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Nature (London), ISSN 1476-4687, 2015, Volume 523, Issue 7562, pp. 555 - 560
Journal Article
Journal of bacteriology, ISSN 0021-9193, 2008, Volume 190, Issue 12, pp. 4147 - 4161
Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
HUMAN EPITHELIAL-CELLS | YERSINIA-ENTEROCOLITICA | BACTERIAL ADHESINS | BARTONELLA ADHESIN | NEISSERIA-MENINGITIDIS | HEMOLYSIN PRODUCTION | MICROBIOLOGY | MORAXELLA-CATARRHALIS | EXTRACELLULAR-MATRIX | BIOFILM FORMATION | ANTIGEN-43-MEDIATED AUTOAGGREGATION | Epithelial Cells - metabolism | Humans | Biofilms - growth & development | Molecular Sequence Data | Adhesins, Escherichia coli - chemistry | Adhesins, Escherichia coli - genetics | Bacterial Adhesion - physiology | Escherichia coli - metabolism | Female | Escherichia coli - growth & development | Dimerization | Urinary Tract - microbiology | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Adhesins, Escherichia coli - metabolism | Protein Structure, Secondary | Escherichia coli Infections - microbiology | Escherichia coli Proteins - metabolism | Escherichia coli Infections - metabolism | Blotting, Western | Fibronectins - metabolism | Sequence Homology, Amino Acid | Animals | Escherichia coli - genetics | Epithelial Cells - microbiology | Bacterial Adhesion - genetics | Escherichia coli Proteins - genetics | Mice | HeLa Cells | Laminin - metabolism | Escherichia coli Proteins - chemistry | Microscopy, Fluorescence | Usage | Carrier proteins | Escherichia coli | Physiological aspects | Genetic aspects | Research | Gene expression | Biofilms/growth & development | Adhesins, Escherichia coli/chemistry | Life Sciences | Adhesins, Escherichia coli/genetics | Escherichia coli Proteins/genetics | Escherichia coli/growth & development | Laminin/metabolism | Epithelial Cells/metabolism | Adhesins, Escherichia coli/metabolism | Escherichia coli Infections/metabolism | Escherichia coli/genetics | Escherichia coli/metabolism | Bacteriology | Microbiology and Parasitology | Epithelial Cells/microbiology | Escherichia coli Proteins/chemistry | Escherichia coli Proteins/metabolism | Fibronectins/metabolism | Escherichia coli Infections/microbiology | Urinary Tract/microbiology | Bacterial Adhesion/genetics | Bacterial Adhesion/physiology | Molecular Biology of Pathogens
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2018, Volume 293, Issue 43, pp. 16778 - 16790
Cytochromes c are ubiquitous proteins, essential for life in most organisms. Their distinctive characteristic is the covalent attachment of heme to their polypeptide chain... 
post-translational modification (PTM) | CHAPERONE CCME | cytochrome c maturation | BACTERIA | APOCYTOCHROME-C | heme | NMR-SPECTROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CcmE | ESCHERICHIA-COLI | TRAFFICKING | CcmC | protein-protein interactions | BIOGENESIS SYSTEM | PATHWAY | nuclear magnetic resonance (NMR) | Gram-negative bacteria | System I | cytochrome c | BINDING SITE | LIGATION COMPLEX | Apoproteins - chemistry | Hemeproteins - genetics | Heme - metabolism | Crystallography, X-Ray | Cytochromes c - genetics | Cytochromes c - chemistry | Heme - chemistry | Heme - genetics | Hemeproteins - chemistry | Escherichia coli - metabolism | Membrane Proteins - metabolism | Protein Interaction Domains and Motifs | Escherichia coli - growth & development | Binding Sites | Apoproteins - metabolism | Bacterial Outer Membrane Proteins - genetics | Mutagenesis, Site-Directed | Hemeproteins - metabolism | Membrane Proteins - genetics | Cytochromes c - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Escherichia coli - genetics | Apoproteins - genetics | Escherichia coli Proteins - genetics | Protein Conformation | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Index Medicus | Bioenergetics
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 2758 - 11
Uropathogenic Escherichia coli attach to tissues using pili type 1. Each pilus is composed by thousands of coiled FimA domains followed by the domains of the tip fibrillum, FimF-FimG-FimH... 
UROPATHOGENIC ESCHERICHIA-COLI | DISULFIDE BOND FORMATION | ATOMIC-FORCE MICROSCOPY | SINGLE PROTEIN | CHAPERONE-USHER PATHWAY | STABILITY | MULTIDISCIPLINARY SCIENCES | FIMD USHER | CATCH BONDS | DONOR-STRAND EXCHANGE | DSBA | Disulfides - metabolism | Molecular Chaperones - metabolism | Fimbriae Proteins - metabolism | Protein Disulfide-Isomerases - metabolism | Molecular Chaperones - chemistry | Fimbriae, Bacterial - genetics | Adhesins, Escherichia coli - chemistry | Adhesins, Escherichia coli - genetics | Uropathogenic Escherichia coli - metabolism | Uropathogenic Escherichia coli - ultrastructure | Disulfides - chemistry | Cloning, Molecular | Escherichia coli - metabolism | Microscopy, Atomic Force | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Gene Expression | Adhesins, Escherichia coli - metabolism | Genetic Vectors - chemistry | Molecular Chaperones - genetics | Genetic Vectors - metabolism | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Fimbriae, Bacterial - ultrastructure | Recombinant Proteins - genetics | Uropathogenic Escherichia coli - genetics | Molecular Dynamics Simulation | Protein Folding | Protein Disulfide-Isomerases - genetics | Fimbriae Proteins - genetics | Protein Conformation, beta-Strand | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Fimbriae Proteins - chemistry | Protein Disulfide-Isomerases - chemistry | Escherichia coli Proteins - chemistry | Fimbriae, Bacterial - metabolism | Pathogens | Spectroscopy | Disulfide bonds | Stability | Pili | E coli | Oxidoreductase | Folding | Molecular chains
Journal Article
Nature (London), ISSN 1476-4687, 2014, Volume 510, Issue 7503, pp. 172 - 175
Previous studies have established that the folding, structure and function of membrane proteins are influenced by their lipid environments(1-7... 
MYCOBACTERIUM-TUBERCULOSIS | ATOM FORCE-FIELD | MOLECULAR-DYNAMICS | MULTIDISCIPLINARY SCIENCES | COMPLEXES | PURIFICATION | ION-CHANNEL | MOBILITY-MASS SPECTROMETRY | MODEL | MSCL | WATER | Apoproteins - chemistry | Cardiolipins - pharmacology | Protein Unfolding - drug effects | Protein Conformation - drug effects | Aquaporins - chemistry | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Membrane Lipids - chemistry | Cation Transport Proteins - metabolism | Protein Folding - drug effects | Mass Spectrometry | Mycobacterium tuberculosis - chemistry | Membrane Proteins - metabolism | Ion Channels - chemistry | Phosphatidylglycerols - metabolism | Apoproteins - metabolism | Ammonia - metabolism | Models, Molecular | Aquaporins - metabolism | Escherichia coli Proteins - metabolism | Cardiolipins - metabolism | Escherichia coli - chemistry | Cardiolipins - chemistry | Phosphatidylglycerols - chemistry | Ion Channels - metabolism | Membrane Proteins - chemistry | Protein Stability - drug effects | Membrane Lipids - metabolism | Phosphatidylglycerols - pharmacology | Bacterial Proteins - metabolism | Membrane Lipids - pharmacology | Lipid Bilayers - chemistry | Cation Transport Proteins - chemistry | Escherichia coli Proteins - chemistry | Biological research | Physiological aspects | Lipids | Cooperative binding (Biochemistry) | Research | Structure | Molecular biology | Membrane proteins | Biology, Experimental | Proteins | Studies | Membranes | E coli | Binding sites | Crystal structure
Journal Article
eLife, ISSN 2050-084X, 2015, Volume 4, Issue 4, pp. 1 - 44
The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family... 
N-Ethylmaleimide-Sensitive Proteins - metabolism | Mad2 Proteins - metabolism | Molecular Chaperones - metabolism | Caenorhabditis elegans Proteins - chemistry | Humans | Crystallography, X-Ray | Phylogeny | N-Ethylmaleimide-Sensitive Proteins - genetics | Amino Acid Sequence | Gene Expression | Caenorhabditis elegans - genetics | Cell Cycle Proteins - metabolism | Molecular Chaperones - genetics | Adenosine Triphosphatases - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Nuclear Proteins - chemistry | Caenorhabditis elegans - classification | Escherichia coli - genetics | Adenosine Triphosphatases - genetics | Escherichia coli Proteins - chemistry | Caenorhabditis elegans Proteins - genetics | Caenorhabditis elegans - enzymology | Adaptor Proteins, Signal Transducing - chemistry | Endopeptidase Clp - chemistry | M Phase Cell Cycle Checkpoints | Caenorhabditis elegans Proteins - metabolism | Molecular Sequence Data | Molecular Chaperones - chemistry | Cell Cycle Proteins - chemistry | Spindle Apparatus - genetics | Escherichia coli - metabolism | Cell Cycle Proteins - genetics | Carrier Proteins - chemistry | Nuclear Proteins - genetics | N-Ethylmaleimide-Sensitive Proteins - chemistry | Protein Structure, Tertiary | Recombinant Proteins - metabolism | ATPases Associated with Diverse Cellular Activities | Endopeptidase Clp - genetics | Escherichia coli Proteins - metabolism | Nuclear Proteins - metabolism | Endopeptidase Clp - metabolism | Mad2 Proteins - chemistry | Recombinant Proteins - genetics | Sequence Homology, Amino Acid | Carrier Proteins - genetics | Sequence Alignment | Animals | Carrier Proteins - metabolism | Adaptor Proteins, Signal Transducing - genetics | Mad2 Proteins - genetics | Escherichia coli Proteins - genetics | Protein Binding | Adenosine Triphosphatases - chemistry | Adaptor Proteins, Signal Transducing - metabolism | Spindle Apparatus - enzymology | Proteins | Medical research | Recombination | Software | Meiosis | Mammals | Chromosomes | DNA repair | Deoxyribonucleic acid--DNA | Adenosine triphosphatase | BASIC BIOLOGICAL SCIENCES
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2011, Volume 333, Issue 6048, pp. 1445 - 1449
Bacterial chromosomes are confined in submicrometer-sized nucleoids. Chromosome organization is facilitated by nucleoid-associated proteins (NAPs... 
Proteins | Molecules | DNA | Genes | Imaging | REPORTS | Cell lines | Genetic loci | Gene expression regulation | Genomes | Chromosomes | LOCALIZATION | STRUCTURING PROTEIN | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | DYNAMICS | OLIGOMERIZATION | MICROSCOPY | H-NS PROTEIN | BINDING | EXPRESSION | Molecular Chaperones - metabolism | DNA, Bacterial - metabolism | Factor For Inversion Stimulation Protein - metabolism | Fimbriae Proteins - metabolism | Protein Multimerization | DNA, Bacterial - chemistry | Genetic Loci | Recombinant Fusion Proteins - metabolism | Escherichia coli K12 - ultrastructure | DNA-Binding Proteins - metabolism | Integration Host Factors - metabolism | Chromosomes, Bacterial - metabolism | Escherichia coli K12 - metabolism | Cell Division | Nucleic Acid Conformation | Binding Sites | Repressor Proteins - metabolism | Protein Structure, Tertiary | Genome, Bacterial | Repressor Proteins - chemistry | Operon | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Chromosomes, Bacterial - ultrastructure | Fimbriae Proteins - genetics | Escherichia coli Proteins - genetics | Fimbriae Proteins - chemistry | Escherichia coli K12 - genetics | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Cellular proteins | Research | Properties | Bacterial genetics | E coli | Microbiology | Bacterial proteins
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2012, Volume 338, Issue 6111, pp. 1214 - 1217
Journal Article
Journal Article