Intense Superoxide Dismutase-1 Immunoreactivity in Intracytoplasmic Hyaline Inclusions of Familial Amyotrophic Lateral Sclerosis with Posterior Column Involvement
about
Muscle atrophy and motor neuron degeneration in human NEDL1 transgenic miceHDAC6 regulates mutant SOD1 aggregation through two SMIR motifs and tubulin acetylationFrom animal models to human disease: a genetic approach for personalized medicine in ALSRedox regulation in amyotrophic lateral sclerosisLate onset of motor neurons in mice overexpressing wild-type peripherinAn in vitro model for Lewy body-like hyaline inclusion/astrocytic hyaline inclusion: induction by ER stress with an ALS-linked SOD1 mutationSpinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS.Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Colocalization of 14-3-3 proteins with SOD1 in Lewy body-like hyaline inclusions in familial amyotrophic lateral sclerosis cases and the animal modelEffects of natural antioxidants in neurodegenerative disease.Pathological aspects of lipid peroxidation.Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity.Cu, Zn-superoxide dismutase 1 (SOD1) is a novel target of Puromycin-sensitive aminopeptidase (PSA/NPEPPS): PSA/NPEPPS is a possible modifier of amyotrophic lateral sclerosis.Transgenic mouse model for familial amyotrophic lateral sclerosis with superoxide dismutase-1 mutation.NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1, targets mutant superoxide dismutase-1.Aggregation propensities of superoxide dismutase G93 hotspot mutants mirror ALS clinical phenotypesGamma-synuclein pathology in amyotrophic lateral sclerosisMetal-deficient SOD1 in amyotrophic lateral sclerosis.Superoxide dismutase 1 encoding mutations linked to ALS adopts a spectrum of misfolded statesEffects of Cellular Pathway Disturbances on Misfolded Superoxide Dismutase-1 in Fibroblasts Derived from ALS PatientsDeletion of the BH3-only protein puma protects motoneurons from ER stress-induced apoptosis and delays motoneuron loss in ALS miceStructural properties and neuronal toxicity of amyotrophic lateral sclerosis-associated Cu/Zn superoxide dismutase 1 aggregates.Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.A common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.The genetics and neuropathology of amyotrophic lateral sclerosis.Clinical and genetic heterogeneity of amyotrophic lateral sclerosis.Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins.The phenotypic variability of amyotrophic lateral sclerosis.A cysteine residue affects the conformational state and neuronal toxicity of mutant SOD1 in mice: relevance to the pathogenesis of ALS.Up-regulation of protein chaperones preserves viability of cells expressing toxic Cu/Zn-superoxide dismutase mutants associated with amyotrophic lateral sclerosis.Autophagy Dysregulation in ALS: When Protein Aggregates Get Out of Hand.Pathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis.Aggregate formation in Cu,Zn superoxide dismutase-related proteins.Histidinyl radical formation in the self-peroxidation reaction of bovine copper-zinc superoxide dismutase.Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability.A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.Relationship between mutant Cu/Zn superoxide dismutase 1 maturation and inclusion formation in cell models.In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants.A computational combinatorial approach identifies a protein inhibitor of superoxide dismutase 1 misfolding, aggregation, and cytotoxicity.Novel intracytoplasmic inclusions immunoreactive for phosphorylated-TDP43 and cystatin C in anterior horn cells in a case of sporadic amyotrophic lateral sclerosis.
P2860
Q21296753-133D5893-2832-4369-AC55-0FD9C0CD2584Q24338404-619DC9AA-C181-47D7-9F96-5325888253E4Q26741250-5CF9D01B-E120-459A-AC8D-9C51E6E4BBE3Q27026894-587D949E-C4BF-4FA9-986C-753F602E0977Q28513274-67C255DB-E35C-4F8D-A4CA-32A9DEC79C0CQ33302125-21D8CE0B-D6A7-4856-A8FF-C8A1E509B07AQ33719399-61D769C5-97BC-470A-B0EF-C314A3D83917Q33772493-9753F141-BA50-4B65-9320-805704C2EE67Q33927182-6E57B6F2-6CC8-4BBE-AB36-EBE05117CAD0Q34030539-7E57FFEE-2F4B-4DA7-821C-697B5C6F6964Q34137628-1D87A086-FAC0-4B60-A39C-E54DCB1AB70FQ34141572-CF125B12-C682-4762-B562-7A6280486CFFQ34183204-C18B2A4A-740C-415D-A77D-16DE512DCA77Q34220144-3E3C8C2F-BEE8-4E3F-94C4-1DB6C3ECAF10Q34284915-DF5ABF58-4178-4217-BFC9-F8B20D69DC54Q34442177-A7E6209E-224A-4707-BFD9-5254FE88F4CAQ34994452-B94C1017-B9C0-4043-AA85-F32CC4404B29Q35533798-83C40579-B786-4044-880D-9F26A4BC0E8BQ35642667-AB9BF2C3-A840-4FA0-977D-48CDDE0C3A6BQ35937181-5C8A7EA8-2A0C-4F48-AEBC-940BE46BF315Q36300133-4D6E8E00-C5D3-4532-876A-E659E4D46440Q36320449-B9F07444-64CD-4425-9FE0-CE31E83B1A49Q36512177-E4F19C7D-C668-42D5-85E4-4AB79D15B294Q37431412-F2D290F3-D9A2-49E3-BF69-1CABCA649CF2Q38035744-87B693B0-3D2F-4CC5-8792-16E7B7C7FAC1Q38078984-6B368646-E406-4E23-B886-CB7E3C9EF12AQ38166717-6D2E634E-E058-43E5-A7B9-F8FAA74FD9A1Q38259758-BDAE1176-5C43-4650-9086-FAE96648832AQ39030282-23E2C469-F2E9-4724-A300-7F5F30B5F6AEQ40975834-593783C1-E6DF-409D-905E-5AAEF45FD244Q41525479-EC36BBF7-F92D-40BF-97A8-292E7B414FD8Q41820610-E95765B8-A4DB-486D-ABA5-41D2C1413228Q42693610-33B05113-CD4F-41A0-ABEF-E78FBE73A140Q43845823-0F841913-3B9C-4EA3-BC74-3222206181DCQ45107835-0F887C05-CBE8-4B98-853E-C2031AC1FD40Q46242593-FB6EC16C-2BB1-4928-B8F9-C2C70660564BQ46537325-5DB75B92-85FE-4C1A-8E6E-02303ACDA0DAQ46809689-04F3CDFF-5101-4DFE-B3EC-81D20DBA0446Q47741777-FE83D850-7274-4603-99AF-983F51056D3AQ47857086-EDB2FF8A-C132-49AB-A982-2F1720D84ABD
P2860
Intense Superoxide Dismutase-1 Immunoreactivity in Intracytoplasmic Hyaline Inclusions of Familial Amyotrophic Lateral Sclerosis with Posterior Column Involvement
description
im April 1996 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 1996
@uk
name
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@en
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@nl
type
label
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@en
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@nl
prefLabel
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@en
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@nl
P2093
P1476
Intense Superoxide Dismutase-1 ...... h Posterior Column Involvement
@en
P2093
Asao Hirano
Han-Xiang Deng
Kohtaro Asayama
Makio Kobayashi
Noriyuki Shibata
Takeo Kato
Teepu Siddique
Wu-Yen Hung
P304
P356
10.1097/00005072-199604000-00011
P577
1996-04-01T00:00:00Z