| scholarly article | Q13442814 |
| P6179 | Dimensions Publication ID | 1099597466 |
| P356 | DOI | 10.1038/S41598-017-17815-Y |
| P932 | PMC publication ID | 5727297 |
| P698 | PubMed publication ID | 29234142 |
| P50 | author | Lucia Banci | Q21264278 |
| Letizia Barbieri | Q47316526 | ||
| Enrico Luchinat | Q47316533 | ||
| P2860 | cites work | Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement | Q49023143 |
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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 | ||
| Equilibrium thermodynamic analysis of amyotrophic lateral sclerosis-associated mutant apo Cu,Zn superoxide dismutases | Q83924087 | ||
| The copper chaperone CCS directly interacts with copper/zinc superoxide dismutase | Q24310363 | ||
| Heterodimeric structure of superoxide dismutase in complex with its metallochaperone | Q27634428 | ||
| Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q † | Q27653849 | ||
| Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme? | Q27765168 | ||
| Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis | Q28131805 | ||
| A faulty interaction between SOD1 and hCCS in neurodegenerative disease | Q28828156 | ||
| A time- and cost-efficient system for high-level protein production in mammalian cells | Q29616132 | ||
| Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1. | Q30157900 | ||
| Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase | Q33423010 | ||
| Atomic-resolution monitoring of protein maturation in live human cells by NMR | Q33595355 | ||
| Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis. | Q33772493 | ||
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| Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS. | Q33979028 | ||
| Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state | Q34429205 | ||
| The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain | Q34487153 | ||
| Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice. | Q34509452 | ||
| Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS | Q35854965 | ||
| Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS) | Q36187334 | ||
| Activation of superoxide dismutases: putting the metal to the pedal | Q36530953 | ||
| The right to choose: multiple pathways for activating copper,zinc superoxide dismutase | Q37375615 | ||
| Cellular distribution of copper to superoxide dismutase involves scaffolding by membranes | Q37409241 | ||
| Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. | Q37646220 | ||
| Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. | Q38291855 | ||
| Structural Biology outside the box-inside the cell | Q38653247 | ||
| Mutant SOD1 mediated pathogenesis of Amyotrophic Lateral Sclerosis | Q38666305 | ||
| Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site | Q38769938 | ||
| In-cell NMR: a topical review | Q38934591 | ||
| Oligomerization of mutant SOD1 in mitochondria of motoneuronal cells drives mitochondrial damage and cell toxicity | Q39864397 | ||
| Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis | Q39972533 | ||
| Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. | Q41987289 | ||
| Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues | Q43821139 | ||
| Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form | Q46807674 | ||
| In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. | Q46809689 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P4510 | describes a project that uses | ImageJ | Q1659584 |
| P433 | issue | 1 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular chaperones | Q422496 |
| P304 | page(s) | 17433 | |
| P577 | publication date | 2017-12-12 | |
| P1433 | published in | Scientific Reports | Q2261792 |
| P1476 | title | A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants | |
| P478 | volume | 7 |
| Q60922146 | Applications of In-Cell NMR in Structural Biology and Drug Discovery |
| Q61803739 | Cadmium effects on superoxide dismutase 1 in human cells revealed by NMR |
| Q91777865 | Copper-zinc superoxide dismutase (Sod1) activation terminates interaction between its copper chaperone (Ccs) and the cytosolic metal-binding domain of the copper importer Ctr1 |
| Q64265968 | Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS |
| Q89976497 | 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) |
| Q55250072 | Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1). |
| Q91419222 | The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis |
| Q90364024 | The yeast copper chaperone for copper-zinc superoxide dismutase (CCS1) is a multifunctional chaperone promoting all levels of SOD1 maturation |
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