Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. - Wikidata - wikimedia - TriplyDB

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

http://www.wikidata.org/entity/Q35085145

about

Binding of thienamycin and clavulanic acid to the penicillin-binding proteins of Escherichia coli K-12 Genome degeneration and adaptation in a nascent stage of symbiosis Bacterial actin MreB assembles in complex with cell shape protein RodZ.Beta-lactamase inhibitors from laboratory to clinic Cefroxadine (CGP-9000), an orally active cephalosporin Evolution of penicillin-binding protein 2 concentration and cell shape during a long-term experiment with Escherichia coli Unstable Escherichia coli L forms revisited: growth requires peptidoglycan synthesis The bacterial actin-like cytoskeleton Self-resistance in Streptomyces, with Special Reference to β-Lactam Antibiotics Activities and regulation of peptidoglycan synthases Coarse-grained simulations of bacterial cell wall growth reveal that local coordination alone can be sufficient to maintain rod shape.Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution Crystal structure of the 47-kDa lipoprotein of Treponema pallidum reveals a novel penicillin-binding protein Dimeric structure of the cell shape protein MreC and its functional implications The Escherichia coli Cell Division Protein and Model Tat Substrate SufI (FtsP) Localizes to the Septal Ring and Has a Multicopper Oxidase-Like Structure The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain Morphological and ultrastructural changes in bacterial cells as an indicator of antibacterial mechanism of action Novel mechanism of beta-lactam resistance due to bypass of DD-transpeptidation in Enterococcus faecium Targeting of PBP1 by β-lactams determines recA/SOS response activation in heterogeneous MRSA clinical strains Interaction of penicillin-binding protein 2 with soluble lytic transglycosylase B1 in Pseudomonas aeruginosa Value addition in the efficacy of conventional antibiotics by Nisin against Salmonella Antibacterial compounds of Canadian honeys target bacterial cell wall inducing phenotype changes, growth inhibition and cell lysis that resemble action of β-lactam antibiotics The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus Separation of Escherichia coli penicillin-binding proteins into different membrane vesicles by agarose electrophoresis and sizing chromatography Rapid beta-lactam-induced lysis requires successful assembly of the cell division machinery.Distinct single-cell morphological dynamics under beta-lactam antibiotics.Identification and molecular analysis of PcsB, a protein required for cell wall separation of group B streptococcus Classic reaction kinetics can explain complex patterns of antibiotic action.Cloning and characterization of PBP 1C, a third member of the multimodular class A penicillin-binding proteins of Escherichia coli.Cytokinesis in bacteria Topology of penicillin-binding protein 1b of Escherichia coli and topography of four antigenic determinants studied by immunocolabeling electron microscopy.Isolation and characterization of the Escherichia coli msbB gene, a multicopy suppressor of null mutations in the high-temperature requirement gene htrB.The extracytoplasmic stress factor, sigmaE, is required to maintain cell envelope integrity in Escherichia coli.Isolation and characterization of the Escherichia coli htrB gene, whose product is essential for bacterial viability above 33 degrees C in rich media.The Escherichia coli lov gene product connects peptidoglycan synthesis, ribosomes and growth rate.Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene Bacterial growth and division: genes, structures, forces, and clocks.Metabolic alarms and cell division in Escherichia coli.Identification of the full set of Listeria monocytogenes penicillin-binding proteins and characterization of PBPD2 (Lmo2812).Characteristics and dynamics of bacterial populations during postantibiotic effect determined by flow cytometry.

P2860

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P2860

Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

http://www.wikidata.org/entity/Q35085145

description

1975 nî lūn-bûn

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1975 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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1975 թվականի օգոստոսին հրատարակված գիտական հոդված

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1975年の論文

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1975年論文

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1975年論文

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1975年論文

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1975年論文

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1975年論文

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1975年论文

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Distinct penicillin binding pr ...... shape of Escherichia coli K12.

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Proceedings of the National Academy of Sciences of the United States of America

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Spratt BG

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P2860

A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels

Penicillin-resistant temperature-sensitive mutants of Escherichia coli which synthesize hypo- or hyper-cross-linked peptidoglycan.

Mechanism of action and development of resistance to a new amidino penicillin.

Mechanism of action of penicillin.

6 -amidinopenicillanic acids--a new group of antibiotics.

A mutation which changes a membrane protein of E. coli.

Electron microscope study of septum formation in Escherichia coli strains B and B-r during synchronous growth.

Inhibition of an early event in the cell division cycle of Escherichia coli by FL1060, an amidinopenicillanic acid

Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate

How penicillin kills bacteria: progress and problems.

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2999-3003

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scholarly article

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10.1073/PNAS.72.8.2999

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8

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72

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1103132

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432906

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