Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae. - Test2 - elhamkhani - TriplyDB

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

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Resistance to antibiotics targeted to the bacterial cell wall Core Steps of Membrane-Bound Peptidoglycan Biosynthesis: Recent Advances, Insight and Opportunities Structure of the pneumococcal l,d-carboxypeptidase DacB and pathophysiological effects of disabled cell wall hydrolases DacA and DacB Addiction of Hypertransformable Pneumococcal Isolates to Natural Transformation for In Vivo Fitness and Virulence Highly Variable Streptococcus oralis Strains Are Common among Viridans Streptococci Isolated from Primates Biological and Epidemiological Features of Antibiotic-Resistant Streptococcus pneumoniae in Pre- and Post-Conjugate Vaccine Eras: a United States Perspective.Insight into the Diversity of Penicillin-Binding Protein 2x Alleles and Mutations in Viridans Streptococci.Deciphering the distance to antibiotic resistance for the pneumococcus using genome sequencing data A low-affinity penicillin-binding protein 2x variant is required for heteroresistance in Streptococcus pneumoniae.Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica.Mechanisms of genome evolution of Streptococcus.Profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39 Commensal streptococci serve as a reservoir for β-lactam resistance genes in Streptococcus pneumoniae.Evolving resistance among Gram-positive pathogens A Novel Metallo-β-Lactamase Involved in the Ampicillin Resistance of Streptococcus pneumoniae ATCC 49136 Strain.Penicillin-Binding Protein Transpeptidase Signatures for Tracking and Predicting β-Lactam Resistance Levels in Streptococcus pneumoniae.SpyB, a Small Heme-Binding Protein, Affects the Composition of the Cell Wall in Streptococcus pyogenes.Complete Genome Sequence of Streptococcus pneumoniae Strain A026, a Clinical Multidrug-Resistant Isolate Carrying Tn2010.Streptococcus pneumoniae PBP2x mid-cell localization requires the C-terminal PASTA domains and is essential for cell shape maintenance.Metallo-β-lactamase structure and function.β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.Pneumococcal lipoproteins involved in bacterial fitness, virulence, and immune evasion.Comprehensive identification of single nucleotide polymorphisms associated with beta-lactam resistance within pneumococcal mosaic genes.Environmental and genetic modulation of the phenotypic expression of antibiotic resistance.Antimicrobial resistance, penicillin-binding protein sequences, and pilus islet carriage in relation to clonal evolution of Streptococcus pneumoniae serotype 19A in Russia, 2002-2013.Penicillin-binding protein 2x of Streptococcus pneumoniae: the mutation Ala707Asp within the C-terminal PASTA2 domain leads to destabilization.Description and characterization of a penicillin-resistant Streptococcus dysgalactiae subsp. equisimilis clone isolated from blood in three epidemiologically linked patients.Transfer of penicillin resistance from Streptococcus oralis to Streptococcus pneumoniae identifies murE as resistance determinant.New Aspects of the Interplay between Penicillin Binding Proteins, murM, and the Two-Component System CiaRH of Penicillin-Resistant Streptococcus pneumoniae Serotype 19A Isolates from Hungary Promoter Identification and Transcription Analysis of Penicillin-Binding Protein Genes in Streptococcus pneumoniae R6 Validation of β-lactam minimum inhibitory concentration predictions for pneumococcal isolates with newly encountered penicillin binding protein (PBP) sequences Suppression of a deletion mutation in the gene encoding essential PBP2b reveals a new lytic transglycosylase involved in peripheral peptidoglycan synthesis in Streptococcus pneumoniae D39.Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox.Pbp2x localizes separately from Pbp2b and other peptidoglycan synthesis proteins during later stages of cell division of Streptococcus pneumoniae D39 Effects of low PBP2b levels on cell morphology and peptidoglycan composition in Streptococcus pneumoniae R6.Discovery of β-lactam-resistant variants in diverse pneumococcal populations.Diversity of Mosaic pbp2x Families in Penicillin-Resistant Streptococcus pneumoniae from Iran and Romania.A visual review of the human pathogen Streptococcus pneumoniae.Novel Electrophilic Scaffold for Imaging of Essential Penicillin-Binding Proteins in Streptococcus pneumoniae.Absence of the KhpA and KhpB (JAG/EloR) RNA-binding proteins suppresses the requirement for PBP2b by overproduction of FtsA in Streptococcus pneumoniae D39.

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P2860

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

http://www.wikidata.org/entity/Q37990942

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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artigo científico

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artikel ilmiah

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name

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

@en

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

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type

label

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

@en

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

@nl

prefLabel

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

@en

Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

@nl

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Future Microbiology

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Molecular mechanisms of β-lactam resistance in Streptococcus pneumoniae.

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Dalia Denapaite

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Patrick Maurer

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Regine Hakenbeck

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Reinhold Brückner

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P2860

Multilocus sequence typing: a portable approach to the identification of clones within populations of pathogenic microorganisms

The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance

Crystal structure of PBP2x from a highly penicillin-resistant Streptococcus pneumoniae clinical isolate: a mosaic framework containing 83 mutations

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

A PBP2x from a clinical isolate of Streptococcus pneumoniae exhibits an alternative mechanism for reduction of susceptibility to beta-lactam antibiotics

Structural and mechanistic basis of penicillin-binding protein inhibition by lactivicins

Common alterations in PBP1a from resistant Streptococcus pneumoniae decrease its reactivity toward beta-lactams: structural insights

PBP active site flexibility as the key mechanism for beta-lactam resistance in pneumococci

X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme

Penicillin-binding proteins and beta-lactam resistance

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395-410

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scholarly article

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10.2217/FMB.12.2

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3

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7

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2012-03-01T00:00:00Z

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22393892

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