Differential modification of Cys10 alters transthyretin's effect on beta-amyloid aggregation and toxicity

Protein Engineering, Design and Selection

Volumn 22, Issue 8, 2009, Pages 479-488

  Liu, Lin ^a,e   Hou, Jie ^a,f   Du, Jiali ^a   Chumanov, Robert S ^b   Xu, Qingge ^c   Ge, Ying ^c   Johnson, Jeffrey A ^b,d   Murphy, Regina M ^a  

^a University of Wisconsin Madison   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

^d UNIVERSITY OF WISCONSIN MADISON   (United States)

^e Wyeth Pharmaceutical   (United States)

^f SHIRE   (United States)

Author keywords

Alzheimer's disease; Beta amyloid; Post translational modification; Transthyretin

Indexed keywords

AGGREGATION KINETICS; ALZHEIMER'S DISEASE; AMYLOID DEPOSITS; BETA-AMYLOID; CEREBRO SPINAL FLUIDS; CORTICAL NEURONS; DIFFERENT EFFECTS; HUMAN PLASMAS; INSOLUBLE FIBRILS; INVERSE CORRELATION; NEUROFIBRILLARY TANGLES; NEURONAL CELL; NORMAL COMPONENT; POST-TRANSLATIONAL MODIFICATION; QUATERNARY STRUCTURE; TRANSTHYRETIN; UP-REGULATION;

CELL MEMBRANES; GLYCOPROTEINS; MARINE RISERS; NEURONS; PLASMA DIAGNOSTICS; PLASMAS;

TOXICITY;

AMYLOID BETA PROTEIN; PREALBUMIN;

ALZHEIMER DISEASE; ANIMAL EXPERIMENT; ARTICLE; BRAIN CELL; CELL LOSS; CELL PROTECTION; CEREBROSPINAL FLUID; CIRCULAR DICHROISM; CONTROLLED STUDY; CYTOTOXICITY; FEMALE; MOUSE; NEUROFIBRILLARY TANGLE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; PROTEIN QUATERNARY STRUCTURE; UPREGULATION;

AMYLOID BETA-PROTEIN; ANIMALS; CELL SURVIVAL; CELLS, CULTURED; CIRCULAR DICHROISM; CYSTEINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FEMALE; HYDROGEN-ION CONCENTRATION; KINETICS; MASS SPECTROMETRY; MICE; MICROSCOPY, ELECTRON, TRANSMISSION; NEURONS; PREALBUMIN; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS;

MUS;

EID: 70349202163     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzp025     Document Type: Article

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