| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2009PNAS..106.6980B |
| P356 | DOI | 10.1073/PNAS.0809845106 |
| P8608 | Fatcat ID | release_7nrn7uzvqfevfhpvy2r5dlvpba |
| P3181 | OpenCitations bibliographic resource ID | 2666051 |
| P932 | PMC publication ID | 2678485 |
| P698 | PubMed publication ID | 19369197 |
| P5875 | ResearchGate publication ID | 24280267 |
| P50 | author | Ivano Bertini | Q3804830 |
| Mirela Boca | Q88573756 | ||
| Stefania Girotto | Q117221441 | ||
| Miguela Vieru | Q117221442 | ||
| Lucia Banci | Q21264278 | ||
| Francesca Cantini | Q28316949 | ||
| Vito Calderone | Q28323962 | ||
| P2860 | cites work | Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. | Q37646220 |
| Mapping superoxide dismutase 1 domains of non-native interaction: roles of intra- and intermolecular disulfide bonding in aggregation | Q37707829 | ||
| A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis. | Q38291545 | ||
| Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis | Q39731255 | ||
| Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1. | Q40100098 | ||
| Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis | Q42846381 | ||
| Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria | Q43708597 | ||
| Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. | Q44441857 | ||
| Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. | Q44735743 | ||
| Familial amyotrophic lateral sclerosis with His46Arg mutation in Cu/Zn superoxide dismutase presenting characteristic clinical features and Lewy body-like hyaline inclusions | Q45090366 | ||
| Arrangement of subunits and ordering of beta-strands in an amyloid sheet | Q46564095 | ||
| Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase | Q46566731 | ||
| Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis | Q48177170 | ||
| SOFAST-HMQC Experiments for Recording Two-dimensional Deteronuclear Correlation Spectra of Proteins within a Few Seconds | Q57896548 | ||
| The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status | Q80485358 | ||
| SOD1 and amyotrophic lateral sclerosis: mutations and oligomerization | Q21090100 | ||
| Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice | Q24544265 | ||
| Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis | Q24644037 | ||
| Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase | Q27639986 | ||
| 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 | ||
| Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein folding | Q27641822 | ||
| ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization | Q27641993 | ||
| A fraction of yeast Cu,Zn-superoxide dismutase and its metallochaperone, CCS, localize to the intermembrane space of mitochondria. A physiological role for SOD1 in guarding against mitochondrial oxidative damage. | Q27936872 | ||
| Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria | Q28270155 | ||
| A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal | Q28907138 | ||
| Primary structure effects on peptide group hydrogen exchange | Q29614750 | ||
| Unraveling the mechanisms involved in motor neuron degeneration in ALS | Q29619073 | ||
| Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria | Q34565165 | ||
| Familial ALS-superoxide dismutases associate with mitochondria and shift their redox potentials. | Q35012498 | ||
| Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS | Q35854965 | ||
| Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis | Q36161189 | ||
| P433 | issue | 17 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | superoxide dismutase 1 | Q2041084 |
| identical protein binding | Q14762994 | ||
| P304 | page(s) | 6980-5 | |
| P577 | publication date | 2009-04-28 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants | |
| P478 | volume | 106 |
| Q51261579 | A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis. |
| Q92862303 | A protocol to automatically calculate homo-oligomeric protein structures through the integration of evolutionary constraints and NMR ambiguous contacts |
| Q28730723 | Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis |
| Q46791114 | Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation |
| Q50969723 | Addition of exogenous SOD1 aggregates causes TDP-43 mislocalisation and aggregation. |
| Q34442177 | Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypes |
| Q38773599 | Amyotrophic lateral sclerosis-like superoxide dismutase 1 proteinopathy is associated with neuronal loss in Parkinson's disease brain |
| Q38174873 | An emerging role for misfolded wild-type SOD1 in sporadic ALS pathogenesis |
| Q37673274 | Basic mechanisms of neurodegeneration: a critical update |
| Q28277615 | Cellular copper distribution: a mechanistic systems biology approach |
| Q58773578 | Cholesterol secosterol aldehyde adduction and aggregation of Cu,Zn-superoxide dismutase: Potential implications in ALS |
| Q50666722 | Colorimetric tracking of protein structural evolution based on the distance-dependent light scattering of embedded gold nanoparticles. |
| Q30155526 | Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels |
| Q47738138 | Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human-A Discrete Molecular Dynamics Study |
| Q33680425 | DNA-Triggered Aggregation of Copper, Zinc Superoxide Dismutase in the Presence of Ascorbate |
| Q39719416 | Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1 |
| Q33652243 | Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells |
| Q43244834 | Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. |
| Q35021849 | Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation |
| Q40885460 | Dynamic properties of SOD1 mutants can predict survival time of patients carrying familial amyotrophic lateral sclerosis. |
| Q28115819 | Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases |
| Q57457968 | Exposure of Solvent-Inaccessible Regions in the Amyloidogenic Protein Human SOD1 Determined by Hydroxyl Radical Footprinting |
| Q27676522 | Global structural motions from the strain of a single hydrogen bond |
| Q30393668 | Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts |
| Q34328850 | Huntingtin fragments and SOD1 mutants form soluble oligomers in the cell |
| Q34317439 | Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis. |
| Q34684165 | Identification of human monoclonal antibodies specific for human SOD1 recognizing distinct epitopes and forms of SOD1. |
| Q37563994 | Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis |
| Q34009391 | In-cell NMR in E. coli to monitor maturation steps of hSOD1. |
| Q46809689 | In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants. |
| Q93083328 | Interaction of Half Oxa-/Half cis-Platin Complex with Human Superoxide Dismutase and Induced Reduction of Neurotoxicity |
| Q30850744 | Lipid-associated aggregate formation of superoxide dismutase-1 is initiated by membrane-targeting loops |
| Q92176495 | Mechanisms of SOD1 regulation by post-translational modifications |
| Q44778683 | Mechanistic aspects of hSOD1 maturation from the solution structure of Cu(I) -loaded hCCS domain 1 and analysis of disulfide-free hSOD1 mutants |
| Q47382895 | Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior |
| Q50069615 | Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling |
| Q30374274 | Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols. |
| Q30431829 | Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants |
| Q47127143 | Partially native intermediates mediate misfolding of SOD1 in single-molecule folding trajectories |
| Q38091029 | Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis. |
| Q34999535 | Recent advances in our understanding of neurodegeneration |
| Q33819255 | Role of mitochondria in mutant SOD1 linked amyotrophic lateral sclerosis |
| Q41049208 | SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability |
| Q47403040 | Size-selective concentration and label-free characterization of protein aggregates using a Raman active nanofluidic device |
| Q30153414 | Solid-state NMR studies of metal-free SOD1 fibrillar structures |
| Q47985099 | Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study. |
| Q64950127 | Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants. |
| Q28477745 | Structural, stability, dynamic and binding properties of the ALS-causing T46I mutant of the hVAPB MSP domain as revealed by NMR and MD simulations |
| Q35049047 | Superoxide dismutases and superoxide reductases |
| Q41668065 | Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity. |
| Q36633172 | TDP-43 or FUS-induced misfolded human wild-type SOD1 can propagate intercellularly in a prion-like fashion |
| Q47889576 | The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase. |
| Q91419222 | The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis |
| Q39437151 | The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis |
| Q37416520 | Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization |
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