Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis. - Wikidata - awgldk - TriplyDB

Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.

Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.

http://www.wikidata.org/entity/Q33559556

about

Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosis A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme Ligand binding and aggregation of pathogenic SOD1 Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS Solid-state NMR studies of metal-free SOD1 fibrillar structures.Cutting off functional loops from homodimeric enzyme superoxide dismutase 1 (SOD1) leaves monomeric β-barrels.Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Lipid-associated aggregate formation of superoxide dismutase-1 is initiated by membrane-targeting loops.Protease-resistant SOD1 aggregates in amyotrophic lateral sclerosis demonstrated by paraffin-embedded tissue (PET) blot.Dysregulation of the proteasome increases the toxicity of ALS-linked mutant SOD1.Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis Structural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mapping Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.SOD1 aggregation in ALS mice shows simplistic test tube behavior.Kinetically competing huntingtin aggregation pathways control amyloid polymorphism and properties Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.Intrinsically semi-disordered state and its role in induced folding and protein aggregation Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis.Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases.A seeded propagation of Cu, Zn-superoxide dismutase aggregates in amyotrophic lateral sclerosis.Extracellular wildtype and mutant SOD1 induces ER-Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells.Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions.Pathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis.Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties.Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates.Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis.Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study.Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling.Cholesterol secosterol aldehyde adduction and aggregation of Cu,Zn-superoxide dismutase: Potential implications in ALS

P2860

Q24297625-A2DF79F8-C4D0-4C83-B842-5DACFDD3E4DB Q24632492-8CBE4E87-EA6D-41BF-BB8D-AA3E787C57CE Q27670773-8ECAF0FE-D10E-435C-94EB-2B469CF4D133 Q27677527-CCD56B10-7595-4DEB-8D86-52A76F8CECC8 Q27680903-51E828DF-60AC-4B62-986E-A799E0C13EDD Q30153414-04512DF9-FACA-4A6C-BABE-1310A9EEB7C9 Q30155526-7D3684A5-544A-47DF-8427-69860F90ADB5 Q30359467-CD20BBF9-E8C4-4838-8812-B118D50EBE90 Q30850744-41D8B0AD-7DBC-42C4-AE3A-88AF21598244 Q34143918-34126AC4-EC20-487E-B315-F2802A260DB5 Q34391529-FC245767-C344-45B2-A8EB-135C7FF96C04 Q34438898-8F8FC353-956A-4834-80E1-CAC5FDFD2770 Q35377964-0BE042E2-69D7-4A4C-8F47-CD1FC1CF88B8 Q35763674-F09A843E-DDCE-4F32-8D2C-C34CA8B4DE52 Q35873804-7CAF2BC4-D5EA-4C9F-A74F-1F452E021CB6 Q35961208-D76E546A-09DE-45CE-91E8-932ED40293A3 Q36088674-7C50C6CE-4991-4113-A45A-1C156F9E54D4 Q36398045-0A8DC6F1-7407-4510-98B0-390D6F9467A3 Q36991027-3C5F0367-8A47-41A7-817C-8C2B8FD39DBF Q37337624-34321B21-047D-4073-AFDA-68BE5DB66012 Q37563994-1401FC81-D4EE-40B2-9EB1-FC559F8FCAC4 Q38185934-2F03540E-C29F-4248-81B8-7FAF6C15348C Q38199669-574D9845-E91F-4EBB-B341-713179C3AE9C Q39139898-102BB279-1DC6-4658-852C-30723832AA1C Q40594112-9FD2CDF8-780B-4A8F-B44C-35C24B16949A Q41820610-C7DB8F0E-7B8C-4011-B362-307F7E78B07F Q41836559-F868E8CA-DFCB-4E49-B0E3-1D2C0B8A6CB3 Q42519015-C4C55181-1F21-4366-83CC-F4BCAAACAB0F Q43244834-FE0EC6E8-DF4D-4126-9538-B778471DEABD Q46791114-07221F66-5C65-4999-89FF-3B1E2C6FCE26 Q46851121-832A83D7-2801-48AB-B724-F9D9245863EB Q47985099-85C5ECE3-1999-4D30-8023-4201D7102E30 Q50069615-959D9622-B8A1-487D-9924-0E7DE7FC4DCA Q58773578-B6C4CB8E-20B4-4C25-8964-91C29CACC707

P2860

Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.

http://www.wikidata.org/entity/Q33559556

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

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

name

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@ast

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@en

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@nl

type

label

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@ast

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@en

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@nl

prefLabel

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@ast

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@en

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@nl

P1433

Q33559556-BD9AE029-C592-4B92-AA98-AD261322D6E2

P1476

Q33559556-3EDAF817-7E29-4A35-8430-A031226B8B6C

P2093

Q33559556-362D68F7-A835-416B-BAFE-67C23299DE16

Q33559556-5761ECD2-58DB-4BAA-B6A3-93762082F331

P2860

Q33559556-0382E83B-4313-4C27-A5AB-6A1D62D4BB4B

Q33559556-076B4055-B4CE-4C09-86AB-92EF3C1D5A09

Q33559556-0FB1181F-5331-4671-8976-42BABF28CDC3

Q33559556-1372E4DF-A549-44C5-BB37-B4FC14142D8C

Q33559556-22E6F505-178F-44E2-8DF2-90B24FDC8010

Q33559556-238FA9F3-1010-4904-8C83-EB30AAC1C9EE

Q33559556-317AB66B-FAFF-4D86-9884-23C5770DB6D8

Q33559556-47E1FE10-9AD4-4406-8437-0ECB8E62B01A

Q33559556-4C0BC5B5-6689-402D-8ACA-467356E54668

Q33559556-56EB70B6-9C44-4BA4-A49F-95390DDBC2F3

P304

Q33559556-D946956C-B422-4CAF-93C1-9A873FE11109

P31

Q33559556-6E68376B-B09F-4A8B-948D-8D2D9CD8910A

P356

Q33559556-4B67B0A4-71AC-4D88-A3AB-6370A0B634FF

P407

Q33559556-A913454B-FBD5-4C94-BB27-C8C45792ACB1

P433

Q33559556-88D4BF12-777A-420D-8B3C-7793A96A9B4D

P478

Q33559556-FB8345F1-7C53-43CC-AC10-9D5E6669B8B2

P50

Q33559556-88DDA116-2D6B-48E7-94FC-D61D77655EEA

Q33559556-D1A6BBF7-5959-49B2-83A0-2112395AB7FB

P577

Q33559556-A945E7A2-118B-49F2-B3DE-E4DD6410C91E

P698

Q33559556-6070AC9B-5D7F-4D83-A819-ABA81A530C46

P921

Q33559556-4566EA33-C4C8-4C85-B3EF-CD005395CA99

P932

Q33559556-7D6CE153-0D52-488F-B898-C41E6979F2DF

P356

JBC.M110.113597

P1433

Journal of Biological Chemistry

P1476

Mutation-dependent polymorphis ...... amyotrophic lateral sclerosis.

@en

P2093

Kumi Kaneko

http://www.w3.org/2001/XMLSchema#string

Nobuyuki Nukina

http://www.w3.org/2001/XMLSchema#string

P2860

Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity

Protein misfolding, functional amyloid, and human disease

Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis

Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury

Motor neuron degeneration in mice that express a human Cu,Zn superoxide dismutase mutation

Unraveling the mechanisms involved in motor neuron degeneration in ALS

Onset and progression in inherited ALS determined by motor neurons and microglia

Neurodegenerative tauopathies

P304

22221-22231

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M110.113597

http://www.w3.org/2001/XMLSchema#string

P407

P433

29

http://www.w3.org/2001/XMLSchema#string

P478

285

http://www.w3.org/2001/XMLSchema#string

P50

Yoshiaki Furukawa

P577

2010-04-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

20404329

http://www.w3.org/2001/XMLSchema#string

P921

amyotrophic lateral sclerosis

P932

2903422

http://www.w3.org/2001/XMLSchema#string