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Volumn 277, Issue 15, 2002, Pages 12657-12665

Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH

(6) Souillac, Pierre O a Uversky, Vladimir N a Millett, Ian S a Khurana, Ritu a Doniach, Sebastian a Fink, Anthony L a,b

a UNIVERSITY OF CALIFORNIA (United States)

b STANFORD UNIVERSITY (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOLOGY; OLIGOMERS; PH EFFECTS; PHYSIOLOGY; UREA;

FIBRILLATION;

PROTEINS;

AMYLOID; IMMUNOGLOBULIN LIGHT CHAIN; UREA;

AMYLOIDOSIS; ARTICLE; ESCHERICHIA COLI; KINETICS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; THERMOSTABILITY;

AMYLOID; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN LIGHT CHAINS; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; UREA;

ESCHERICHIA COLI;

EID: 0037066786 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M109230200 Document Type: Article

Times cited : (80)

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