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)

scientific article published on 28 February 2020

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) is …
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scholarly articleQ13442814

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P356DOI10.3390/MOLECULES25051086
P932PMC publication ID7179120
P698PubMed publication ID32121118

P50authorGabriele MeloniQ55948458
Duane D WinklerQ64936480
Jenifer CalvoQ39184654
P2093author name stringStefanie D Boyd
Fatemeh Behnia
Morgan S Ullrich
P2860cites workSOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationQ21090100
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Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Q27653849
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Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80RQ27662078
Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALSQ27680903
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Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutaseQ28343973
Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injuryQ28511628
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Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosisQ56837049
Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu–Zn, Zn–Zn and As-isolated Wild-type EnzymesQ57909227
Erratum: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisQ59048476
Preparation and physicochemical properties of human erythrocupreinQ68599277
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Superoxide dismutase activity, oxidative damage, and mitochondrial energy metabolism in familial and sporadic amyotrophic lateral sclerosisQ72621641
The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide statusQ80485358
Quantifying chromatin-associated interactions: the HI-FI systemQ84838486
The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturationQ90364024
Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1Q91777865
Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Q33772493
Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis.Q33897544
Human zinc deficiencyQ33912975
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Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosisQ34438898
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 neuronsQ35206666
Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathologyQ35749657
Copper-zinc superoxide dismutase and amyotrophic lateral sclerosisQ36161189
Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)Q36187334
Zinc transporters and the cellular trafficking of zincQ36468399
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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Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry siteQ38769938
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Prognostic role of "prion-like propagation" in SOD1-linked familial ALS: an alternative viewQ42970220
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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 mutantsQ44778683
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 mutantsQ46242593
Copper-zinc superoxide dismutase: theoretical insights into the catalytic mechanismQ46451444
An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutaseQ47987103
On the stability of bovine superoxide dismutase. The effects of metals.Q48004534
Limited corticospinal tract involvement in amyotrophic lateral sclerosis subjects with the A4V mutation in the copper/zinc superoxide dismutase geneQ48447713
P275copyright licenseCreative Commons Attribution 4.0 InternationalQ20007257
P6216copyright statuscopyrightedQ50423863
P433issue5
P921main subjectamyotrophic lateral sclerosisQ206901
P577publication date2020-02-28
P1433published inMoleculesQ151332
P1476titleMutations 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)
P478volume25