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Journal of Biological Chemistry, ISSN 0021-9258, 12/2010, Volume 285, Issue 52, pp. 40573 - 40580
Secretion of the Escherichia coli toxin hemolysin A (HlyA) is catalyzed by the membrane protein complex HlyB-HlyD-TolC and requires a secretion sequence... 
SIGNAL | ANTIFOLDING ACTIVITY | SECB CHAPERONE | TRANSPORTER | MALTOSE-BINDING PROTEIN | MEMBRANE TRANSLOCATION | PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | EXPORT | EXPRESSION | Hemolysin Proteins - genetics | Bacterial Proteins - genetics | Escherichia coli Proteins - metabolism | Hemolysin Proteins - secretion | Multiprotein Complexes - genetics | Mutation, Missense | Bacterial Secretion Systems - physiology | Protein Folding | Carrier Proteins - genetics | Multiprotein Complexes - metabolism | Carrier Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli - genetics | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | Escherichia coli Proteins - genetics | Escherichia coli Proteins - secretion | Bacterial Proteins - metabolism | Membrane Transport Proteins - metabolism | Periplasmic Binding Proteins - genetics | Bacterial Outer Membrane Proteins - genetics | Hemolysin Proteins - metabolism | Amino Acid Substitution | Periplasmic Binding Proteins - metabolism | Bacterial Outer Membrane Proteins | Bacterial Secretion Systems | Hemolysin Proteins | Escherichia coli | Multiprotein Complexes | Biochemistry, Molecular Biology | Bacterial Proteins | Life Sciences | Microbiology and Parasitology | Escherichia coli Proteins | Membrane Transport Proteins | Periplasmic Binding Proteins | Carrier Proteins | Membrane Proteins | Fusion Protein | Secretion | Membrane Biology | ABC Transporter
Journal Article
PLoS Biology, ISSN 1544-9173, 2015, Volume 13, Issue 2, p. e1002049
Journal Article
Nature Communications, ISSN 2041-1723, 2015, Volume 6, Issue 1, p. 6198
Journal Article
PLoS ONE, ISSN 1932-6203, 07/2012, Volume 7, Issue 7, p. e40460
The Hly translocator complex of Escherichia coli catalyzes type I secretion of the toxin hemolysin A (HlyA). In this complex, HlyB is an inner membrane ABC... 
PERIPLASMIC COMPONENT | TRANSPORTER | TIP REGION | HAIRPIN | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | HEMOLYSIN TRANSLOCATOR | MULTIDRUG EFFLUX | IDENTIFICATION | HLYD | Hemolysin Proteins - genetics | Molecular Sequence Data | Acyltransferases - metabolism | Hemolysin Proteins - chemistry | Recombinant Fusion Proteins - metabolism | ATP-Binding Cassette Transporters - chemistry | ATP-Binding Cassette Transporters - genetics | Membrane Transport Proteins - genetics | Escherichia coli - metabolism | ATP-Binding Cassette Transporters - metabolism | Conserved Sequence | Membrane Transport Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Bacterial Outer Membrane Proteins - genetics | Aggregatibacter actinomycetemcomitans | Amino Acid Sequence | Mutagenesis, Site-Directed | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Recombinant Fusion Proteins - chemistry | Amino Acid Motifs | Membrane Transport Proteins - chemistry | Carrier Proteins - metabolism | Bacterial Outer Membrane Proteins - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Escherichia coli Proteins - chemistry | Hemolysin Proteins - metabolism | Amino Acid Substitution | Amino acids | Bacteria | Escherichia coli | Binding | Efflux | Membrane fusion | Polypeptides | Secretion | Cloning | Adaptors | Mutants | Membrane proteins | Proteins | E coli | Pharmacy | Physiology | Life sciences | Manufacturing | Mutation | Gram-negative bacteria | Localization | Transporter
Journal Article
Scientific Reports, ISSN 2045-2322, 12/2017, Volume 7, Issue 1, pp. 2386 - 9
Cry1A insecticidal toxins bind sequentially to different larval gut proteins facilitating oligomerization, membrane insertion and pore formation. Cry1Ac... 
MANDUCA-SEXTA | TRICHOPLUSIA-NI | ALKALINE-PHOSPHATASE | CABBAGE-LOOPER | MULTIDISCIPLINARY SCIENCES | PRE-PORE | INSECT RESISTANCE | HELICOVERPA-ARMIGERA LARVAE | PORE FORMATION | FIELD-EVOLVED RESISTANCE | MODIFIED BT TOXINS | Insecticides - chemistry | Hemolysin Proteins - pharmacology | Microvilli - chemistry | Hemolysin Proteins - genetics | Protein Multimerization | Bacterial Proteins - chemistry | Cell-Derived Microparticles - chemistry | Hemolysin Proteins - chemistry | Cell Membrane - chemistry | Larva - drug effects | Endotoxins - chemistry | Biological Control Agents - chemistry | Protein Engineering | Multidrug Resistance-Associated Proteins - genetics | Cell Membrane - metabolism | Cell-Derived Microparticles - metabolism | Larva - chemistry | Biological Control Agents - metabolism | Insect Proteins - metabolism | Cell Membrane - drug effects | Endotoxins - metabolism | Endotoxins - genetics | Insecticide Resistance | Larva - metabolism | Bacterial Proteins - genetics | Multidrug Resistance-Associated Proteins - chemistry | Insect Proteins - genetics | Microvilli - drug effects | Bacterial Proteins - pharmacology | Manduca - drug effects | Animals | Insecticides - metabolism | Microvilli - metabolism | Insect Proteins - chemistry | Protein Isoforms | Protein Binding | Bacterial Proteins - metabolism | Mutation | Multidrug Resistance-Associated Proteins - metabolism | Endotoxins - pharmacology | Hemolysin Proteins - metabolism | Moths - drug effects | Oligomerization | Cry1Ac toxin | Membrane vesicles | Toxins | Cadherin | ABC transporter | Western blotting
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2010, Volume 107, Issue 30, pp. 13473 - 13478
Staphylococcus aureus α-hemolysin (Hla), a potent cytotoxin, plays an important role in the pathogenesis of staphylococcal diseases, including those caused by... 
Receptors | Epithelial cells | Cell lines | Erythrocytes | Small interfering RNA | Cytotoxicity | Toxins | Cell membranes | Focal adhesions | Staphylococcus aureus | Cellular receptor | Pore-forming cytotoxin | CELLS | INFECTIONS | TYROSINE PHOSPHORYLATION | PROTECTION | pore-forming cytotoxin | TOXIN | MULTIDISCIPLINARY SCIENCES | P130(CAS) | MURINE MODEL | ERYTHROCYTES | PORE | BINDING | cellular receptor | Amyloid Precursor Protein Secretases - genetics | Epithelial Cells - metabolism | Hemolysin Proteins - pharmacology | Staphylococcus aureus - physiology | Hemolysin Proteins - genetics | Humans | Focal Adhesions | Molecular Sequence Data | Immunoblotting | RNA Interference | Membrane Proteins - metabolism | Staphylococcus aureus - metabolism | Staphylococcus aureus - genetics | Amino Acid Sequence | Cell Line | Cell Survival - drug effects | Rabbits | Membrane Proteins - genetics | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | ADAM10 Protein | Epithelial Cells - pathology | Host-Pathogen Interactions | Integrin beta1 - metabolism | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Bacterial Proteins - pharmacology | Animals | Epithelial Cells - microbiology | Erythrocytes - metabolism | Cell Line, Tumor | Protein Binding | Bacterial Proteins - metabolism | Mutation | ADAM Proteins - genetics | Integrin beta1 - genetics | Hemolysin Proteins - metabolism | Biological Sciences
Journal Article
Methods, ISSN 1046-2023, 2005, Volume 36, Issue 2, pp. 148 - 171
We provide an overview of lipid-dependent polytopic membrane protein topogenesis, with particular emphasis on Escherichia coli strains genetically altered in... 
Topogenesis | Protein topology | Membrane protein | Phosphatidylethanolamine | Cysteine scanning | Phospholipid | Maleimides | METAL-TETRACYCLINE/H+ ANTIPORTER | REDUCED FOLATE CARRIER | BIOCHEMISTRY & MOLECULAR BIOLOGY | F1F0 ATP SYNTHASE | BIOCHEMICAL RESEARCH METHODS | topogenesis | SCANNING MUTAGENESIS | PHOSPHOLIPID-COMPOSITION | LARGE ENVELOPE PROTEIN | phoshatidylethanolamine | ESCHERICHIA-COLI-CELLS | STAPHYLOCOCCAL ALPHA-HEMOLYSIN | protein topology | DEPENDENT PHOSPHOTRANSFERASE SYSTEM | membrane protein | cysteine scanning | ENDOPLASMIC-RETICULUM | phospholipid | maleimides | Models, Chemical | Cytoplasm - metabolism | Membrane Lipids - chemistry | Dose-Response Relationship, Drug | Lipids - chemistry | X-Ray Diffraction | Escherichia coli - metabolism | Sulfhydryl Compounds - chemistry | Cell Membrane - metabolism | Genes, Reporter | Catalytic Domain | Magnetic Resonance Spectroscopy | Protein Structure, Secondary | Phospholipids - chemistry | Lipid Metabolism | Glycosylation | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Macromolecular Substances | Membrane Transport Proteins - chemistry | Algorithms | Biochemistry - methods | Protein Isoforms | Liposomes - metabolism | Epitopes - chemistry | Lipid Bilayers - chemistry | Mutation | Maleimides - chemistry | Phosphatidylethanolamines - chemistry | Proteins | Protein biosynthesis | Cysteine | Methods | Cystine | Thiols | Chemical tests and reagents | Phospholipids
Journal Article
Infection and Immunity, ISSN 0019-9567, 2017, Volume 85, Issue 11, pp. e00541 - 17
The pathogenesis of Listeria monocytogenes depends on the ability of this bacterium to escape from the phagosome of the host cells via the action of the... 
Hemolysis | Listeria monocytogenes | Spontaneous mutations | Genomics | Virulence | STRAINS | INFECTIOUS DISEASES | spontaneous mutations | IMMUNOLOGY | LINEAGES | hemolysis | MUTANTS | PATHOGENICITY | EVOLUTION | virulence | GENES | PRFA | genomics | DIFFERENTIATION | MUTATIONS | EXPRESSION | Hemolysin Proteins - genetics | Humans | Phylogeny | Heat-Shock Proteins - genetics | Cloning, Molecular | Listeria monocytogenes - classification | Bacterial Toxins - genetics | Recombinant Proteins - metabolism | Severity of Illness Index | Peptide Termination Factors - genetics | Heat-Shock Proteins - metabolism | Bacterial Proteins - genetics | Selection, Genetic | Listeria monocytogenes - growth & development | Recombinant Proteins - genetics | Peptide Termination Factors - metabolism | Biological Evolution | Bacterial Toxins - metabolism | Erythrocytes - microbiology | Listeria monocytogenes - pathogenicity | Animals | Listeriosis - pathology | Listeria monocytogenes - genetics | Bacterial Proteins - metabolism | Listeriosis - microbiology | Mice | Mice, Inbred BALB C | Mutation | Gene Expression Regulation, Bacterial | Hemolysin Proteins - metabolism | Amino Acid Substitution | Erythrocytes | Listeriosis | Recombinant Proteins | Life Sciences | Bacterial Toxins | Heat-Shock Proteins | Hemolysin Proteins | Bacteriology | Bacterial Proteins | Human health and pathology | Microbiology and Parasitology | Infectious diseases | Peptide Termination Factors
Journal Article
Structure, ISSN 0969-2126, 10/2012, Volume 20, Issue 10, pp. 1778 - 1787
Journal Article
Biochemical Journal, ISSN 0264-6021, 01/2017, Volume 474, Issue 2, pp. 317 - 331
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/2009, Volume 106, Issue 31, pp. 12735 - 12740
Although the structures of many ß-barre I membrane proteins are available, our knowledge of the principles that govern their energetics and oligomerization... 
Proteins | Oligomers | Harmonic functions | Enzymes | Melting | Energy | Energy value | Monomers | Membrane proteins | P branes | Weakly stable TM strand | Membrane protein oligomerization |