Neuroserpin Portland (Ser52Arg) is trapped as an inactive intermediate that rapidly forms polymers Implications for the epilepsy seen in the dementia FENIB

European Journal of Biochemistry

Volumn 271, Issue 16, 2004, Pages 3360-3367

  Belorgey, Didier ^a,d   Sharp, Lynda K ^a   Crowther, Damian C ^a   Onda, Maki ^b   Johansson, Jan ^c   Lomas, David A ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b Osaka Prefecture University   (Japan)

^c SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^d WELLCOME TRUST SANGER INSTITUTE   (United Kingdom)

Author keywords

Conformational diseases; Neuroserpin; Polymerization; Serpin; Serpinopathies

Indexed keywords

POLYMER; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR; TISSUE PLASMINOGEN ACTIVATOR; UREA;

ARTICLE; BRAIN DISEASE; CELL INCLUSION; DEMENTIA; HUMAN; HUMAN CELL; PHENOTYPE; POLYMERIZATION; PRIORITY JOURNAL; SEQUENCE ANALYSIS; TEMPERATURE SENSITIVITY;

AMINO ACID SUBSTITUTION; ARGININE; BIOPOLYMERS; CATALYSIS; CIRCULAR DICHROISM; DEMENTIA; EPILEPSY; HUMANS; HYDROLYSIS; INCLUSION BODIES; MODELS, MOLECULAR; NEUROPEPTIDES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SERINE; SERPINS; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TISSUE PLASMINOGEN ACTIVATOR; UREA;

EID: 4344586923     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04270.x     Document Type: Article

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