The 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenic

Biochemistry

Volumn 48, Issue 48, 2009, Pages 11370-11380

  Solomon, James P ^a   Yonemoto, Isaac T ^a   Murray, Amber N ^a   Price, Joshua L ^a   Powers, Evan T ^a   Balch, William E ^a   Kelly, Jeffery W ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID DISEASE; AMYLOID FIBRIL; AMYLOIDOGENESIS; C-TERMINAL FRAGMENTS; CONCENTRATION DEPENDENCE; ENDOPROTEOLYSIS; FINNISH; GELSOLIN; HIGH ENERGY; HUMAN PLASMAS; IN-VITRO; MATRIX METALLOPROTEASE; MEMBRANE TYPES; MISFOLDING; MMP INHIBITOR; NUCLEATED POLYMERIZATION; SECRETORY PATHWAYS; TRANSGENIC MICE;

AMINO ACIDS; OLIGOMERS; ORGANIC ACIDS; POLYMERIZATION; ULSI CIRCUITS;

GLYCOPROTEINS;

AMYLOID; GELSOLIN; INTERSTITIAL COLLAGENASE;

AMYLOIDOSIS; ARTICLE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN POLYMERIZATION;

AMYLOID; AMYLOIDOSIS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GELSOLIN; HUMANS; MICROSCOPY, ATOMIC FORCE; MOLECULAR WEIGHT; PEPTIDE FRAGMENTS; SPECTROMETRY, FLUORESCENCE;

MUS MUSCULUS;

EID: 73149083275     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901368e     Document Type: Article

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