Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant

Proceedings of the National Academy of Sciences of the United States of America

Volumn 103, Issue 36, 2006, Pages 13357-13361

  Ignatova, Zoya ^a,b   Gierasch, Lila M ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

Amyloid; Huntington's disease; Osmolyte; Polyglutamine; Proline

Indexed keywords

HUNTINGTIN; ORGANIC COMPOUND; POLYGLUTAMINE; PROLINE; PROTEIN P39A; RETINOIC ACID BINDING PROTEIN; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; CELL TYPE; CONTROLLED STUDY; DEGENERATIVE DISEASE; ESCHERICHIA COLI; EXON; HUNTINGTON CHOREA; IN VIVO STUDY; NONHUMAN; PARKINSON DISEASE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILIZATION;

ALANINE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ESCHERICHIA COLI; EXONS; FLUORESCEINS; FLUORESCENT DYES; GLUTAMINE; HUMANS; KINETICS; MICROSCOPY, FLUORESCENCE; MODELS, BIOLOGICAL; NERVE TISSUE PROTEINS; NUCLEAR PROTEINS; ORGANOMETALLIC COMPOUNDS; OSMOLAR CONCENTRATION; OSMOTIC PRESSURE; PROLINE; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEINS; RECEPTORS, RETINOIC ACID; RECOMBINANT FUSION PROTEINS; SOLUBILITY; SPECTROMETRY, FLUORESCENCE;

ESCHERICHIA COLI;

EID: 33748588165     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0603772103     Document Type: Article

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