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Versatility of Aminoglycosides and Prospects for Their Future

Clinical Microbiology Reviews, 2003-07, Vol.16 (3), p.430-450

2003

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Crystal Structure of Carbapenemase OXA-58 from Acinetobacter baumannii

Antimicrobial agents and chemotherapy, 2014-04, Vol.58 (4), p.2135-2143

2014

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C6 Hydroxymethyl-Substituted Carbapenem MA-1-206 Inhibits the Major Acinetobacter baumannii Carbapenemase OXA-23 by Impeding Deacylation

mBio, 2022-04, Vol.13 (3), p.e0036722-e0036722

2022

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Novel Aminoglycoside 2″-Phosphotransferase Identified in a Gram-Negative Pathogen

Antimicrobial Agents and Chemotherapy, 2013-01, Vol.57 (1), p.452-457

2013

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Effects of Inactivation of d,d-Transpeptidases of Acinetobacter baumannii on Bacterial Growth and Susceptibility to β-Lactam Antibiotics

Antimicrobial agents and chemotherapy, 2022-01, Vol.66 (1), p.e0172921-e0172921

2022

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Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase

Antimicrobial agents and chemotherapy, 2019-10, Vol.63 (10)

2019

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A Synthetic Dual Drug Sideromycin Induces Gram-Negative Bacteria To Commit Suicide with a Gram-Positive Antibiotic

Journal of medicinal chemistry, 2018-05, Vol.61 (9), p.3845-3854

2018

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Class A Carbapenemase FPH-1 from Francisella philomiragia

Antimicrobial Agents and Chemotherapy, 2012-06, Vol.56 (6), p.2852-2857

2012

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Multiplex PCR for Detection of Aminoglycoside Resistance Genes in Enterococci

Antimicrobial Agents and Chemotherapy, 2003-04, Vol.47 (4), p.1423-1426

2003

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Source of Phosphate in the Enzymic Reaction as a Point of Distinction among Aminoglycoside 2″-Phosphotransferases

The Journal of biological chemistry, 2009-03, Vol.284 (11), p.6690-6696

2009

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Class D β-Lactamases: Are They All Carbapenemases?

Antimicrobial agents and chemotherapy, 2014-04, Vol.58 (4), p.2119-2125

2014

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Bulky “Gatekeeper” Residue Changes the Cosubstrate Specificity of Aminoglycoside 2″-Phosphotransferase IIa

Antimicrobial Agents and Chemotherapy, 2013-08, Vol.57 (8), p.3763-3766

2013

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The Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside-2′′-Phosphotransferase-IIa [APH(2′′)-IIa] Provide Insights into Substrate Selectivity in the APH(2′′) Subfamily

Journal of Bacteriology, 2009-07, Vol.191 (13), p.4133-4143

2009

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Catalytic Mechanism of Penicillin-Binding Protein 5 of Escherichia coli

Biochemistry (Easton), 2007-09, Vol.46 (35), p.10113-10121

2007

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Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6')-Im

Microbial cell, 2017-11, Vol.4 (12), p.402-410

2017

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Co-opting the Cell Wall in Fighting Methicillin-Resistant Staphylococcus aureus: Potent Inhibition of PBP 2a by Two Anti-MRSA β-Lactam Antibiotics

Journal of the American Chemical Society, 2008-07, Vol.130 (29), p.9212-9213

2008

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Mutant APH(2″)-IIa Enzymes with Increased Activity against Amikacin and Isepamicin

Antimicrobial Agents and Chemotherapy, 2010-04, Vol.54 (4), p.1590-1595

2010

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Revisiting the Nucleotide and Aminoglycoside Substrate Specificity of the Bifunctional Aminoglycoside Acetyltransferase(6′)-Ie/Aminoglycoside Phosphotransferase(2″)-Ia Enzyme

The Journal of biological chemistry, 2012-12, Vol.287 (52), p.43262-43269

2012

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A surface loop modulates activity of the Bacillus class D β-lactamases

Journal of structural biology, 2020-08, Vol.211 (2), p.107544-107544, Article 107544

2020

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The crystal structures of CDD-1, the intrinsic class D β-lactamase from the pathogenic Gram-positive bacterium Clostridioides difficile, and its complex with cefotaxime

Journal of structural biology, 2019-12, Vol.208 (3), p.107391-107391, Article 107391

2019

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The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D β‐lactamases

Acta crystallographica. Section D, Structural biology, 2017-08, Vol.73 (8), p.692-701

2017

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Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside‐2′′‐phosphotransferases

Acta crystallographica. Section D, Biological crystallography., 2019-12, Vol.75 (12), p.1129-1137

2019

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Kinetic and Structural Requirements for Carbapenemase Activity in GES-Type β‑Lactamases

Biochemistry (Easton), 2015-01, Vol.54 (2), p.588-597

2015

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Mechanistic Basis for the Action of New Cephalosporin Antibiotics Effective against Methicillin- and Vancomycin-resistant Staphylococcus aureus

The Journal of biological chemistry, 2006-04, Vol.281 (15), p.10035-10041

2006

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The Basis for Resistance to β-Lactam Antibiotics by Penicillin-binding Protein 2a of Methicillin-resistant Staphylococcus aureus

The Journal of biological chemistry, 2004-09, Vol.279 (39), p.40802-40806

2004

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Versatility of Aminoglycosides and Prospects for Their Future

Crystal Structure of Carbapenemase OXA-58 from Acinetobacter baumannii

C6 Hydroxymethyl-Substituted Carbapenem MA-1-206 Inhibits the Major Acinetobacter baumannii Carbapenemase OXA-23 by Impeding Deacylation

Novel Aminoglycoside 2″-Phosphotransferase Identified in a Gram-Negative Pathogen

Effects of Inactivation of d,d-Transpeptidases of Acinetobacter baumannii on Bacterial Growth and Susceptibility to β-Lactam Antibiotics

Structural Insights into the Mechanism of Carbapenemase Activity of the OXA-48 β-Lactamase

A Synthetic Dual Drug Sideromycin Induces Gram-Negative Bacteria To Commit Suicide with a Gram-Positive Antibiotic

Class A Carbapenemase FPH-1 from Francisella philomiragia

Multiplex PCR for Detection of Aminoglycoside Resistance Genes in Enterococci

Source of Phosphate in the Enzymic Reaction as a Point of Distinction among Aminoglycoside 2″-Phosphotransferases

Class D β-Lactamases: Are They All Carbapenemases?

Bulky “Gatekeeper” Residue Changes the Cosubstrate Specificity of Aminoglycoside 2″-Phosphotransferase IIa

The Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside-2′′-Phosphotransferase-IIa [APH(2′′)-IIa] Provide Insights into Substrate Selectivity in the APH(2′′) Subfamily

Catalytic Mechanism of Penicillin-Binding Protein 5 of Escherichia coli

Aminoglycoside resistance profile and structural architecture of the aminoglycoside acetyltransferase AAC(6')-Im

Co-opting the Cell Wall in Fighting Methicillin-Resistant Staphylococcus aureus: Potent Inhibition of PBP 2a by Two Anti-MRSA β-Lactam Antibiotics

Mutant APH(2″)-IIa Enzymes with Increased Activity against Amikacin and Isepamicin

Revisiting the Nucleotide and Aminoglycoside Substrate Specificity of the Bifunctional Aminoglycoside Acetyltransferase(6′)-Ie/Aminoglycoside Phosphotransferase(2″)-Ia Enzyme

A surface loop modulates activity of the Bacillus class D β-lactamases

The crystal structures of CDD-1, the intrinsic class D β-lactamase from the pathogenic Gram-positive bacterium Clostridioides difficile, and its complex with cefotaxime

The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D β‐lactamases

Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside‐2′′‐phosphotransferases

Kinetic and Structural Requirements for Carbapenemase Activity in GES-Type β‑Lactamases

Mechanistic Basis for the Action of New Cephalosporin Antibiotics Effective against Methicillin- and Vancomycin-resistant Staphylococcus aureus

The Basis for Resistance to β-Lactam Antibiotics by Penicillin-binding Protein 2a of Methicillin-resistant Staphylococcus aureus

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