Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers

Biochemistry

Volumn 50, Issue 32, 2011, Pages 7057-7066

  Redler, Rachel L ^a   Wilcox, Kyle C ^a,b   Proctor, Elizabeth A ^a,b   Fee, Lanette ^a   Caplow, Michael ^a   Dokholyan, Nikolay V ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION PROPENSITY; AMYOTROPHIC LATERAL SCLEROSIS; ASSOCIATION RATES; COMPUTATIONAL RESULTS; CU/ZN-SUPEROXIDE DISMUTASE; CYTOSOLIC ENZYMES; DIMER INTERFACE; DISEASE PROGRESSION; DISSOCIATION KINETICS; DISSOCIATION RATES; EQUILIBRIUM DISSOCIATION CONSTANT; GLUTATHIONYLATION; MISFOLDING; OXIDATIVE MODIFICATION; REDOX REGULATION; STRUCTURAL MODELING; STRUCTURAL REARRANGEMENT; WILD TYPES;

NEURODEGENERATIVE DISEASES; OXYGEN; SURFACE PLASMON RESONANCE;

DISSOCIATION;

CYSTINE; DIMER; GLUTATHIONE; SUPEROXIDE DISMUTASE;

AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; COMPUTATIONAL FLUID DYNAMICS; DISSOCIATION; DISSOCIATION CONSTANT; HUMAN; MODEL; MUTANT; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN PROCESSING; SURFACE PLASMON RESONANCE; WILD TYPE;

CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CYSTEINE; DIMERIZATION; GLUTATHIONE; KINETICS; MUTATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUPEROXIDE DISMUTASE; SURFACE PLASMON RESONANCE;

EID: 80051503291     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200614y     Document Type: Article

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