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FEMS Microbiology Letters, ISSN 0378-1097, 2018, Volume 365, Issue 17
The 16S-23S rDNA internal transcribed spacer (ITS) sequence, located in the rrn operon, has been analyzed and evaluated for use in phylogenetic analysis and... 
Vibrio parahaemolyticus | Mosaic-like structure | RNA | 16S-23S rDNA internal transcribed spacer sequence | The secondary structure | the secondary structure | STRAINS | SEQUENCES | mosaic-like structure | RIBOSOMAL-RNA OPERON | REGIONS | MICROBIOLOGY | INTERGENIC SPACERS | IDENTIFICATION
Journal Article
Phycologia, ISSN 0031-8884, 07/2013, Volume 52, Issue 4, pp. 333 - 337
Comte K., Coursin T. and Carre-Mlouka A. 2013. A new genotype in the genus Arthrospira (Oscillatoriales, Cyanobacteria) revealed by a mosaic-like structure of... 
ITS rRNA | Arthrospira | New genotype | Mosaic-like structure | Its rrna | SEQUENCES | MARINE & FRESHWATER BIOLOGY | INTERNALLY TRANSCRIBED SPACER | 4 CONTINENTS | PLANT SCIENCES | Trees | Phylogenetics | Genotype & phenotype | Software | Microbiology | Genes
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2012, Volume 7, Issue 9, p. e44918
The increasing prevalence of N. gonorrhoeae strains exhibiting decreased susceptibility to third-generation cephalosporins and the recent isolation of two... 
REDUCED SUSCEPTIBILITY | DECREASED SUSCEPTIBILITY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | MIMETIC BETA-LACTAMS | ANTIBIOTIC-RESISTANCE | SPECTRUM CEPHALOSPORINS | TRANSITION-STATE | MOSAIC-LIKE STRUCTURE | LEVEL RESISTANCE | Small Molecule Libraries - pharmacology | Bacterial Proteins - chemistry | Dose-Response Relationship, Drug | Microbial Sensitivity Tests | Penicillin-Binding Proteins - chemistry | Boron Compounds - analysis | Anti-Bacterial Agents - chemistry | Penicillins - analysis | Penicillin-Binding Proteins - antagonists & inhibitors | Penicillins - pharmacology | Cephalosporins - pharmacology | Recombinant Proteins - metabolism | Bacterial Proteins - antagonists & inhibitors | Boron Compounds - pharmacology | Catalytic Domain | Recombinant Proteins - antagonists & inhibitors | Neisseria gonorrhoeae - drug effects | Recombinant Proteins - chemistry | Penicillin-Binding Proteins - metabolism | Neisseria gonorrhoeae - growth & development | Small Molecule Libraries - chemistry | High-Throughput Screening Assays | Protein Binding | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Molecular Docking Simulation | Fluorescence Polarization | Neisseria gonorrhoeae - metabolism | beta-Lactam Resistance - drug effects | Physiological aspects | Drug resistance in microorganisms | Genetic aspects | Neisseria gonorrhoeae | Research | Binding proteins | Antimicrobial activity | Molecular structure | Laboratories | Serine | Fluorescence | High-throughput screening | Amides | Biochemistry | Ceftriaxone | Assaying | Antiinfectives and antibacterials | Optimization | Molecular docking | Streptococcus infections | Proteins | Sexually transmitted diseases | Cell growth | Immunology | Cephalosporins | Penicillin | Bacteria | Inhibition | Cefixime | Crystal structure | Enzymes | Fluorescence polarization | Penicillin-binding protein | Bacterial infections | β-Lactam antibiotics | Gonorrhea | Lead compounds | Penicillin-binding protein 2 | Cephalosporin | Screening | Inhibitors | Antibiotics | Mutation | Molecular biology | STD
Journal Article
Journal Article
Journal Article
Sexually Transmitted Diseases, ISSN 0148-5717, 02/2018, Volume 45, Issue 2, pp. 92 - 95
ABSTRACTReal-time polymerase chain reaction (PCR) assays to detect antimicrobial resistance–associated mutations were tested on Neisseria gonorrhoeae–positive... 
INFECTIOUS DISEASES | REDUCED SUSCEPTIBILITY | AZITHROMYCIN RESISTANCE | CEFIXIME | CANADA | CEFTRIAXONE | PENICILLIN-BINDING PROTEIN-2 | ANTIBIOTIC-RESISTANCE | MUTATIONS | MOSAIC-LIKE STRUCTURE | MOLECULAR ASSAY
Journal Article
PLoS Medicine, ISSN 1549-1277, 07/2017, Volume 14, Issue 7, p. e1002366
Journal Article
Journal Article