One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams - Test2 - elhamkhani - TriplyDB

One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams

One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams

http://www.wikidata.org/entity/Q38712471

about

Self-resistance in Streptomyces, with Special Reference to β-Lactam Antibiotics Structure and Mechanism of Staphylococcus aureus TarS, the Wall Teichoic Acid β-glycosyltransferase Involved in Methicillin Resistance A High-Throughput Approach To Identify Compounds That Impair Envelope Integrity in Escherichia coli Identification and Characterization of the Sulfazecin Monobactam Biosynthetic Gene Cluster.Virulence and transcriptome profile of multidrug-resistant Escherichia coli from chicken.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Synthesis and biological evaluation of the progenitor of a new class of cephalosporin analogues, with a particular focus on structure-based computational analysis.Antibacterial and β-Lactamase Inhibitory Activity of Monocyclic β-Lactams.Pharmacokinetics of β-Lactam Antibiotics: Clues from the Past To Help Discover Long-Acting Oral Drugs in the Future Tackling the Antibiotic Resistance Caused by Class A -Lactamases through the Use of -Lactamase Inhibitory Protein A Natural Deep Eutectic Solvent Formulated to Stabilize β-Lactam Antibiotics

P2860

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P2860

One ring to rule them all: Current trends in combating bacterial resistance to the β-lactams

http://www.wikidata.org/entity/Q38712471

description

2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

One ring to rule them all: Cur ...... al resistance to the β-lactams

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One ring to rule them all: Cur ...... al resistance to the β-lactams

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One ring to rule them all: Cur ...... al resistance to the β-lactams

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Protein Science

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One ring to rule them all: Cur ...... al resistance to the β-lactams

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Dustin T King

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Natalie C J Strynadka

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P2860

Altered antibiotic transport in OmpC mutants isolated from a series of clinical strains of multi-drug resistant E. coli

Kinetics of avibactam inhibition against Class A, C, and D β-lactamases

Enterobactin: an archetype for microbial iron transport

RND-type drug eﬄux pumps from Gram-negative bacteria: molecular mechanism and inhibition

Who will develop new antibacterial agents?

Bacterial multidrug efflux pumps: mechanisms, physiology and pharmacological exploitations

Critical involvement of a carbamylated lysine in catalytic function of class D -lactamases

Crystal structure of bacterial multidrug efflux transporter AcrB

Structural basis for the beta lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus

The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strains

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787-803

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scholarly article

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10.1002/PRO.2889

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4

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25

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Solmaz Sobhanifar

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2016-01-27T00:00:00Z

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26813250

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4941212

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