Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis - Test2 - elhamkhani - TriplyDB

Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis

Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis

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Carbapenems: past, present, and future Three decades of beta-lactamase inhibitors New agents for the treatment of drug-resistant Mycobacterium tuberculosis Carbapenems to Treat Multidrug and Extensively Drug-Resistant Tuberculosis: A Systematic Review Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections Antibiotic adjuvants: identification and clinical use Rising to the challenge: new therapies for tuberculosis Protein complexes and proteolytic activation of the cell wall hydrolase RipA regulate septal resolution in mycobacteria The 1.4 Å Crystal Structure of the Class D β-Lactamase OXA-1 Complexed with Doripenem The structures of the anti-tuberculosis antibiotics viomycin and capreomycin bound to the 70S ribosome Unusual Conformation of the SxN Motif in the Crystal Structure of Penicillin-Binding Protein A from Mycobacterium tuberculosis Biochemical and Structural Characterization of Mycobacterium tuberculosis β-Lactamase with the Carbapenems Ertapenem and Doripenem Structural and Biochemical Characterization of Mycobacterium tuberculosis CYP142: EVIDENCE FOR MULTIPLE CHOLESTEROL 27-HYDROXYLASE ACTIVITIES IN A HUMAN PATHOGEN Structures of the Michaelis Complex (1.2 Å) and the Covalent Acyl Intermediate (2.0 Å) of Cefamandole Bound in the Active Sites of the Mycobacterium tuberculosis β-Lactamase K73A and E166A Mutants,Structural basis for the inhibition ofMycobacterium tuberculosisL,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains Structure of LdtMt2, anL,D-transpeptidase fromMycobacterium tuberculosis Crystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosis The Role of the β5–α11 Loop in the Active-Site Dynamics of Acylated Penicillin-Binding Protein A from Mycobacterium tuberculosis NXL104 Irreversibly Inhibits the β-Lactamase from Mycobacterium tuberculosis Directed evolution of Mycobacterium tuberculosis β-lactamase reveals gatekeeper residue that regulates antibiotic resistance and catalytic efficiency Can Inhibitor-Resistant Substitutions in the Mycobacterium tuberculosis -Lactamase BlaC Lead to Clavulanate Resistance?: a Biochemical Rationale for the Use of -Lactam- -Lactamase Inhibitor Combinations Chemical and Structural Insights into the Regioversatility of the Aminoglycoside Acetyltransferase Eis Tebipenem, a New Carbapenem Antibiotic, Is a Slow Substrate That Inhibits the β-Lactamase from Mycobacterium tuberculosis Structures of free and inhibited forms of the L,D-transpeptidase LdtMt1 from Mycobacterium tuberculosis Potent Inhibitors of Acetyltransferase Eis Overcome Kanamycin Resistance in Mycobacterium tuberculosis Crystal structures of the transpeptidase domain of the Mycobacterium tuberculosis penicillin-binding protein PonA1 reveal potential mechanisms of antibiotic resistance TB drug development: immunology at the table Kinetic and Structural Characterization of the Interaction of 6-Methylidene Penem 2 with the β-Lactamase from Mycobacterium tuberculosis Class D β-lactamases: a reappraisal after five decades From multidrug- to extensively drug-resistant tuberculosis: upward trends as seen from a 15-year nationwide study Kinetic features of L,D-transpeptidase inactivation critical for β-lactam antibacterial activity Bibliometric analysis of worldwide publications on multi-, extensively, and totally drug - resistant tuberculosis (2006-2015)Repurposing clinically approved cephalosporins for tuberculosis therapy Binding and processing of β-lactam antibiotics by the transpeptidase LdtMt2 from Mycobacterium tuberculosis.Simple model for testing drugs against nonreplicating Mycobacterium tuberculosis Rapid cytolysis of Mycobacterium tuberculosis by faropenem, an orally bioavailable β-lactam antibiotic.What is next for small-molecule drug discovery?Importance of microbial natural products and the need to revitalize their discovery.New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in Mycobacteria Enhancing resistance to cephalosporins in class C beta-lactamases: impact of Gly214Glu in CMY-2.

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Meropenem-Clavulanate Is Effective Against Extensively Drug-Resistant Mycobacterium tuberculosis

http://www.wikidata.org/entity/Q27653976

description

2009 nî lūn-bûn

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2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2009 թվականի փետրվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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label

Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Meropenem-Clavulanate Is Effec ...... ant Mycobacterium tuberculosis

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Helena I Boshoff

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John S Blanchard

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Lee W Tremblay

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Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

Structure of the covalent adduct formed between Mycobacterium tuberculosis beta-lactamase and clavulanate

Activity of amoxicillin/clavulanate in patients with tuberculosis

Extensively drug-resistant tuberculosis as a cause of death in patients co-infected with tuberculosis and HIV in a rural area of South Africa

In vitro activity of amoxicillin in combination with clavulanic acid against Mycobacterium tuberculosis

An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence

Contribution of beta-lactamases to beta-lactam susceptibilities of susceptible and multidrug-resistant Mycobacterium tuberculosis clinical isolates

The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation

Crystal structure and activity studies of the Mycobacterium tuberculosis beta-lactamase reveal its critical role in resistance to beta-lactam antibiotics

How beta-lactamases have driven pharmaceutical drug discovery. From mechanistic knowledge to clinical circumvention.

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10.1126/SCIENCE.1167498

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Clifton E Barry

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24146168

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19251630

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Mycobacterium tuberculosis

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2679150

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