相关参考文献
注意：仅列出部分参考文献，下载原文获取全部文献信息。Suppression of β-Lactam Resistance by Aspergillomarasmine A Is Influenced by both the Metallo-β-Lactamase Target and the Antibiotic Partner
Caitlyn M. Rotondo et al.
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY (2020)
Identification of the AMA Synthase from the Aspergillomarasmine A Biosynthesis and Evaluation of Its Biocatalytic Potential
Qianqian Guo et al.
ACS CATALYSIS (2020)
Iron and Chelation in Biochemistry and Medicine: New Approaches to Controlling Iron Metabolism and Treating Related Diseases
George J. Kontoghiorghes et al.
CELLS (2020)
NDM Metallo-β-Lactamases and Their Bacterial Producers in Health Care Settings
Wenjing Wu et al.
CLINICAL MICROBIOLOGY REVIEWS (2019)
Probing the Interaction of Aspergillomarasmine A with Metallo-beta-lactamases NDM-1, VIM-2, and IMP-7
Alexander Bergstrom et al.
ACS INFECTIOUS DISEASES (2018)
Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activity
Zishuo Cheng et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2018)
The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters
Lin-Cheng Ju et al.
TRENDS IN PHARMACOLOGICAL SCIENCES (2018)
Chemoenzymatic asymmetric synthesis of the metallo-β-lactamase inhibitor aspergillomarasmine A and related aminocarboxylic acids
Haigen Fu et al.
NATURE CATALYSIS (2018)
Total Syntheses of Natural Metallophores Staphylopine and Aspergillomarasmine A
Jian Zhang et al.
JOURNAL OF ORGANIC CHEMISTRY (2017)
A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases
Maria-Natalia Lisa et al.
NATURE COMMUNICATIONS (2017)
Inhibitors of metallo-β-lactamases
Caitlyn M. Rotondo et al.
CURRENT OPINION IN MICROBIOLOGY (2017)
Total Synthesis of Aspergillomarasmine A and Related Compounds: A Sulfamidate Approach Enables Exploration of Structure-Activity Relationships
Silvia A. Albu et al.
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2016)
B1-Metallo-beta-Lactamases: Where Do We Stand?
Maria F. Mojica et al.
CURRENT DRUG TARGETS (2016)
Revised stability constant, spectroscopic properties and binding mode of Zn(II) to FluoZin-3, the most common zinc probe in life sciences
I. Marszalek et al.
JOURNAL OF INORGANIC BIOCHEMISTRY (2016)
Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase
Lisandro J. Gonzalez et al.
NATURE CHEMICAL BIOLOGY (2016)
Bayesian Deconvolution of Mass and Ion Mobility Spectra: From Binary Interactions to Polydisperse Ensembles
Michael T. Marty et al.
ANALYTICAL CHEMISTRY (2015)
Overcoming differences: The catalytic mechanism of metallo-β-lactamases
Maria-Rocio Meini et al.
FEBS LETTERS (2015)
Molar absorption coefficients and stability constants of metal complexes of 4-(2-pyridylazo)resorcinol (PAR): Revisiting common chelating probe for the study of metalloproteins
Anna Kocyla et al.
JOURNAL OF INORGANIC BIOCHEMISTRY (2015)
Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-β-lactamase VIM-2
Mahesh Aitha et al.
BIOCHEMISTRY (2014)
Aspergillomarasmine A overcomes metallo-β-lactamase antibiotic resistance
Andrew M. King et al.
NATURE (2014)
Metallo-beta-lactamase structure and function
Timothy Palzkill
ANTIMICROBIAL THERAPEUTICS REVIEWS: THE BACTERIAL CELL WALL AS AN ANTIMICROBIAL TARGET (2013)
On the binding affinity of macromolecular interactions: daring to ask why proteins interact
Panagiotis L. Kastritis et al.
JOURNAL OF THE ROYAL SOCIETY INTERFACE (2013)
Stormy waters ahead: global emergence of carbapenemases
Gopi Patel et al.
FRONTIERS IN MICROBIOLOGY (2013)
New Delhi Metallo-β-Lactamase: Structural Insights into β-Lactam Recognition and Inhibition
Dustin T. King et al.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2012)
Structural and Kinetic Studies on Metallo-β-lactamase IMP-1
Dionne H. Griffin et al.
BIOCHEMISTRY (2011)
A Demetallation Method for IMP-1 Metallo-β-Lactamase with Restored Enzymatic Activity Upon Addition of Metal Ion(s)
Yoshihiro Yamaguchi et al.
CHEMBIOCHEM (2011)
Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistance
Dustin King et al.
PROTEIN SCIENCE (2011)
Positively Cooperative Binding of Zinc Ions to Bacillus cereus 569/H/9 β-Lactamase II Suggests that the Binuclear Enzyme Is the Only Relevant Form for Catalysis
Olivier Jacquin et al.
JOURNAL OF MOLECULAR BIOLOGY (2009)
Crystal structure of Pseudomonas aeruginosa SPM-1 provides insights into variable zinc affinity of metallo-β-lactamases
TA Murphy et al.
JOURNAL OF MOLECULAR BIOLOGY (2006)
Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-β-lactamase
RM Rasia et al.
BIOCHEMISTRY (2002)
分享论文
