scholarly article | Q13442814 |
P2093 | author name string | P John Hart | |
David R Borchelt | |||
Valeria C Culotta | |||
Duane D Winkler | |||
Jonathan P Schuermann | |||
Mark C Carroll | |||
Xiaohang Cao | |||
Stephen P Holloway | |||
Jody B Proescher | |||
P2860 | cites work | Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo | Q24298397 |
The copper chaperone for superoxide dismutase | Q24311669 | ||
Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis | Q24644037 | ||
Processing of X-ray diffraction data collected in oscillation mode | Q26778468 | ||
The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis | Q27641126 | ||
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS | Q27641284 | ||
Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase | Q27731976 | ||
Use of TLS parameters to model anisotropic displacements in macromolecular refinement | Q27860499 | ||
Coot: model-building tools for molecular graphics | Q27860505 | ||
Efficient anisotropic refinement of macromolecular structures using FFT | Q27861028 | ||
Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury | Q28511628 | ||
Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation | Q29547561 | ||
Unraveling the mechanisms involved in motor neuron degeneration in ALS | Q29619073 | ||
Pathogenic superoxide dismutase structure, folding, aggregation and turnover | Q30159887 | ||
Metals and neuroscience. | Q33878376 | ||
Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. | Q33897544 | ||
Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALS. | Q33979028 | ||
The copper chaperone CCS is abundant in neurons and astrocytes in human and rodent brain | Q34487153 | ||
Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. | Q35125315 | ||
Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathology | Q35749657 | ||
Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models | Q35956902 | ||
Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis | Q36161189 | ||
Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases | Q36539434 | ||
Selenocysteine positional variants reveal contributions to copper binding from cysteine residues in domains 2 and 3 of human copper chaperone for superoxide dismutase. | Q37104965 | ||
The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase | Q37375579 | ||
Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers | Q37619322 | ||
Oxygen and the copper chaperone CCS regulate posttranslational activation of Cu,Zn superoxide dismutase | Q37681868 | ||
Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants | Q41969514 | ||
Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. | Q41987289 | ||
Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg. | Q42252269 | ||
Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis | Q42846381 | ||
Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits | Q43556693 | ||
Copper and zinc binding modulates the aggregation and neurotoxic properties of the prion peptide PrP106-126. | Q43659816 | ||
Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site | Q44070818 | ||
Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature | Q44579313 | ||
Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. | Q44735743 | ||
Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability | Q45107835 | ||
ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. | Q46135324 | ||
Electrostatic recognition between superoxide and copper, zinc superoxide dismutase | Q47649395 | ||
An intersubunit disulfide bond prevents in vitro aggregation of a superoxide dismutase-1 mutant linked to familial amytrophic lateral sclerosis | Q47700139 | ||
A selenocysteine variant of the human copper chaperone for superoxide dismutase. A Se-XAS probe of cluster composition at the domain 3-domain 3 dimer interface | Q47790368 | ||
Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis | Q48177170 | ||
Restricted and regulated overexpression reveals calcineurin as a key component in the transition from short-term to long-term memory. | Q52040390 | ||
An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS. | Q52578937 | ||
Free R value: cross-validation in crystallography | Q57000467 | ||
A characterization of copper/zinc superoxide dismutase mutants at position 124. Zinc-deficient proteins | Q67913985 | ||
Heterodimer formation between superoxide dismutase and its copper chaperone | Q73255474 | ||
Decreased zinc affinity of amyotrophic lateral sclerosis-associated superoxide dismutase mutants leads to enhanced catalysis of tyrosine nitration by peroxynitrite | Q73829106 | ||
Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: alphaB-crystallin modulates aggregation | Q80340613 | ||
The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status | Q80485358 | ||
Disulphide-reduced superoxide dismutase-1 in CNS of transgenic amyotrophic lateral sclerosis models | Q81579334 | ||
Rats expressing human cytosolic copper-zinc superoxide dismutase transgenes with amyotrophic lateral sclerosis: associated mutations develop motor neuron disease | Q94029459 | ||
P433 | issue | 15 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | biophysics | Q7100 |
P304 | page(s) | 3436-47 | |
P577 | publication date | 2009-04-21 | |
P1433 | published in | Biochemistry | Q764876 |
P1476 | title | Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q † | |
P478 | volume | 48 |
Q28828156 | A faulty interaction between SOD1 and hCCS in neurodegenerative disease |
Q46242593 | A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants |
Q92513199 | A new function of copper zinc superoxide dismutase: as a regulatory DNA-binding protein in gene expression in response to intracellular hydrogen peroxide |
Q34981744 | Association of Nrf2 polymorphism haplotypes with acute lung injury phenotypes in inbred strains of mice |
Q41955617 | Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)? |
Q27658869 | Characterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase, |
Q34509452 | Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice. |
Q28275083 | Copper metallochaperones |
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 |
Q38769938 | Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site |
Q39601987 | Department of Veterans Affairs Geriatric Research, Education and Clinical Centers: translating aging research into clinical geriatrics |
Q27662078 | Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R |
Q33736326 | Finding inhibitors of mutant superoxide dismutase-1 for amyotrophic lateral sclerosis therapy from traditional chinese medicine |
Q35047631 | Heat shock factor 1 over-expression protects against exposure of hydrophobic residues on mutant SOD1 and early mortality in a mouse model of amyotrophic lateral sclerosis. |
Q33772493 | Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis. |
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) |
Q89706496 | Nucleation and kinetics of SOD1 aggregation in human cells for ALS1 |
Q55250072 | Quantifying the Interaction between Copper-Zinc Superoxide Dismutase (Sod1) and its Copper Chaperone (Ccs1). |
Q41911532 | S-acylation of SOD1, CCS, and a stable SOD1-CCS heterodimer in human spinal cords from ALS and non-ALS subjects |
Q30992306 | Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis |
Q64950127 | Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants. |
Q27657645 | Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A |
Q27664114 | Structures of mouse SOD1 and human/mouse SOD1 chimeras |
Q35049047 | Superoxide dismutases and superoxide reductases |
Q47889576 | The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase. |
Q43881721 | The application of hybrid pixel detectors for in-house SAXS instrumentation with a view to combined chromatographic operation |
Q91419222 | The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis |
Q54965091 | The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation. |
Q92317999 | The molecular pathogenesis of superoxide dismutase 1-linked ALS is promoted by low oxygen tension |
Q42731259 | The structural plasticity of the human copper chaperone for SOD1: insights from combined size-exclusion chromatographic and solution X-ray scattering studies |
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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