Congo red populates partially unfolded states of an amyloidogenic protein to enhance aggregation and amyloid fibril formation

Journal of Biological Chemistry

Volumn 278, Issue 12, 2003, Pages 10842-10850

  Kim, Yong Sung ^a,d   Randolph, Theodore W ^b   Manning, Mark C ^a   Stevens, Fred J ^c   Carpenter, John F ^a  

^a UNIVERSITY OF COLORADO   (United States)

^b University of Colorado at Boulder   (United States)

^c ARGONNE NATIONAL LABORATORY   (United States)

^d Massachusetts Institute of Technology   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; CALORIMETRY; CONFORMATIONS; ION EXCHANGE; THERMODYNAMIC STABILITY; TITRATION;

CONGO RED (CR);

PROTEINS;

AMYLOID; AMYLOID PROTEIN; CONGO RED; DEUTERIUM; DIMER; HYDROGEN; IMMUNOGLOBULIN LIGHT CHAIN;

ARTICLE; CALORIMETRY; CHEMICAL BINDING; CONTROLLED STUDY; ENTHALPY; IMMUNOGLOBULIN VARIABLE REGION; KINETICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON TRANSPORT; THERMODYNAMICS; THERMOSTABILITY; CHEMISTRY; CIRCULAR DICHROISM; DIMERIZATION; DOSE RESPONSE; ELECTRON MICROSCOPY; HUMAN; INFRARED SPECTROSCOPY;

AMYLOID; CIRCULAR DICHROISM; CONGO RED; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; IMMUNOGLOBULIN LIGHT CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MICROSCOPY, ELECTRON; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 0038532258     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M212540200     Document Type: Article

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