The structural stability and chaperone activity of artemin, a ferritin homologue from diapause-destined Artemia embryos, depend on different cysteine residues

Cell Stress and Chaperones

Volumn 16, Issue 2, 2011, Pages 133-141

  Hu, Yan ^a   Bojikova Fournier, Svetla ^a   King, Allison M ^a   MacRae, Thomas H ^a  

^a DALHOUSIE UNIVERSITY   (Canada)

Author keywords

Artemia franciscana; Artemin; Cysteine; Diapause; Ferritin homologue; Molecular chaperone; Protein structure function

Indexed keywords

ALANINE; ARTEMIN; CHAPERONE; CITRATE SYNTHASE; CYSTEINE; OLIGOMER;

AMINO ACID SUBSTITUTION; ARTEMIA; ARTICLE; BACTERIUM TRANSFORMATION; CONTROLLED STUDY; DENATURATION; DIAPAUSE; EMBRYO; ENZYME ACTIVITY; HEAT; HYDROPHOBICITY; IN VITRO STUDY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; PURIFICATION; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANIMALS; ARTEMIA; CYSTEINE; EMBRYO, NONMAMMALIAN; FERRITINS; HOT TEMPERATURE; INVERTEBRATE HORMONES; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NEUROPEPTIDES; PROTEIN STABILITY; RNA-BINDING PROTEINS; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP;

ARTEMIA; ARTEMIA FRANCISCANA; CRUSTACEA;

EID: 79951673529     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-010-0225-7     Document Type: Article

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