Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis. - Wikidata - awgldk - TriplyDB

Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.

Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.

http://www.wikidata.org/entity/Q33803831

about

Structural insights into the dual strategy of recognition by peptidoglycan recognition protein, PGRP-S: structure of the ternary complex of PGRP-S with lipopolysaccharide and stearic acid Activities and regulation of peptidoglycan synthases Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex Inhibition of dd -Peptidases by a Specific Trifluoroketone: Crystal Structure of a Complex with the Actinomadura R39 dd -Peptidase Formation of the glycan chains in the synthesis of bacterial peptidoglycan Interaction energies between beta-lactam antibiotics and E. coli penicillin-binding protein 5 by reversible thermal denaturation Bacillus anthracis Peptidoglycan Integrity Is Disrupted by the Chemokine CXCL10 through the FtsE/X Complex.Identification and Characterization of Noncovalent Interactions That Drive Binding and Specificity in DD-Peptidases and β-Lactamases Difference between type I autoimmune inhibitors of fibrin stabilization in two patients with severe hemorrhagic disorder.Rapid beta-lactam-induced lysis requires successful assembly of the cell division machinery.Distinct single-cell morphological dynamics under beta-lactam antibiotics.Response of Cell Walls of Escherichia coli to a Sudden Reduction of the Environmental Osmotic Pressure.The chlamydia: molecular biology of procaryotic obligate parasites of eucaryocytes.Antibiotics of the virginiamycin family, inhibitors which contain synergistic components.Derepression of beta-lactamase (penicillinase in Bacillus cereus by peptidoglycans.Differential recovery of auxotrophs after penicillin enrichment in Escherichia coli Beta-lactam antibiotics: from antibiosis to resistance and bacteriology How antibiotics kill bacteria: from targets to networks On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins.Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates.Cycloserine Induction, Propagation, and Antimicrobial Susceptibility of Wall-Defective Staphylococcus aureus Antagonism of the antibacterial action of some penicillins by other penicillins and cephalosporins Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.Teichoic acid hydrolase activity in soil bacteria (Bacillus subtilis-sporulation-phosphodiesterase-polyamines-concanavalin A).Temperature effects on minimum inhibitory and bactericidal concentrations of cell wall antibiotics in Streptococcus faecalis Altered penicillin-binding components in penicillin-resistant mutants of Bacillus subtilis Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity.Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro Peptidoglycan of Myxococcus xanthus: structure and relation to morphogenesis.Reactivation of peptidoglycan synthesis in ether-permeabilized Escherichia coli after inhibition by beta-lactam antibiotics.A DNA damage-induced, SOS-independent checkpoint regulates cell division in Caulobacter crescentus.A Simple Method for the Efficient Isolation of Genomic DNA from Lactobacilli Isolated from Traditional Indian Fermented Milk (dahi)Peptidoglycan structure of Lactobacillus casei, a species highly resistant to glycopeptide antibiotics.DD-carboxypeptidase-transpeptidase and killing site of beta-lactam antibiotics in Streptomyces strains R39, R61, and K11.Exocellular beta-lactamases of Streptomyces albus G and strains R39 and K11 Regulation of the bacterial cell wall: effect of antibiotics on lipid biosynthesis.Altered penicillin-binding proteins in methicillin-resistant strains of Staphylococcus aureus.Penicillin-binding proteins in Clostridium perfringens Studying antibiotic-membrane interactions via X-ray diffraction and fluorescence microscopy The chimeric genome of Sphaerochaeta: nonspiral spirochetes that break with the prevalent dogma in spirochete biology.

P2860

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P2860

Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis.

http://www.wikidata.org/entity/Q33803831

description

1965 nî lūn-bûn

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1965 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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1965 թվականի հուլիսին հրատարակված գիտական հոդված

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1965年の論文

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1965年論文

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1965年論文

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1965年論文

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1965年論文

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1965年論文

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1965年论文

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

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Penicillin: its basic site of ...... ll wall mucopeptide synthesis.

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P2093

Park JT

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Wise EM Jr

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P2860

BIOSYNTHESIS OF CELL WALL MUCOPEPTIDE BY A PARTICULATE FRACTION FROM STAPHYLOCOCCUS AUREUS

BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS.

LIPID-PHOSPHOACETYLMURAMYL-PENTAPEPTIDE AND LIPID-PHOSPHODISACCHARIDE-PENTAPEPTIDE: PRESUMED MEMBRANE TRANSPORT INTERMEDIATES IN CELL WALL SYNTHESIS

Some differences in the action of penicillin, bacitracin, and vancomycin on Bacillus megaterium.

Inhibition by antibiotics of the growth of bacterial and yeast protoplasts

BACTERIAL PROTOPLASTS INDUCED BY PENICILLIN.

Inhibition of the biosynthesis of cell-wall mucopeptides by the penicillins. A study of penicillin-sensitive and penicillin-resistant strains of Staphylococcus aureus.

The incorporation of amino acids into the cell-wall mucopeptide of staphylococci and the effect of antibiotics on the process

STRUCTURE OF THE CELL WALL OF STAPHYLOCOCCUS AUREUS, STRAIN COPENHAGEN. I. PREPARATION OF FRAGMENTS BY ENZYMATIC HYDROLYSIS.

Autolytic enzymes as a source of error in the preparation and study of gram-negative cell walls.

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75-81

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scholarly article

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10.1073/PNAS.54.1.75

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1

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54

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5216369

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285799

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