SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability.
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Trimming Down a Protein Structure to Its Bare Foldons: SPATIAL ORGANIZATION OF THE COOPERATIVE UNITThe complex molecular biology of amyotrophic lateral sclerosis (ALS)Nuclear export of misfolded SOD1 mediated by a normally buried NES-like sequence reduces proteotoxicity in the nucleus.Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesDecreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.The stability of myocilin olfactomedin domain variants provides new insight into glaucoma as a protein misfolding disorder.Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis.Glutathionylation at Cys-111 induces dissociation of wild type and FALS mutant SOD1 dimers.Thermodynamics of protein destabilization in live cellsAmyotrophic lateral sclerosis: update and new developments.Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.Early steps in thermal unfolding of superoxide dismutase 1 are similar to the conformational changes associated with the ALS-associated A4V mutation.Distinctive features of the D101N and D101G variants of superoxide dismutase 1; two mutations that produce rapidly progressing motor neuron diseaseSpecies-specific activation of Cu/Zn SOD by its CCS copper chaperone in the pathogenic yeast Candida albicans.Computing disease-linked SOD1 mutations: deciphering protein stability and patient-phenotype relations.Mutant superoxide dismutase-1 indistinguishable from wild-type causes ALS.Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1Dynamic properties of SOD1 mutants can predict survival time of patients carrying familial amyotrophic lateral sclerosis.Susceptibility of Mutant SOD1 to Form a Destabilized Monomer Predicts Cellular Aggregation and Toxicity but Not In vitro Aggregation Propensity.Protein charge ladders reveal that the net charge of ALS-linked superoxide dismutase can be different in sign and magnitude from predicted values.Prognostic role of "prion-like propagation" in SOD1-linked familial ALS: an alternative view.Superoxide dismutase 1 is positively selected to minimize protein aggregation in great apes.Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.Study of mutation and misfolding of Cu-Zn SOD1 protein.Destabilization of the metal site as a hub for the pathogenic mechanism of five ALS-linked mutants of copper, zinc superoxide dismutase.Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study.Tryptophan 32-mediated SOD1 aggregation is attenuated by pyrimidine-like compounds in living cellsImplications of Metal Binding and Asparagine Deamidation for Amyloid Formation
P2860
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P2860
SOD1 mutations targeting surface hydrogen bonds promote amyotrophic lateral sclerosis without reducing apo-state stability.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
SOD1 mutations targeting surfa ...... reducing apo-state stability.
@en
type
label
SOD1 mutations targeting surfa ...... reducing apo-state stability.
@en
prefLabel
SOD1 mutations targeting surfa ...... reducing apo-state stability.
@en
P2093
P2860
P356
P1476
SOD1 mutations targeting surfa ...... reducing apo-state stability.
@en
P2093
Gerhard Gröbner
Mikael Oliveberg
Roberth Byström
P2860
P304
19544-19552
P356
10.1074/JBC.M109.086074
P407
P577
2010-02-26T00:00:00Z