Wild-type Cu/Zn superoxide dismutase stabilizes mutant variants by heterodimerization

Neurobiology of Disease

Volumn 62, Issue , 2014, Pages 479-488

  Weichert, Anna ^a   Besemer, Anna S ^a   Liebl, Martina ^a   Hellmann, Nadja ^f   Koziollek Drechsler, Ingrid ^a   Ip, Philbert ^b,c,d   Decker, Heinz ^f   Robertson, Janice ^b,e   Chakrabartty, Avijit ^b   Behl, Christian ^a   Clement, Albrecht M ^a  

^a UNIVERSITY MEDICAL CENTER MAINZ   (Germany)

^b UNIVERSITY OF TORONTO   (Canada)

^c PRINCESS MARGARET HOSPITAL   (Canada)

^d MaRS Centre   (Canada)

^e UNIVERSITY OF TORONTO   (Canada)

^f JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Dismutase activity; Heterodimerization; Misfolding; Mutant homodimers; Protein aggregation; SEDI; SOD1; USOD

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; HETERODIMER; MUTANT PROTEIN;

ANTIBODY AFFINITY; ARTICLE; BIOCHEMISTRY; CIRCULAR DICHROISM; CONTROLLED STUDY; DIMERIZATION; ENZYME ACTIVITY; ENZYME STABILITY; GENE EXPRESSION; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DEFECT; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; SOD1 GENE; WILD TYPE;

DISMUTASE ACTIVITY; HETERODIMERIZATION; MISFOLDING; MUTANT HOMODIMERS; PROTEIN AGGREGATION; SEDI; SOD1; USOD;

HEK293 CELLS; HUMANS; MUTATION; PROTEIN MULTIMERIZATION; SUPEROXIDE DISMUTASE;

EID: 84888115055     PISSN: 09699961     EISSN: 1095953X     Source Type: Journal    
DOI: 10.1016/j.nbd.2013.10.027     Document Type: Article

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