Conformational constraints for amyloid fibrillation: The importance of being unfolded

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1698, Issue 2, 2004, Pages 131-153

  Uversky, Vladimir N ^a,b   Fink, Anthony L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

Author keywords

Amyloid; Conformational stability; Fibrillation; Natively unfolded protein; Partially folded intermediate

Indexed keywords

ACIDIC FIBROBLAST GROWTH FACTOR; ACYLPHOSPHATASE; ALPHA LACTALBUMIN; ALPHA SYNUCLEIN; AMYLIN; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; APOLIPOPROTEIN; APOLIPOPROTEIN C2; BETA 2 MICROGLOBULIN; CYTOCHROME C; GLOBULAR PROTEIN; IMMUNOGLOBULIN LIGHT CHAIN; INSULIN; LYSOZYME; METHIONYL AMINOPEPTIDASE; MONELLIN; MYOGLOBIN; PHOSPHOGLYCERATE KINASE; POLYGLUTAMINE; PRION PROTEIN; PROTEIN P53; PROTHYMOSIN ALPHA; SERUM AMYLOID A; STRUCTURAL PROTEIN; TAU PROTEIN; TETRAMER; TUMOR SUPPRESSOR PROTEIN;

AMYLOIDOSIS; CHRONIC INFLAMMATION; EQUILIBRIUM CONSTANT; FIBER; HUMAN; KIDNEY DISEASE; MALIGNANT NEOPLASTIC DISEASE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; REVIEW;

AMYLOID; ANIMALS; CIRCULAR DICHROISM; COLLOIDS; HUMANS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON; PROTEIN CONFORMATION; PROTEIN DENATURATION;

EID: 2342569618     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.12.008     Document Type: Review

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