| scholarly article | Q13442814 |
| P50 | author | Julian P Whitelegge | Q88590279 |
| P2093 | author name string | Armando Durazo | |
| Kym F Faull | |||
| Joan Selverstone Valentine | |||
| Aram M Nersissian | |||
| Bryan F Shaw | |||
| Madhuri Chattopadhyay | |||
| P2860 | cites work | The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis | Q27641126 |
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| Protein misfolding, functional amyloid, and human disease | Q28131732 | ||
| Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis | Q28131805 | ||
| Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation | Q29547561 | ||
| Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry | Q30159818 | ||
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| A billion-fold range in acidity for the solvent-exposed amides of Pyrococcus furiosus rubredoxin | Q31155352 | ||
| Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase | Q33423010 | ||
| Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. | Q33897544 | ||
| Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation | Q33928500 | ||
| Amyloid binding ligands as Alzheimer's disease therapies | Q35019441 | ||
| Electrostatic potential energy within a protein monitored by metal charge-dependent hydrogen exchange | Q35128913 | ||
| Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. | Q35818148 | ||
| Beta-sheet breakers for Alzheimer's disease therapy | Q35843392 | ||
| Hydrogen exchange methods to study protein folding | Q35850714 | ||
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| Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. | Q36512177 | ||
| How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein? | Q36701609 | ||
| Initiation and elongation in fibrillation of ALS-linked superoxide dismutase | Q36978868 | ||
| A common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop | Q37431412 | ||
| Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis. | Q38291855 | ||
| Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins | Q43898083 | ||
| High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation | Q43918294 | ||
| Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations | Q57187844 | ||
| Dynamic model of globular protein conformations based on NMR studies in solution | Q67381833 | ||
| Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase | Q70862448 | ||
| A general multistate model for the analysis of hydrogen-exchange kinetics | Q71392264 | ||
| Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance | Q72684541 | ||
| The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status | Q80485358 | ||
| P433 | issue | 49 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | amyotrophic lateral sclerosis | Q206901 |
| beta barrel | Q310424 | ||
| P304 | page(s) | 34382-34389 | |
| P577 | publication date | 2009-10-05 | |
| P1433 | published in | Journal of Biological Chemistry | Q867727 |
| P1476 | title | Metal-free superoxide dismutase-1 and three different amyotrophic lateral sclerosis variants share a similar partially unfolded beta-barrel at physiological temperature | |
| P478 | volume | 284 |
| Q51261579 | A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis. |
| Q38174873 | An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis |
| Q36246992 | Anti-superoxide dismutase antibodies are associated with survival in patients with sporadic amyotrophic lateral sclerosis |
| Q45953477 | Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS). |
| Q42160937 | Cellular toxicity of mutant SOD1 protein is linked to an easily soluble, non-aggregated form in vitro |
| Q33671609 | Conformational specificity of the C4F6 SOD1 antibody; low frequency of reactivity in sporadic ALS cases |
| Q40885460 | Dynamic properties of SOD1 mutants can predict survival time of patients carrying familial amyotrophic lateral sclerosis. |
| Q37012813 | Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation |
| Q57457968 | Exposure of Solvent-Inaccessible Regions in the Amyloidogenic Protein Human SOD1 Determined by Hydroxyl Radical Footprinting |
| Q34082710 | Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants |
| Q34317439 | Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis. |
| Q27677527 | Ligand binding and aggregation of pathogenic SOD1 |
| Q30850744 | Lipid-associated aggregate formation of superoxide dismutase-1 is initiated by membrane-targeting loops |
| Q35887311 | Localization of a toxic form of superoxide dismutase 1 protein to pathologically affected tissues in familial ALS |
| Q50069615 | Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling |
| Q48302583 | Oral treatment with Cu(II)(atsm) increases mutant SOD1 in vivo but protects motor neurons and improves the phenotype of a transgenic mouse model of amyotrophic lateral sclerosis. |
| Q42074999 | Protein charge ladders reveal that the net charge of ALS-linked superoxide dismutase can be different in sign and magnitude from predicted values. |
| Q37918059 | Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis |
| Q46713654 | Reduced net charge and heterogeneity of pI isoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase |
| Q42664185 | Small molecules present in the cerebrospinal fluid metabolome influence superoxide dismutase 1 aggregation |
| Q36991027 | Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy |
| Q35049047 | Superoxide dismutases and superoxide reductases |
| Q36020398 | Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept |
| Q36381998 | The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation |
| Q47889576 | The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase. |
| Q28263899 | The complex molecular biology of amyotrophic lateral sclerosis (ALS) |
| Q30497215 | Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS |
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