,4-dichlorophenyl)-2-methyl-5-oxo-5H-pyrrolo[3,4-b]pyridin-6(7H)-yl)-N,N-dimethylacetamide (BMS-767778).

C. Weigelt, K. Kish, H. Klei, 2013, Journal of medicinal chemistry.

Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.

C. Weigelt, K. Kish, H. Klei, 2010, Journal of medicinal chemistry.

Pharmacokinetics of the Dipeptidyl Peptidase 4 Inhibitor Saxagliptin in Rats, Dogs, and Monkeys and Clinical Projections

W. Humphreys, L. Hamann, M. Kirby, 2009, Drug Metabolism and Disposition.

Inhibitor selectivity in the clinical application of dipeptidyl peptidase-4 inhibition.

M. Kirby, M. Gorrell, D. Yu, 2009, Clinical science.

Mechanism of Gly-Pro-pNA cleavage catalyzed by dipeptidyl peptidase-IV and its inhibition by saxagliptin (BMS-477118).

W. Metzler, C. Weigelt, L. Hamann, 2006, Archives of biochemistry and biophysics.

Effects of saxagliptin and sitagliptin on glycaemic control and pancreatic β‐cell mass in a streptozotocin‐induced mouse model of type 2 diabetes

M. Kirby, S. Poucher, B. Zinker, 2012, Diabetes, obesity & metabolism.

Synthesis and structure-activity relationship of 2-adamantylmethyl tetrazoles as potent and selective inhibitors of human 11β-hydroxysteroid dehydrogenase type 1 (11β-HSD1).

M. Kirby, R. Seethala, A. Nayeem, 2014, Bioorganic & medicinal chemistry letters.

Discovery of Clinical Candidate 2-((2S,6S)-2-Phenyl-6-hydroxyadamantan-2-yl)-1-(3'-hydroxyazetidin-1-yl)ethanone [BMS-816336], an Orally Active Novel Selective 11β-Hydroxysteroid Dehydrogenase Type 1 Inhibitor.

David K. Leahy, J. Barrish, M. Kirby, 2017, Journal of medicinal chemistry.

DPP8 and DPP9 expression in cynomolgus monkey and Sprague Dawley rat tissues

M. Kirby, J. Rosenblum, M. Gorrell, 2013, Regulatory Peptides.

Involvement of DPP‐IV catalytic residues in enzyme–saxagliptin complex formation

W. Metzler, J. Yanchunas, C. Weigelt, 2008, Protein science : a publication of the Protein Society.