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Cell, ISSN 0092-8674, 04/2017, Volume 169, Issue 3, pp. 442 - 456.e18
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2010, Volume 107, Issue 40, pp. 17152 - 17157
Differences between the structures of bacterial, archaeal, and eukaryotic ribosomes account for the selective action of antibiotics. Even minor variations in... 
Ketolides | Antibiotics | Macrolides | Drug interactions | Ribosomes | Bacteria | Nucleotides | Electron density | Genetic mutation | Binding sites | Ribosome structure | Chloramphenicol | Telithromycin | Erythromycin | Clindamycin | BACTERIAL RIBOSOME | RNA GENE | MULTIDISCIPLINARY SCIENCES | telithromycin | RESISTANCE MUTATIONS | CONFERRING RESISTANCE | 23S | erythromycin | DOMAIN-II | BINDING-SITE | chloramphenicol | ARCHAEON HALOBACTERIUM-HALOBIUM | MACROLIDE ANTIBIOTICS | ribosome structure | clindamycin | SUBUNIT | Haloarcula marismortui - genetics | Haloarcula marismortui - metabolism | Chloramphenicol - chemistry | Erythromycin - metabolism | Molecular Sequence Data | Ribosomes - metabolism | Deinococcus - metabolism | Deinococcus - genetics | Haloarcula marismortui - chemistry | X-Ray Diffraction | Anti-Bacterial Agents - chemistry | Base Sequence | Escherichia coli - metabolism | Ketolides - metabolism | Deinococcus - chemistry | Molecular Structure | Clindamycin - chemistry | Peptidyl Transferases - metabolism | Clindamycin - metabolism | Peptidyl Transferases - chemistry | Ribosomes - chemistry | Anti-Bacterial Agents - metabolism | Escherichia coli - chemistry | RNA, Ribosomal, 23S - chemistry | Erythromycin - chemistry | Escherichia coli - genetics | Ketolides - chemistry | RNA, Ribosomal, 23S - metabolism | Chloramphenicol - metabolism | Escherichia coli | Crystals | Genetic aspects | Research | Properties | Structure | Observations | Peptidyl transferases | Eukaryotes | E coli | Peptides | Ribonucleic acid--RNA | Bacteriology | Index Medicus | Drugs | lincosamides | Pathogens | rRNA | rRNA 23S | Data processing | Ribosomal subunits | Ionizing radiation | Peptidyltransferase | Crystal structure | Tunnels | Biological Sciences
Journal Article
Science, ISSN 0036-8075, 11/2012, Volume 338, Issue 6111, pp. 1214 - 1217
Millions of molecules of lipopolysaccharide (LPS) must be assembled on the Escherichia coli cell surface each time the cell divides. The biogenesis of LPS... 
Proteins | Hydrolysis | ATP binding cassette transporters | Molecules | REPORTS | Periplasm | Biochemistry | Binding sites | P branes | Lipopolysaccharides | Adducts | OUTER-MEMBRANE | GENETIC-CODE | MECHANISM | CELL-ENVELOPE | MULTIDISCIPLINARY SCIENCES | INNER-MEMBRANE | FUNCTIONAL-ANALYSIS | SURFACE | EXPORT | IDENTIFICATION | PROTEIN COMPLEX | Membrane Proteins - genetics | Bacterial Proteins - chemistry | Lipopolysaccharides - metabolism | Cytoplasm - metabolism | Escherichia coli Proteins - metabolism | Carrier Proteins - genetics | ATP-Binding Cassette Transporters - chemistry | Carrier Proteins - metabolism | Biological Transport | Membrane Proteins - chemistry | Periplasm - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | ATP-Binding Cassette Transporters - metabolism | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Carrier Proteins - chemistry | Protein Conformation | Membrane Proteins - metabolism | Mutation | Escherichia coli Proteins - chemistry | Escherichia coli | Biological transport | Physiological aspects | Bacterial cell walls | Research | Natural history | Adenosine triphosphate | Lipids | Biosynthesis | Gram-negative bacteria | E coli | Cytoplasm | Adenosine triphosphatase | Index Medicus | International trade | Membranes | Bacteria | Transport | Transit | Exports
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 04/2014, Volume 9, Issue 4, pp. e94816 - e94816
The emerging view of N-epsilon-lysine acetylation in eukaryotes is of a relatively abundant post-translational modification (PTM) that has a major impact on... 
GCN5-RELATED N-ACETYLTRANSFERASES | SELF-ASSEMBLED MONOLAYERS | BACILLUS-SUBTILIS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | CRYSTAL-STRUCTURES | GCN5 TRANSCRIPTIONAL COACTIVATOR | HISTONE ACETYLTRANSFERASE | LYSINE ACETYLATION | CATALYTIC MECHANISM | MASS-SPECTROMETRY | Organophosphates - metabolism | Amino Acid Sequence | Escherichia coli - enzymology | Escherichia coli - drug effects | Molecular Sequence Data | Crystallography, X-Ray | Escherichia coli Proteins - metabolism | Mutant Proteins - metabolism | Glucose - pharmacology | Blotting, Western | Acetylation - drug effects | Mass Spectrometry | Staining and Labeling | Escherichia coli - metabolism | Lysine - metabolism | Kinetics | Proteomics - methods | Escherichia coli Proteins - chemistry | Binding Sites | Post-translational modification | Physiological aspects | Research | Bacterial proteins | Phosphates | Health sciences | Transcription | Structural stability | Genomics | Escherichia coli | Kinases | Crystallography | Triose-phosphate isomerase | DNA-directed RNA polymerase | Proteins | Eukaryotes | Immunology | E coli | Post-translation | Aging | Acetyl phosphate | Bacteria | Coenzyme A | Acetylation | Biomedical engineering | Enzymes | Mass spectroscopy | Pharmacology | RNA polymerase | Metabolism | Mutants | Medicine | Polymerase | Chemistry | Infectious diseases | Ribonucleic acids | Lysine | Glyceraldehyde-3-phosphate dehydrogenase | Scientific imaging | Molecular biology | Mass spectrometry | Binding sites | Structural analysis | Structure-function relationships | Index Medicus
Journal Article
Journal Article
Nature, ISSN 0028-0836, 05/2016, Volume 534, Issue 7606, pp. 277 - 280
In order to survive, bacteria continually sense, and respond to, environmental fluctuations. Stringent control represents a key bacterial stress response to... 
EF-TU | ELECTRON CRYOMICROSCOPY | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | CRYO-EM | TRANSFER-RNA | RIBONUCLEIC ACID SYNTHESIS | PROTEIN-SYNTHESIS | RELA | GUANOSINE TETRAPHOSPHATE | Guanosine Tetraphosphate - chemistry | Phosphorylation | Protein Biosynthesis | RNA, Transfer, Amino Acyl - chemistry | Stress, Physiological | Ribosomes - metabolism | Escherichia coli Proteins - ultrastructure | RNA, Transfer - ultrastructure | Guanosine Tetraphosphate - metabolism | Escherichia coli - pathogenicity | Escherichia coli - metabolism | RNA, Transfer, Amino Acyl - metabolism | GTP Pyrophosphokinase - metabolism | RNA, Transfer - genetics | Escherichia coli Proteins - antagonists & inhibitors | GTP Pyrophosphokinase - ultrastructure | RNA, Transfer - chemistry | Binding Sites | Second Messenger Systems | Protein Structure, Tertiary | GTP Pyrophosphokinase - antagonists & inhibitors | RNA, Transfer - metabolism | Ribosomes - chemistry | Models, Molecular | Escherichia coli Proteins - metabolism | RNA, Transfer, Amino Acyl - genetics | Amino Acids - deficiency | Cryoelectron Microscopy | Ribosomes - ultrastructure | Metabolic Networks and Pathways | Escherichia coli - genetics | Adenosine - metabolism | GTP Pyrophosphokinase - genetics | Protein Conformation | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Escherichia coli - ultrastructure | Microbiological research | Transcription factors | Escherichia coli | Ribosomes | Research | Virulence (Microbiology) | Transfer RNA | E coli | Antibiotics | Ribonucleic acid--RNA | Crystal structure | Index Medicus
Journal Article