Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.
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Misfolded CuZnSOD and amyotrophic lateral sclerosisEvidence for a novel role of copper-zinc superoxide dismutase in zinc metabolism.Transcriptional activation in yeast in response to copper deficiency involves copper-zinc superoxide dismutaseThe proteome response to amyloid protein expression in vivoPost-translational modification of Cu/Zn superoxide dismutase under anaerobic conditions.Function of the Greek key connection analysed using circular permutants of superoxide dismutase.Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the proteinModeling Huntington disease in yeast: perspectives and future directions.Insights into SOD1-linked amyotrophic lateral sclerosis from NMR studies of Ni(2+)- and other metal-ion-substituted wild-type copper-zinc superoxide dismutases.Aggregation modulating elements in mutant human superoxide dismutase 1.Common denominator of Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis: decreased stability of the apo state.Role of disulfide cross-linking of mutant SOD1 in the formation of inclusion-body-like structures.Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells.Measuring copper and zinc superoxide dismutase from spinal cord tissue using electrospray mass spectrometry.Analysis of mutant SOD1 electrophoretic mobility by Blue Native gel electrophoresis; evidence for soluble multimeric assembliesA common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.Transition metal homeostasis: from yeast to human disease.Using yeast models to probe the molecular basis of amyotrophic lateral sclerosis.Contribution of yeast models to neurodegeneration research.A limited role for disulfide cross-linking in the aggregation of mutant SOD1 linked to familial amyotrophic lateral sclerosis.Antioxidant functions required for insusceptibility of Saccharomyces cerevisiae to tetracycline antibiotics.Copper/zinc-Superoxide dismutase is required for oxytetracycline resistance of Saccharomyces cerevisiae.Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis.Copper stabilizes a heterodimer of the yCCS metallochaperone and its target superoxide dismutase.The structural analysis of the pro-oxidant copper-binding site of denatured apo-H43R SOD1 and the elucidation of the origin of the acquisition of the pro-oxidant activity.Rapid one-step purification of native dimeric ALS-associated human Cu/Zn superoxide dismutase from transgenic rat tissues.ALS Yeast Models—Past Success Stories and New Opportunities
P2860
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P2860
Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh
1994年學術文章
@zh-hant
name
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@ast
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@en
type
label
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@ast
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@en
prefLabel
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@ast
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@en
P2093
P2860
P356
P1476
Characterization of three yeas ...... amyotrophic lateral sclerosis.
@en
P2093
C R Nishida
E B Gralla
J S Valentine
P2860
P304
P356
10.1073/PNAS.91.21.9906
P407
P577
1994-10-01T00:00:00Z