Characterization of variants of the pore-forming toxin ClyA from Escherichia coli controlled by a redox switch

Biochemistry

Volumn 53, Issue 40, 2014, Pages 6357-6369

  Roderer, Daniel ^a   Benke, Stephan ^b   Müller, Marcus ^a,c   Fäh Rechsteiner, Helene ^a   Ban, Nenad ^a   Schuler, Benjamin ^b   Glockshuber, Rudi ^a  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF ZURICH   (Switzerland)

^c DECTRIS LTD   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

CIRCULAR DICHROISM SPECTROSCOPY; COVALENT BONDS; DICHROISM; FLUORESCENCE SPECTROSCOPY; MONOMERS; SALMONELLA; SULFUR COMPOUNDS;

ASSEMBLY KINETICS; CONFORMATIONAL TRANSITIONS; DISULFIDE REDUCTION; HEMOLYTIC ACTIVITY; PORE FORMING TOXINS; SALMONELLA ENTERICA; SECONDARY STRUCTURES; STRUCTURAL REARRANGEMENT;

ESCHERICHIA COLI;

CYTOLYSIN; CYTOLYSIN A; DISULFIDE; MONOMER; UNCLASSIFIED DRUG; CYSTINE; ESCHERICHIA COLI PROTEIN; HEMOLYSIN; HEMOLYTIC AGENT; HLYE PROTEIN, E COLI;

ANIMAL CELL; ARTICLE; BINDING SITE; CHANNEL GATING; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; ERYTHROCYTE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HEMOLYSIS; NONHUMAN; OXIDATION REDUCTION STATE; PROTEIN ASSEMBLY; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; REDUCTION; TRANSMISSION ELECTRON MICROSCOPY; WILD TYPE; AMINO ACID SUBSTITUTION; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENETICS; HORSE; KINETICS; OXIDATION REDUCTION REACTION; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

AMINO ACID SUBSTITUTION; ANIMALS; CRYSTALLOGRAPHY, X-RAY; CYSTINE; ERYTHROCYTES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HEMOLYSIN PROTEINS; HEMOLYSIS; HEMOLYTIC AGENTS; HORSES; KINETICS; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 84908030403     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5007578     Document Type: Article

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