Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase - Wikidata - wikimedia - TriplyDB

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

http://www.wikidata.org/entity/Q28252386

about

Oxygen-dependent activation of Cu,Zn-superoxide dismutase-1.Relationship between mutant Cu/Zn superoxide dismutase 1 maturation and inclusion formation in cell models.Computational investigation of the human SOD1 mutant, Cys146Arg, that directs familial amyotrophic lateral sclerosis.Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations.CNS inflammation and neurodegeneration.

P2860

Q39420851-C1A58299-0716-47DF-871B-6443AEA7A1FF Q46537325-D495E876-3274-48CA-B971-86A5F0CEF172 Q48059574-28C7B4E9-4D0B-4684-A7D0-89500837C1DA Q49907306-24081EC5-41C3-43C6-A512-3A461904EE33 Q50223200-D65F4F3B-A0E6-4E78-9268-432CAC9769DC

P2860

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

http://www.wikidata.org/entity/Q28252386

description

2015 nî lūn-bûn

@nan

2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@ast

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@en

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@nl

type

label

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@ast

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@en

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@nl

prefLabel

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@ast

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@en

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@nl

P1433

Q28252386-785A1541-2C15-41D0-A093-E72795A7BACA

P1476

Q28252386-80B4CB78-E65A-4D20-B01E-6094BA7A85A3

P2093

Q28252386-0D28996F-486F-4DC4-AB7F-8D4FB6DCD0B5

Q28252386-1B267BFC-0D3A-4E0D-835D-2B77FBC1CA67

Q28252386-3B890269-430A-45BD-AD38-BD17A44C7210

Q28252386-4C83C4ED-A9DB-4F1E-BCE0-3DF8F404BA53

Q28252386-869DB5CD-73A8-4E8C-AA4F-9F7F3286CA1F

Q28252386-AEC5D08D-8EFF-425C-9F4D-A398520B7079

Q28252386-AFC4C771-A230-4E4F-AC74-D91E40B55BAC

Q28252386-B858C3E6-C525-41DA-ACAA-D99F5403652E

Q28252386-BEA1E4EF-42A0-43F0-B3CC-323800324B63

Q28252386-CC6CC6AB-C8EC-4EB6-8328-096F8C5A9CE0

P2860

Q28252386-00E1437C-93BA-4BDE-85E5-7E41FCE82B6F

Q28252386-07DDE302-01A1-404C-8B28-A7DC52F97AF7

Q28252386-0BF56E71-094B-41F9-88B6-79A454D03B8E

Q28252386-0EB60350-885B-41E4-BAD2-EBC41CE75370

Q28252386-14F770B6-EAA6-4C50-B176-94B7A6126035

Q28252386-15877C35-0067-4F00-ABA1-1596BFE9872B

Q28252386-17C122A0-7978-4EF0-999B-4AEE085B3A78

Q28252386-1B897EC4-26BB-4F94-8FE1-87C0CEF6DB92

Q28252386-1BFD5414-F8D4-4E9A-8FA3-EC44814E6608

Q28252386-1DF4C065-B32C-489C-832E-6E5EE57DA12A

P304

Q28252386-5F29559F-6698-4509-A202-756FD5C64337

P31

Q28252386-C7505B89-241F-4B65-BB4C-B42FA7CED05B

P356

Q28252386-43718EF4-C28A-4760-AB33-9E537B045208

P407

Q28252386-B26C3903-CC7E-431F-8A40-B02DE4DDEFBC

P433

Q28252386-DA3D3FCF-4688-4269-A3A8-82D2EF283206

P478

Q28252386-66EAE8FB-D679-4155-B5AD-0C0DAE0D8A4A

P577

Q28252386-2EEA1C2A-1F05-40B1-B3C6-18B9617F31FD

P698

Q28252386-20F753DF-5B9F-4642-BE3D-0CF0A13F9ACA

P921

Q28252386-A4E039AB-AF52-4610-90D4-01148B089BF5

P932

Q28252386-50371947-4B3B-4054-B8D2-B0A6BE9B45B2

P356

JBC.M114.588798

P1433

Journal of Biological Chemistry

P1476

Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase

@en

P2093

Alexander B Taylor

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

Armando Durazo

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

Bryan F Shaw

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

Diane E Cabelli

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

Edith Butler Gralla

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

Joan Selverstone Valentine

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

Kevin Sea

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

Lisa J Whitson

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

P John Hart

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

Se Hui Sohn

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

P2860

Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein

The copper chaperone for superoxide dismutase

The Protein Data Bank

Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice

PHENIX: a comprehensive Python-based system for macromolecular structure solution

The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited

Heterodimeric structure of superoxide dismutase in complex with its metallochaperone

An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate

The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis

Coot: model-building tools for molecular graphics

P304

2405-18

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

P31

scholarly article

P356

10.1074/JBC.M114.588798

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

P407

P433

4

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

P478

290

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

P577

2015-01-23T00:00:00Z

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

P698

25433341

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

P921

P932

4303690

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