Alexey Bulychev

University of Notre Dame — United States

Biochemistry, Genetics and Molecular Biology · Life Sciences

12h-index506citations18works0.02yr avg
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Research Topics

Antibiotic Resistance in Bacteria(10), Microbial Natural Products and Biosynthesis(3), Chemical Synthesis and Analysis(3), Antibiotics Pharmacokinetics and Efficacy(3), Enzyme Structure and Function(3)

Publications18 total

The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A β-Lactamases and Penicillin-binding Proteins
Journal of Biological Chemistry·2004· 71 citedOpen Access
A stabilized molten globule protein
FEBS Letters·2000· 20 cited
N-Sulfonyloxy-β-lactam Inhibitors for β-Lactamases
Tetrahedron·2000· 23 cited
The Underlying Mechanism for the Diversity of Disulfide Folding Pathways
Journal of Biological Chemistry·2000· 50 citedOpen Access
Unfolding of Hirudin Characterized by the Composition of Denatured Scrambled Isomers
Journal of Protein Chemistry·1999· 12 cited
Inhibition of the Broad Spectrum Nonmetallocarbapenamase of Class A (NMC-A) ␤-Lactamase from Enterobacter cloacae by Monocyclic ␤-Lactams* □ S
HAL (Le Centre pour la Communication Scientifique Directe)·1999Open Access
Inhibition of the Broad Spectrum Nonmetallocarbapenamase of Class A (NMC-A) β-Lactamase from Enterobacter cloacae by Monocyclic β-Lactams
Journal of Biological Chemistry·1999· 21 citedOpen Access
X-ray Structure of the Asn276Asp Variant of the <i>Escherichia coli</i> TEM-1 β-Lactamase:  Direct Observation of Electrostatic Modulation in Resistance to Inactivation by Clavulanic Acid<sup>,</sup>
Biochemistry·1999· 47 cited
Class C β-Lactamases Operate at the Diffusion Limit for Turnover of Their Preferred Cephalosporin Substrates
Antimicrobial Agents and Chemotherapy·1999· 39 citedOpen Access
Elucidation of Mechanism of Inhibition and X-ray Structure of the TEM-1 β-Lactamase from <i>Escherichia coli</i> Inhibited by a <i>N</i>-Sulfonyloxy-β-lactam
Journal of the American Chemical Society·1999· 27 cited
ChemInform Abstract: Templates for Design of Inhibitors for Serine Proteases: Application of the Program Dock to the Discovery of Novel Inhibitors for Thrombin.
ChemInform·1999
Hydrogen Bonding and Attenuation of the Rate of Enzymic Catalysis
Journal of the American Chemical Society·1998· 10 cited
6ALPHA-(HYDROXYPROPYL)PENICILLANATE ACYLATED ON NMC-A BETA-LACTAMASE FROM ENTEROBACTER CLOACAE
1998
Templates for design of inhibitors for serine proteases: Application of the program dock to the discovery of novel inhibitors for thrombin
Bioorganic & Medicinal Chemistry Letters·1998· 9 citedOpen Access
Inhibition of the NMC-A β-Lactamase by a Penicillanic Acid Derivative and the Structural Bases for the Increase in Substrate Profile of This Antibiotic Resistance Enzyme
Journal of the American Chemical Society·1998· 48 citedOpen Access
Nuances of Mechanisms and Their Implications for Evolution of the Versatile β-Lactamase Activity:  From Biosynthetic Enzymes to Drug Resistance Factors
Journal of the American Chemical Society·1997· 65 cited
Potent mechanism-based inhibition of the TEM-1 .beta.-lactamase by novel N-sulfonyloxy .beta.-lactams
Journal of the American Chemical Society·1995· 31 cited
Penem BRL 42715: An Effective Inactivator for .beta.-Lactamases
Journal of the American Chemical Society·1995· 33 cited

Frequent Co-authors

Shahriar Mobashery(15), Irina Massova(7), Jean‐Pierre Samama(7), Lionel Mourey(4), Peter Swarén(4), Marvin J. Miller(4), Lakshmi P. Kotra(4), Jui‐Yoa Chang(3), E O’Brien(3), John R. Bellettini(3), Laurent Maveyraud(2), Remek Kocz(2), Maureen Doyle(2), Brian F.P. Edwards(2), Dasantila Golemi‐Kotra(1), Samy O. Meroueh(1), Choon Kim(1), Sergei B. Vakulenko(1), Ann J. Stemmler(1), Timothy L. Stemmler(1)