scholarly article | Q13442814 |
P50 | author | Gabriele Meloni | Q55948458 |
Duane D Winkler | Q64936480 | ||
Jenifer Calvo | Q39184654 | ||
P2093 | author name string | Stefanie D Boyd | |
Fatemeh Behnia | |||
Morgan S Ullrich | |||
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Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutase | Q28343973 | ||
Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury | Q28511628 | ||
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The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status | Q80485358 | ||
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The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturation | Q90364024 | ||
Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1 | Q91777865 | ||
Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis. | Q33772493 | ||
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Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis | Q34438898 | ||
Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice. | Q34509452 | ||
Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. | Q35125315 | ||
Astrocytes from familial and sporadic ALS patients are toxic to motor neurons | Q35206666 | ||
Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology | Q35749657 | ||
Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis | Q36161189 | ||
Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS) | Q36187334 | ||
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How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? | Q36701609 | ||
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Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V. | Q37359481 | ||
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Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants | Q44778683 | ||
Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. | Q45251257 | ||
A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants | Q46242593 | ||
Copper-zinc superoxide dismutase: theoretical insights into the catalytic mechanism | Q46451444 | ||
An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase | Q47987103 | ||
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Limited corticospinal tract involvement in amyotrophic lateral sclerosis subjects with the A4V mutation in the copper/zinc superoxide dismutase gene | Q48447713 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 5 | |
P921 | main subject | amyotrophic lateral sclerosis | Q206901 |
P577 | publication date | 2020-02-28 | |
P1433 | published in | Molecules | Q151332 |
P1476 | title | Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs) | |
P478 | volume | 25 |