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Cell (Cambridge), ISSN 0092-8674, 2011, Volume 145, Issue 1, pp. 54 - 66
Journal Article
Cell host & microbe, ISSN 1931-3128, 2007, Volume 1, Issue 1, pp. 77 - 83
Many bacteria pathogenic for plants or animals, including Shigella spp., which is responsible for shigellosis in humans, use a type III secretion apparatus to inject effector proteins into host cells... 
PROTEINS | MICROBIO | SHIGELLA-FLEXNERI | IMMUNITY | MUTANTS | TRANSCRIPTION | MICROBIOLOGY | DIVERSITY | SACCHAROMYCES-CEREVISIAE | G-PROTEIN | EXPRESSION | APPARATUS | CELL-DEATH | Protein Kinases - metabolism | Protein Kinases - genetics | Shigella flexneri - genetics | Saccharomyces cerevisiae - genetics | Shigella flexneri - metabolism | Humans | Shigella flexneri - pathogenicity | Ubiquitin - metabolism | Antigens, Bacterial - genetics | Saccharomyces cerevisiae - metabolism | Mitogen-Activated Protein Kinase Kinases | Protein Kinase C - metabolism | Genes, Reporter | Protein Structure, Tertiary | Bacterial Proteins - genetics | Ubiquitin-Protein Ligases - metabolism | Pheromones - metabolism | Saccharomyces cerevisiae Proteins - genetics | Animals | Saccharomyces cerevisiae Proteins - metabolism | Bacterial Proteins - metabolism | Signal Transduction - physiology | Biological Transport - physiology | Proteasome Endopeptidase Complex - metabolism | Ubiquitin-Protein Ligases - genetics | Antigens, Bacterial - metabolism | Mitogen-Activated Protein Kinases - metabolism | Ubiquitin | Ligases | Mitogen-Activated Protein Kinases | Signal Transduction | Biochemistry, Molecular Biology | Shigella flexneri | Antigens, Bacterial | Pheromones | Proteasome Endopeptidase Complex | Bacterial Proteins | Ubiquitin-Protein Ligases | Life Sciences | Protein Kinases | Biological Transport | Saccharomyces cerevisiae Proteins | Saccharomyces cerevisiae | Protein Kinase C
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 (London), ISSN 1476-4687, 2015, Volume 523, Issue 7562, pp. 555 - 560
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2011, Volume 108, Issue 36, pp. 14944 - 14949
The bacterial pathogen Helicobacter pylori chronically infects the human gastric mucosa and is the leading risk factor for the development of gastric cancer.... 
Helicobacter pylori | Epithelial cells | DNA damage | DNA | Cell nucleus | Cell lines | Bacteria | Cultured cells | Infections | Mice | Chromosome breaks | DNA damage signaling | Gastric tumorigenesis | Genomic instability | CYTOLETHAL DISTENDING TOXIN | MULTIDISCIPLINARY SCIENCES | RISK | MISMATCH REPAIR | COLONIZATION | GENETIC INSTABILITY | EPITHELIAL-CELLS | chromosome breaks | GASTRIC-CANCER | INFLAMMATION | INFECTION | MICE | genomic instability | gastric tumorigenesis | Phosphorylation | Epithelial Cells - metabolism | Humans | Stomach Neoplasms - metabolism | Helicobacter Infections - complications | Stomach Neoplasms - pathology | Intracellular Signaling Peptides and Proteins - metabolism | Antigens, Bacterial - genetics | DNA Breaks, Double-Stranded | Helicobacter Infections - pathology | DNA-Binding Proteins - metabolism | Tumor Suppressor Proteins - genetics | Trans-Activators - genetics | Cell Cycle Proteins - genetics | Helicobacter Infections - metabolism | Nuclear Proteins - genetics | Intracellular Signaling Peptides and Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Stomach Neoplasms - genetics | Tumor Suppressor Proteins - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Protein-Serine-Threonine Kinases - genetics | Genomic Islands | Epithelial Cells - pathology | Nuclear Proteins - metabolism | Ataxia Telangiectasia Mutated Proteins | DNA-Binding Proteins - genetics | Chromosomal Proteins, Non-Histone - genetics | Bacterial Adhesion | Stomach Neoplasms - microbiology | Animals | Histones - genetics | Helicobacter pylori - metabolism | Epithelial Cells - microbiology | Chromosome Aberrations | Cell Line, Tumor | Bacterial Proteins - metabolism | Trans-Activators - metabolism | Histones - metabolism | Tumor Suppressor p53-Binding Protein 1 | Antigens, Bacterial - metabolism | Carcinogens | Cocarcinogens | Physiological aspects | Genetic aspects | Research | Health aspects | Cells | 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
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
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 09/2009, Volume 106, Issue 37, pp. 15628 - 15632
...Assembly of the Cdc45-Mcm2–7-GINS complex in human cells requires the Ctf4/And-1, RecQL4, and Mcm10 proteins Jun-Sub Im a,1 , Sang-Hee Ki a,1 , Andrea Farina b... 
Cdc7-Dbf4 kinase | Cyclin-dependent kinase | Cdc45-Mcm-GINS complex | Bimolecular fluorescence complementation | BUDDING YEAST | INITIATION | MULTIDISCIPLINARY SCIENCES | EUKARYOTIC DNA-REPLICATION | POLYMERASE-ALPHA | SACCHAROMYCES-CEREVISIAE | CDC45 | ROTHMUND-THOMSON-SYNDROME | S-PHASE | TOPBP1 | bimolecular fluorescence complementation | cyclin-dependent kinase | PROGRESSION | Minichromosome Maintenance Proteins | Cyclin-Dependent Kinases - metabolism | RecQ Helicases - metabolism | Humans | Multiprotein Complexes | Bacterial Proteins - chemistry | RecQ Helicases - genetics | Minichromosome Maintenance Complex Component 7 | Minichromosome Maintenance Complex Component 2 | Recombinant Fusion Proteins - metabolism | Cell Cycle Proteins - chemistry | DNA-Binding Proteins - metabolism | Cell Cycle Proteins - genetics | Luminescent Proteins - chemistry | Nuclear Proteins - genetics | Protein-Serine-Threonine Kinases - metabolism | Chromosomal Proteins, Non-Histone - metabolism | Bacterial Proteins - genetics | Cell Cycle Proteins - metabolism | Nuclear Proteins - metabolism | Recombinant Fusion Proteins - chemistry | DNA-Binding Proteins - genetics | Nuclear Proteins - chemistry | DNA-Binding Proteins - chemistry | Chromosomal Proteins, Non-Histone - genetics | Carrier Proteins - metabolism | Cell Cycle | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | RecQ Helicases - chemistry | HeLa Cells | Chromosomal Proteins, Non-Histone - chemistry | Luminescent Proteins - metabolism | Proteins | DNA replication | HeLa cells | Physiological aspects | Genetic aspects | Research | Molecular biology | Biological Sciences
Journal Article
PLoS ONE, ISSN 1932-6203, 09/2012, Volume 7, Issue 9, p. e46275
Escherichia coli FadR plays two regulatory roles in fatty acid metabolism. FadR represses the fatty acid degradation (fad... 
DNA-BINDING | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | GROWTH | DEGRADATION | SYNTHETASE | EXCISION | RECEPTOR PROTEIN | REPRESSOR | TRANSCRIPTION FACTOR | ACYL-COENZYME | Protein Kinases - metabolism | Protein Kinases - genetics | Coenzyme A Ligases - genetics | Cyclic AMP Receptor Protein - genetics | Cyclic AMP Receptor Protein - metabolism | Oxygen - metabolism | Coenzyme A Ligases - metabolism | Regulon | Fatty Acid Transport Proteins - metabolism | Biological Transport | Escherichia coli - metabolism | Transcription, Genetic | Membrane Proteins - metabolism | Binding Sites | Cyclic AMP - metabolism | Fatty Acids - metabolism | Bacterial Outer Membrane Proteins - genetics | Repressor Proteins - metabolism | Promoter Regions, Genetic | Oxidation-Reduction | Signal Transduction | Membrane Proteins - genetics | Bacterial Proteins - genetics | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Bacterial Proteins - metabolism | Gene Expression Regulation, Bacterial | Fatty Acid Transport Proteins - genetics | Fatty acid metabolism | Crosstalk | Analysis | Escherichia coli | Physiological aspects | Cyclic adenylic acid | Research | Genetic transcription | Enzymes | Regulators | Oxygen | Transcription | Genes | Cyclic AMP | Chains | Biosynthesis | Glucose | Metabolism | Gene expression | Fatty acids | Flavin-adenine dinucleotide | Proteins | FADD protein | E coli | Plasmids | Oxidation | In vivo methods and tests | Transport | Binding sites
Journal Article
Journal Article
Nature communications, ISSN 2041-1723, 2018, Volume 9, Issue 1, pp. 825 - 12
STIM1 and Orai1 are key components of the Ca2+-release activated Ca2+ (CRAC) current. Orai1, which represents the subunit forming the CRAC channel complex, is... 
CHANNEL FUNCTION | OPERATED CALCIUM-ENTRY | ORAI CHANNELS | MULTIDISCIPLINARY SCIENCES | MUTATION | CA2+ SENSOR | STORE | INTERACTION MOLECULE-1 STIM1 | PLASMA-MEMBRANE | SAM DOMAIN | CRAC CHANNEL | Calcium - metabolism | Dyslexia - metabolism | Humans | Dyslexia - pathology | Green Fluorescent Proteins - genetics | Calcium - chemistry | ORAI1 Protein - chemistry | Migraine Disorders - pathology | Stromal Interaction Molecule 1 - chemistry | Neoplasm Proteins - genetics | Binding Sites | Blood Platelet Disorders - genetics | ORAI1 Protein - metabolism | Amino Acid Sequence | Gene Expression | Models, Molecular | Recombinant Proteins - chemistry | Neoplasm Proteins - chemistry | Patch-Clamp Techniques | Migraine Disorders - genetics | Miosis - pathology | Luminescent Proteins - genetics | Muscle Fatigue - genetics | Miosis - metabolism | Blood Platelet Disorders - pathology | Ichthyosis - metabolism | Protein Multimerization | Erythrocytes, Abnormal - metabolism | Neoplasm Proteins - metabolism | Stromal Interaction Molecule 1 - genetics | Migraine Disorders - metabolism | Ichthyosis - pathology | Miosis - genetics | HEK293 Cells | Ichthyosis - genetics | Ion Transport | Protein Interaction Domains and Motifs | Spleen - pathology | Genes, Reporter | Recombinant Proteins - metabolism | Green Fluorescent Proteins - metabolism | Protein Conformation, alpha-Helical | ORAI1 Protein - genetics | Bacterial Proteins - genetics | Gene Expression Regulation | Recombinant Proteins - genetics | Spleen - abnormalities | Dyslexia - genetics | Point Mutation | Stromal Interaction Molecule 1 - metabolism | Erythrocytes, Abnormal - pathology | Spleen - metabolism | Protein Binding | Bacterial Proteins - metabolism | Blood Platelet Disorders - metabolism | Amino Acid Substitution | Luminescent Proteins - metabolism | Calcium channels | STIM1 protein | Activation | Exposure | Orai1 protein | Elongation | Calcium ions
Journal Article