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A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad

Science advances, 2018-04, Vol.4 (4), p.eaas8667-eaas8667

2018

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The Thermodynamics of Ligand Binding to the Aminoglycoside O-Nucleotidyltransferase(4′) and Variants Yields Clues about Thermophilic Properties

Biochemistry (Easton), 2019-03, Vol.58 (12), p.1579-1586

2019

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Thermodynamics of an aminoglycoside modifying enzyme with low substrate promiscuity: The aminoglycoside N3 acetyltransferase‐VIa

Proteins, structure, function, and bioinformatics, 2017-07, Vol.85 (7), p.1258-1265

2017

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Encoding of Promiscuity in an Aminoglycoside Acetyltransferase

Journal of medicinal chemistry, 2018-11, Vol.61 (22), p.10218-10227

2018

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Low‐Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad

Angewandte Chemie (International ed.), 2019-11, Vol.58 (45), p.16260-16266

International ed. in English, 2019

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“Catch and Release”: a Variation of the Archetypal Nucleotidyl Transfer Reaction

ACS catalysis, 2020-03, Vol.10 (6), p.3548-3555

2020

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Thermophilic Enzyme or Mesophilic Enzyme with Enhanced Thermostability: Can We Draw a Line?

The journal of physical chemistry. B, 2017-07, Vol.121 (29), p.7086-7094

2017

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Solvent Reorganization Plays a Temperature-Dependent Role in Antibiotic Selection by a Thermostable Aminoglycoside Nucleotidyltransferase-4

Biochemistry (Easton), 2014-09, Vol.53 (34), p.5544-5550

2014

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Ligand promiscuity through the eyes of the aminoglycoside N3 acetyltransferase IIa

Protein science, 2013-07, Vol.22 (7), p.916-928

2013

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Aminoglycoside binding and catalysis specificity of aminoglycoside 2″-phosphotransferase IVa: A thermodynamic, structural and kinetic study

Biochimica et biophysica acta, 2016-04, Vol.1860 (4), p.802-813

2016

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Hydrogen−Deuterium (H/D) Exchange Mapping of Aβ1 - 40 Amyloid Fibril Secondary Structure Using Nuclear Magnetic Resonance Spectroscopy

Biochemistry (Easton), 2005-03, Vol.44 (11), p.4434-4441

2005

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Protein Dynamics Are Influenced by the Order of Ligand Binding to an Antibiotic Resistance Enzyme

Biochemistry (Easton), 2014-01, Vol.53 (1), p.30-38

2014

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Correction to Thermodynamics and Kinetics of Association of Antibiotics with the Aminoglycoside Acetyltransferase (3)-IIIb, a Resistance-Causing Enzyme

Biochemistry (Easton), 2013-10, Vol.52 (43), p.7702-7702

2013

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Antibiotic Selection by the Promiscuous Aminoglycoside Acetyltransferase-(3)-IIIb Is Thermodynamically Achieved through the Control of Solvent Rearrangement

Biochemistry (Easton), 2011-11, Vol.50 (43), p.9309-9317

2011

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Interactions of Coenzyme A with the Aminoglycoside Acetyltransferase (3)-IIIb and Thermodynamics of a Ternary System

Biochemistry (Easton), 2010-05, Vol.49 (19), p.4036-4042

2010

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NMR Detected Hydrogen−Deuterium Exchange Reveals Differential Dynamics of Antibiotic- and Nucleotide-Bound Aminoglycoside Phosphotransferase 3′-IIIa

Journal of the American Chemical Society, 2009-06, Vol.131 (24), p.8587-8594

2009

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ATP Binding Enables Broad Antibiotic Selectivity of Aminoglycoside Phosphotransferase(3′)-IIIa: An Elastic Network Analysis

Journal of molecular biology, 2011-06, Vol.409 (3), p.450-465

2011

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Thermodynamics and Kinetics of Association of Antibiotics with the Aminoglycoside Acetyltransferase (3)-IIIb, a Resistance-Causing Enzyme

Biochemistry (Easton), 2010-05, Vol.49 (19), p.4027-4035

2010

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Deciphering interactions of the aminoglycoside phosphotransferase(3′)-IIIa with its ligands

Biopolymers, 2009-09, Vol.91 (9), p.801-809

2009

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Transient kinetics of aminoglycoside phosphotransferase(3′)-IIIa reveals a potential drug target in the antibiotic resistance mechanism

FEBS letters, 2012-11, Vol.586 (23), p.4223-4227

2012

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Correction to Thermodynamic Characterization of a Thermostable Antibiotic Resistance Enzyme, the Aminoglycoside Nucleotidyltransferase (4′)

Biochemistry (Easton), 2015-08, Vol.54 (32), p.5120-5120

2015

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Low‐Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad

Angewandte Chemie, 2019-11, Vol.131 (45), p.16406-16412

2019

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Coenzyme A Binding to the Aminoglycoside Acetyltransferase (3)-IIIb Increases Conformational Sampling of Antibiotic Binding Site

Biochemistry (Easton), 2011-12, Vol.50 (48), p.10559-10565

2011

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Molecular Determinants of Affinity for Aminoglycoside Binding to the Aminoglycoside Nucleotidyltransferase(2‘ ‘)-Ia

Biochemistry (Easton), 2006-08, Vol.45 (34), p.10243-10250

2006

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Assignment of the Four Disulfides in the N-terminal Somatomedin B Domain of Native Vitronectin Isolated from Human Plasma

The Journal of biological chemistry, 2004-08, Vol.279 (34), p.35867-35878

2004

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A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad

The Thermodynamics of Ligand Binding to the Aminoglycoside O-Nucleotidyltransferase(4′) and Variants Yields Clues about Thermophilic Properties

Thermodynamics of an aminoglycoside modifying enzyme with low substrate promiscuity: The aminoglycoside N3 acetyltransferase‐VIa

Encoding of Promiscuity in an Aminoglycoside Acetyltransferase

Low‐Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad

“Catch and Release”: a Variation of the Archetypal Nucleotidyl Transfer Reaction

Thermophilic Enzyme or Mesophilic Enzyme with Enhanced Thermostability: Can We Draw a Line?

Solvent Reorganization Plays a Temperature-Dependent Role in Antibiotic Selection by a Thermostable Aminoglycoside Nucleotidyltransferase-4

Ligand promiscuity through the eyes of the aminoglycoside N3 acetyltransferase IIa

Aminoglycoside binding and catalysis specificity of aminoglycoside 2″-phosphotransferase IVa: A thermodynamic, structural and kinetic study

Hydrogen−Deuterium (H/D) Exchange Mapping of Aβ1 - 40 Amyloid Fibril Secondary Structure Using Nuclear Magnetic Resonance Spectroscopy

Protein Dynamics Are Influenced by the Order of Ligand Binding to an Antibiotic Resistance Enzyme

Correction to Thermodynamics and Kinetics of Association of Antibiotics with the Aminoglycoside Acetyltransferase (3)-IIIb, a Resistance-Causing Enzyme

Antibiotic Selection by the Promiscuous Aminoglycoside Acetyltransferase-(3)-IIIb Is Thermodynamically Achieved through the Control of Solvent Rearrangement

Interactions of Coenzyme A with the Aminoglycoside Acetyltransferase (3)-IIIb and Thermodynamics of a Ternary System

NMR Detected Hydrogen−Deuterium Exchange Reveals Differential Dynamics of Antibiotic- and Nucleotide-Bound Aminoglycoside Phosphotransferase 3′-IIIa

ATP Binding Enables Broad Antibiotic Selectivity of Aminoglycoside Phosphotransferase(3′)-IIIa: An Elastic Network Analysis

Thermodynamics and Kinetics of Association of Antibiotics with the Aminoglycoside Acetyltransferase (3)-IIIb, a Resistance-Causing Enzyme

Deciphering interactions of the aminoglycoside phosphotransferase(3′)-IIIa with its ligands

Transient kinetics of aminoglycoside phosphotransferase(3′)-IIIa reveals a potential drug target in the antibiotic resistance mechanism

Correction to Thermodynamic Characterization of a Thermostable Antibiotic Resistance Enzyme, the Aminoglycoside Nucleotidyltransferase (4′)

Low‐Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of a Catalytic Triad

Coenzyme A Binding to the Aminoglycoside Acetyltransferase (3)-IIIb Increases Conformational Sampling of Antibiotic Binding Site

Molecular Determinants of Affinity for Aminoglycoside Binding to the Aminoglycoside Nucleotidyltransferase(2‘ ‘)-Ia

Assignment of the Four Disulfides in the N-terminal Somatomedin B Domain of Native Vitronectin Isolated from Human Plasma

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