| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/J.FREERADBIOMED.2003.12.021 |
| P8608 | Fatcat ID | release_fkixysh42jhonhdryv4tzo4skq |
| P698 | PubMed publication ID | 15019975 |
| P2093 | author name string | Joseph S Beckman | |
| Douglas F Barofsky | |||
| Barbara Leinweber | |||
| Elisabeth Barofsky | |||
| Keith Nylin | |||
| Vladimir Ermilov | |||
| P433 | issue | 7 | |
| P921 | main subject | Escherichia coli | Q25419 |
| amyotrophic lateral sclerosis | Q206901 | ||
| P304 | page(s) | 911-918 | |
| P577 | publication date | 2004-04-01 | |
| P1433 | published in | Free Radical Biology and Medicine | Q5500023 |
| P1476 | title | Aggregation of ALS mutant superoxide dismutase expressed in Escherichia coli | |
| P478 | volume | 36 |
| Q95379945 | A novel 65-mer peptide imitates the synergism of superoxide dismutase and glutathione peroxidase |
| Q33742705 | A role for copper in the toxicity of zinc-deficient superoxide dismutase to motor neurons in amyotrophic lateral sclerosis |
| Q53296871 | ALS Untangled No.33 Endotherapia |
| Q40409233 | Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis. |
| Q45251257 | Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. |
| Q30420296 | Automatic Determination of Disulfide Bridges in Proteins |
| Q34232041 | Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability. |
| Q37194259 | Direct magnetic resonance evidence for peroxymonocarbonate involvement in the cu,zn-superoxide dismutase peroxidase catalytic cycle |
| Q37326811 | Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis |
| Q35055366 | Measuring copper and zinc superoxide dismutase from spinal cord tissue using electrospray mass spectrometry. |
| Q36466309 | Rapid profiling of disease alleles using a tunable reporter of protein misfolding. |
| Q41825746 | Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis. |
| Q35062293 | Selective fluorescent imaging of superoxide in vivo using ethidium-based probes |
| Q27648424 | Structural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALS |
| Q41668065 | Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity. |
| Q84493518 | Targeting of monomer/misfolded SOD1 as a therapeutic strategy for amyotrophic lateral sclerosis |
Search more.