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1. Full Text Binding interface between the Salmonella σ(S)/RpoS subunit of RNA polymerase and Crl: hints from bacterial species lacking crl
by Cavaliere, Paola and Sizun, Christina and Levi-Acobas, Fabienne and Nowakowski, Mireille and Monteil, Véronique and Bontems, François and Bellalou, Jacques and Mayer, Claudine and Norel, Françoise
Scientific reports, ISSN 2045-2322, 09/2015, Volume 5, pp. 13564 - 13564
Amino Acid Sequence | DNA-Directed RNA Polymerases - ultrastructure | Protein Subunits | Sigma Factor - chemistry | Sigma Factor - metabolism | Models, Chemical | Species Specificity | Bacterial Proteins - chemistry | Molecular Sequence Data | Structure-Activity Relationship | Pseudomonas aeruginosa - metabolism | Protein Binding | Bacterial Proteins - metabolism | Protein Conformation | Bacterial Proteins - ultrastructure | DNA-Directed RNA Polymerases - chemistry | Molecular Docking Simulation | DNA-Directed RNA Polymerases - metabolism | Binding Sites | Salmonella - metabolism | Amino Acid Substitution | Sigma Factor - ultrastructure | Index Medicus | Life Sciences | Sigma Factor/metabolism | DNA-Directed RNA Polymerases/metabolism | Bacterial Proteins/chemistry | Biochemistry, Molecular Biology | Salmonella/metabolism | Microbiology and Parasitology | Bacterial Proteins/metabolism | Sigma Factor/chemistry | Bacterial Proteins/ultrastructure | Sigma Factor/ultrastructure | DNA-Directed RNA Polymerases/chemistry | DNA-Directed RNA Polymerases/ultrastructure | Pseudomonas aeruginosa/metabolism
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2. Full Text Tripartite assembly of RND multidrug efflux pumps
by Daury, Laetitia and Orange, François and Taveau, Jean-Christophe and Verchère, Alice and Monlezun, Laura and Gounou, Céline and Marreddy, Ravi K. R and Picard, Martin and Broutin, Isabelle and Pos, Klaas M and Lambert, Olivier
Nature communications, ISSN 2041-1723, 02/2016, Volume 7, Issue 1, pp. 10731 - 10731
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Microscopy, Electron, Transmission | Native Polyacrylamide Gel Electrophoresis | Bacterial Outer Membrane Proteins - ultrastructure | Escherichia coli | Escherichia coli Proteins - metabolism | Escherichia coli Proteins - ultrastructure | Lipoproteins - ultrastructure | Nanostructures | Multiprotein Complexes - metabolism | Multiprotein Complexes - ultrastructure | Bacterial Outer Membrane Proteins - metabolism | Membrane Transport Proteins - ultrastructure | Drug Resistance, Multiple, Bacterial | Lipoproteins - metabolism | Membrane Transport Proteins - metabolism | Pseudomonas aeruginosa | Periplasmic Proteins - metabolism | Multidrug Resistance-Associated Proteins - metabolism | Multidrug Resistance-Associated Proteins - ultrastructure | Index Medicus | Life Sciences
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3. Full Text Effects of heavy metals on Cyanothece sp. CCY 0110 growth, extracellular polymeric substances (EPS) production, ultrastructure and protein profiles
by Mota, Rita and Pereira, Sara B and Meazzini, Marianna and Fernandes, Rui and Santos, Arlete and Evans, Caroline A and De Philippis, Roberto and Wright, Phillip C and Tamagnini, Paula
Journal of proteomics, ISSN 1874-3919, 04/2015, Volume 120, pp. 75 - 94
iTRAQ | Proteome | Cyanothece | Extracellular polymeric substances (EPS) | Heavy metals | Cyanobacteria | ITRAQ | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Biochemical Research Methods | Science & Technology | Gene Expression Regulation, Bacterial - drug effects | Cyanothece - physiology | Cell Proliferation - physiology | Metals, Heavy - pharmacology | Bacterial Proteins - metabolism | Cyanothece - ultrastructure | Cell Proliferation - drug effects | Cyanothece - drug effects | Proteome - metabolism | Gene Expression Regulation, Bacterial - physiology | Proteins | Physiological aspects | Carbohydrate metabolism | Analysis | Index Medicus
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4. Full Text Structural rearrangements of a polyketide synthase module during its catalytic cycle
by Whicher, Jonathan R and Dutta, Somnath and Hansen, Douglas A and Hale, Wendi A and Chemler, Joseph A and Dosey, Annie M and Narayan, Alison R. H and Håkansson, Kristina and Sherman, David H and Smith, Janet L and Skiniotis, Georgios
Nature (London), ISSN 0028-0836, 2014, Volume 510, Issue 7506, pp. 560 - 564
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Protein Structure, Tertiary | Catalytic Domain | Biocatalysis | Polyketide Synthases - ultrastructure | Acyl Carrier Protein - metabolism | Bacterial Proteins - chemistry | Models, Molecular | Alcohol Oxidoreductases - metabolism | Macrolides - metabolism | Acyltransferases - metabolism | Alcohol Oxidoreductases - ultrastructure | Cryoelectron Microscopy | Acyl Carrier Protein - chemistry | Polyketide Synthases - chemistry | Polyketide Synthases - metabolism | Alcohol Oxidoreductases - chemistry | Acyltransferases - ultrastructure | Bacterial Proteins - metabolism | Streptomyces - enzymology | Acyltransferases - chemistry | Bacterial Proteins - ultrastructure | Acyl Carrier Protein - ultrastructure | Streptomyces | Polyketides | Observations | Health aspects | Protein-protein interactions | Proteins | Fourier transforms | Biosynthesis | Chromatography | Crystal structure | Index Medicus
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5. Full Text Structural basis of MsbA-mediated lipopolysaccharide transport
by Mi, Wei and Li, Yanyan and Yoon, Sung Hwan and Ernst, Robert K and Walz, Thomas and Liao, Maofu
Nature (London), ISSN 0028-0836, 09/2017, Volume 549, Issue 7671, pp. 233 - 237
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Bacterial Proteins - chemistry | Lipopolysaccharides - metabolism | Adenosine Diphosphate - chemistry | Escherichia coli - cytology | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Biological Transport | Periplasm - metabolism | ATP-Binding Cassette Transporters - metabolism | Protein Domains | Cell Membrane - metabolism | Periplasm - chemistry | Periplasm - ultrastructure | Nanostructures - ultrastructure | Escherichia coli - enzymology | Models, Molecular | Cell Membrane - ultrastructure | Cryoelectron Microscopy | ATP-Binding Cassette Transporters - ultrastructure | Hydrophobic and Hydrophilic Interactions | Nanostructures - chemistry | Protein Binding | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Adenosine Diphosphate - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli - ultrastructure | Biological research | Biological transport | Physiological aspects | Cell membranes | Research | Lipopolysaccharides | Biology, Experimental | Adenosine diphosphate | Lipids | Hydrophobicity | Electron microscopy | Vanadate | Proteins | Transmission electron microscopy | Bacteria | Transmembrane domains | Gram-negative bacteria | Embedded structures | Cell envelopes | Transporter | Adenosine triphosphate | Conformation | Structural analysis | Index Medicus
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6. Full Text The pathway to GTPase activation of elongation factor SelB on the ribosome
by Fischer, Niels and Neumann, Piotr and Bock, Lars V and Maracci, Cristina and Wang, Zhe and Paleskava, Alena and Konevega, Andrey L and Schröder, Gunnar F and Grubmüller, Helmut and Ficner, Ralf and Rodnina, Marina V and Stark, Holger
Nature (London), ISSN 0028-0836, 12/2016, Volume 540, Issue 7631, pp. 80 - 85
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Selenocysteine - metabolism | Protein Biosynthesis | Ribosome Subunits, Large, Bacterial - metabolism | Codon, Terminator - genetics | Bacterial Proteins - chemistry | RNA, Transfer, Amino Acid-Specific - metabolism | Ribosomes - metabolism | GTP Phosphohydrolases - ultrastructure | Ribosomes - enzymology | Escherichia coli - metabolism | Protein Domains | Nucleic Acid Conformation | Binding Sites | Codon, Terminator - chemistry | Ribosome Subunits, Small, Bacterial - metabolism | Endoribonucleases - metabolism | Ribosome Subunits, Large, Bacterial - ultrastructure | Ribosomes - chemistry | Models, Molecular | RNA, Transfer, Amino Acid-Specific - genetics | Escherichia coli - chemistry | Codon, Terminator - metabolism | Cryoelectron Microscopy | RNA, Transfer, Amino Acid-Specific - chemistry | Ribosome Subunits, Small, Bacterial - ultrastructure | Ribosomes - ultrastructure | GTP Phosphohydrolases - metabolism | Ricin - metabolism | Escherichia coli - genetics | Ribosome Subunits, Large, Bacterial - chemistry | Protein Binding | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Enzyme Activation | RNA, Transfer, Amino Acid-Specific - ultrastructure | Ribosome Subunits, Small, Bacterial - chemistry | Escherichia coli - ultrastructure | Fungal Proteins - metabolism | Physiological aspects | Protein research | Protein biosynthesis | Research | Guanosine triphosphatase | Ribosomes | Enzymes | E coli | Ribonucleic acid--RNA | Crystal structure | Index Medicus
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7. Full Text MinCD cell division proteins form alternating copolymeric cytomotive filaments
by Ghosal, Debnath and Trambaiolo, Daniel and Amos, Linda A and Lowe, Jan
Nature communications, ISSN 2041-1723, 2014, Volume 5, Issue 1, pp. 5341 - 5341
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Cytoskeletal Proteins - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Cell Cycle Proteins - chemistry | Cell Membrane - chemistry | Cell Division | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Cytoskeletal Proteins - metabolism | Cell Membrane - metabolism | Membrane Proteins - metabolism | Binding Sites | Cytoskeleton - chemistry | Genes, Reporter | Green Fluorescent Proteins - metabolism | Gene Expression | Membrane Proteins - genetics | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | Polymerization | Escherichia coli Proteins - metabolism | Cell Membrane - ultrastructure | Cytoskeletal Proteins - chemistry | Cytoskeleton - ultrastructure | Recombinant Fusion Proteins - chemistry | Escherichia coli - chemistry | Microscopy, Electron | Protein Transport | Liposomes - chemistry | Membrane Proteins - chemistry | Cytoskeleton - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Adenosine Triphosphatases - chemistry | Bacterial Proteins - metabolism | Adenosine Triphosphatases - genetics | Mutation | Escherichia coli Proteins - chemistry | Liposomes - ultrastructure | Escherichia coli - ultrastructure | Index Medicus
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8. Full Text Structural basis for the regulated protease and chaperone function of DegP
by Krojer, Tobias and Clausen, Tim and Schäfer, Eva and Ehrmann, Michael and Sawa, Justyna and Saibil, Helen R
Nature (London), ISSN 0028-0836, 06/2008, Volume 453, Issue 7197, pp. 885 - 890
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Structure in molecular biology | Molecular biophysics | Crystalline structure | Escherichia coli - enzymology | Molecular Chaperones - metabolism | Periplasmic Proteins - chemistry | Heat-Shock Proteins - ultrastructure | Bacterial Outer Membrane Proteins - ultrastructure | Heat-Shock Proteins - metabolism | Bacterial Outer Membrane Proteins - chemistry | Models, Molecular | Crystallography, X-Ray | Serine Endopeptidases - chemistry | Structure-Activity Relationship | Molecular Chaperones - chemistry | Protein Folding | Bacterial Outer Membrane Proteins - biosynthesis | Cryoelectron Microscopy | Serine Endopeptidases - ultrastructure | Bacterial Outer Membrane Proteins - metabolism | Protein Structure, Quaternary | Cell Membrane - metabolism | Periplasmic Proteins - metabolism | Serine Endopeptidases - metabolism | Molecular Chaperones - ultrastructure | Periplasmic Proteins - ultrastructure | Heat-Shock Proteins - chemistry | Heat shock proteins | Chemical properties | Research | Structure | Protein folding | Proteases | Enzymes | E coli | Atoms & subatomic particles | Mass spectrometry | Substrates | Crystal structure | Index Medicus
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