Metallo-β-lactamase structure and function (original) (raw)

Structure, function, and evolution of metallo-β-lactamases from the B3 subgroup—emerging targets to combat antibiotic resistance

Gerhard Schenk

Frontiers in Chemistry

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Metallo-β-Lactamases: A Major Threat to Human Health

Gerhard Schenk

American Journal of Molecular Biology, 2014

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Zinc and antibiotic resistance: metallo-β-lactamases and their synthetic analogues

Govindasamy Mugesh

Journal of Biological Inorganic Chemistry, 2008

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Overcoming differences: The catalytic mechanism of metallo-β-lactamases

María Rocío Meini

FEBS letters, 2015

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Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme

Carine Bebrone

FEBS Journal, 2011

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Metallo-β-lactamases: a last frontier for β-lactams?

Gian Rossolini

The Lancet Infectious Diseases, 2011

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Metallo- -Lactamases: the Quiet before the Storm?

Laurent Poirel

Clinical Microbiology Reviews, 2005

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Diversity and proliferation of metallo-β-lactamases: a clarion call for clinically effective metallo-β-lactamase inhibitors

John Osei

Applied and Environmental Microbiology, 2018

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Engineered Mononuclear Variants in Bacillus cereus Metallo-β-lactamase BcII Are Inactive

Lisandro Gonzalez

Biochemistry, 2008

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Unusual metallo-β-lactamases may constitute a new subgroup in this family of enzymes

Chun-Feng David Hou

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Metallo‐β‐Lactamases: A Class Apart

Karen Bush

Clinical Infectious Diseases, 1998

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Biochemical characterization of the metallo-beta-lactamase CcrA from Bacteroides fragilis TAL3636

Karen Bush

Antimicrobial Agents and Chemotherapy, 1992

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β-Lactamases: A Focus on Current Challenges

Robert Bonomo

Cold Spring Harbor Perspectives in Medicine, 2016

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Unusual metallo-<i>β</i>-lactamases may constitute a new subgroup in this family of enzymes

Gerhard Schenk

American Journal of Molecular Biology, 2014

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Kinetic Properties and Metal Content of the Metallo-β-lactamase CcrA Harboring Selective Amino Acid Substitutions

Norman Canfield

Journal of Biological Chemistry, 1999

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A Metallo-β-lactamase Enzyme in Action: Crystal Structures of the Monozinc Carbapenemase CphA and its Complex with Biapenem

Carine Bebrone

Journal of Molecular Biology, 2005

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Approaches to the simultaneous inactivation of metallo- and serine-β-lactamases

sudhakar ganta

Bioorganic & Medicinal Chemistry Letters, 2009

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Past and Present Perspectives on β-Lactamases

Karen Bush

Antimicrobial Agents and Chemotherapy, 2018

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Evaluation of 1, 4, 7-Triazacyclononane (TACN) as a potential Metallo-B-Lactamase inhibitor in Enterobacteriaceae: Restoring the Activity of B-lactams

DANIEL GYAMFI AMOAKO

bioRxiv (Cold Spring Harbor Laboratory), 2018

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An Update on the Status of Potent Inhibitors of Metallo-β-Lactamases.

Nazar Ul Islam

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Functional Analysis of the Active Site of a Metallo-β-Lactamase Proliferating in Japan

Shin Haruta

Antimicrobial Agents and Chemotherapy, 2000

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On functional and structural heterogeneity of VIM-type metallo-beta-lactamases

Jean-marie Frère

Journal of Antimicrobial Chemotherapy, 2003

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A novel metallo-β-lactamase, Mbl1b, produced by the environmental bacterium Caulobacter crescentus

Alan Simm

FEBS Letters, 2001

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The Development of New Small-Molecule Inhibitors Targeting Bacterial Metallo-β-lactamases

Cong Liu

Current topics in medicinal chemistry, 2018

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Probing the Specificity of the Subclass B3 FEZ-1 Metallo-β-lactamase by Site-directed Mutagenesis

bart devreese

Journal of Biological Chemistry, 2004

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Dramatic Broadening of the Substrate Profile of the Aeromonas hydrophila CphA Metallo-β-lactamase by Site-directed Mutagenesis

bart devreese

Journal of Biological Chemistry, 2005

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Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro Evolution

María Rocío Meini

Antibiotics, 2014

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High specificity of cphA-encoded metallo-beta-lactamase from Aeromonas hydrophila AE036 for carbapenems and its contribution to beta-lactam resistance

Orietta Massidda

Antimicrobial Agents and Chemotherapy, 1993

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Metallo-β-lactamases and a tug-of-war for the available zinc at the host–pathogen interface

Lisandro González

Current Opinion in Chemical Biology, 2022

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The identification of new metallo-β-lactamase inhibitor leads from fragment-based screening

Gerhard Schenk

Bioorganic & Medicinal Chemistry Letters, 2011

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TACN (1, 4, 7-Triazacyclononane) restores the activity of β-lactam antibiotics against Metallo-β-Lactamase producing Enterobacteriaceae: The exploration of potential Metallo-β-Lactamase inhibitors

DANIEL GYAMFI AMOAKO

Applied and Environmental Microbiology, 2018

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Dramatic Broadening of the Substrate Profile of the Aeromonas hydrophila CphA Metallo -lactamase by Site-directed Mutagenesis

Carine Bebrone

Journal of Biological Chemistry, 2005

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