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Volumn 277, Issue 21, 2002, Pages 19027-19036
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Amyloid-like fibril formation in an all β-barrel protein involves the formation of partially structured intermediate(s)
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Author keywords
[No Author keywords available]
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Indexed keywords
ORGANIC OSMOLYTES;
CONFORMATIONS;
ELECTRON MICROSCOPY;
NUCLEAR MAGNETIC RESONANCE;
ORGANIC COMPOUNDS;
PROTEINS;
X RAY DIFFRACTION ANALYSIS;
BIOCHEMISTRY;
ACIDIC FIBROBLAST GROWTH FACTOR;
AMYLOID;
ANILINO 8 NAPHTHALENESULFONATE;
BETA BARREL PROTEIN;
PROLINE;
SOLVENT;
SULFONIC ACID DERIVATIVE;
UNCLASSIFIED DRUG;
ANIMAL CELL;
ARTICLE;
ELECTRON MICROSCOPY;
FIBER;
NEWT;
NONHUMAN;
NUCLEAR MAGNETIC RESONANCE;
OSMOLALITY;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE;
REACTION ANALYSIS;
THERMAL ANALYSIS;
X RAY DIFFRACTION;
AMYLOID;
ANIMALS;
CIRCULAR DICHROISM;
FIBROBLAST GROWTH FACTOR 1;
HEAT;
MICROSCOPY, ELECTRON;
MODELS, MOLECULAR;
NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR;
PROTEIN CONFORMATION;
PROTEIN DENATURATION;
RECOMBINANT PROTEINS;
SALAMANDRIDAE;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
X-RAY DIFFRACTION;
ANIMALIA;
INVERTEBRATA;
NOTOPHTHALMUS VIRIDESCENS;
SALAMANDRIDAE;
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EID: 0037166276
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M110762200 Document Type: Article |
Times cited : (62)
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References (45)
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