Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers - Wikidata - wikimedia - TriplyDB

Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers

Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers

http://www.wikidata.org/entity/Q37619322

about

Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis Dissecting toxin immunity in virus-infected killer yeast uncovers an intrinsic strategy of self-protection Structural Characterization of Zinc-deficient Human Superoxide Dismutase and Implications for ALS Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48Q †Functional features cause misfolding of the ALS-provoking enzyme SOD1 Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A Characterization of a Covalent Polysulfane Bridge in Copper−Zinc Superoxide Dismutase,Disrupted Zinc-Binding Sites in Structures of Pathogenic SOD1 Variants D124V and H80R Global structural motions from the strain of a single hydrogen bond Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase The complex molecular biology of amyotrophic lateral sclerosis (ALS)Dose response relationship in anti-stress gene regulatory networks RNA-binding protein is involved in aggregation of light neurofilament protein and is implicated in the pathogenesis of motor neuron degeneration 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.Structural and thermodynamic effects of post-translational modifications in mutant and wild type Cu, Zn superoxide dismutase.Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.Local unfolding in a destabilized, pathogenic variant of superoxide dismutase 1 observed with H/D exchange and mass spectrometry.Disulfide bond as a switch for copper-zinc superoxide dismutase activity in asthma.Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS.3D complex: a structural classification of protein complexes Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species A systems biology perspective on Nrf2-mediated antioxidant response A role for copper in the toxicity of zinc-deficient superoxide dismutase to motor neurons in amyotrophic lateral sclerosis Aggregation of copper-zinc superoxide dismutase in familial and sporadic ALS Immature copper-zinc superoxide dismutase and familial amyotrophic lateral sclerosis.Physicochemical code for quinary protein interactions in Escherichia coli.Systematically perturbed folding patterns of amyotrophic lateral sclerosis (ALS)-associated SOD1 mutants Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation.Exposure of hydrophobic surfaces initiates aggregation of diverse ALS-causing superoxide dismutase-1 mutants.Performance analysis of orthogonal pairs designed for an expanded eukaryotic genetic code.Cu,Zn-superoxide dismutase increases toxicity of mutant and zinc-deficient superoxide dismutase by enhancing protein stability.Cytotoxicity of superoxide dismutase 1 in cultured cells is linked to Zn2+ chelation.Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: parallels to precursors in amyloid disease Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation

P2860

Q24544265-8F19E96D-517D-4336-9398-55F265A5A1FD Q24644037-31F52DDE-C214-49F2-B38F-9379EAB096E5 Q24682066-0C7EC4D9-34F4-4E06-9B01-D099B67B9580 Q27648424-0DA7442F-DF86-42D5-BB7F-BE32C6BA4587 Q27653849-0E081465-65D0-45F4-BA9D-03078E6DB42F Q27655747-A74182D3-C5E3-48E1-A2EF-FB7A0B459D7C Q27657645-E4E24779-5FCB-485A-A406-A76D6AA61B74 Q27658869-4EC31B87-B861-463F-A74B-FE1426B6FEBD Q27662078-651515FD-051F-4695-946F-C14A4A6D6C47 Q27676522-14C8A0D1-382D-48D8-9325-0D24DCC3EA2C Q28252386-1B897EC4-26BB-4F94-8FE1-87C0CEF6DB92 Q28263899-E78C8769-99E1-4C26-9843-E6E31E6076F7 Q28469152-8AE53AC3-C110-4B14-8C53-23595A92D837 Q28595098-1D89CE7A-8AE1-4950-937E-1E34905678C9 Q30153414-D0A3D03C-C323-404E-85E4-E4599FC1C5C9 Q30155526-C72E55EA-9891-4CB7-A4C8-0E5358D20111 Q30155624-C12B5138-204B-4E72-8319-2CF11B8404FB Q30157502-802844A1-5D54-43AB-A477-E8DEC62925C1 Q30159679-AA3204CC-084C-466F-A2A6-DB1B5A16B4D5 Q30159818-571F1621-371F-4CF8-8DF1-118673F46F6C Q30420089-647B96E9-0DF6-4557-AF1E-0ADCAC7F13A7 Q30497215-A43F4B2B-FD17-460A-B580-995518624C98 Q33263952-69214E0A-7E08-468D-8C28-43744D8631ED Q33423010-24C80FBF-6142-4458-9715-5E58FB9DF9EA Q33559671-F780BD8F-D46A-4D98-B0EE-A5DD71BE3A2F Q33724409-A6CA3347-9337-4A4A-A0F2-961BE9E9D267 Q33742705-171C8921-D342-46F4-AB83-34374D5CECC1 Q33742742-2F178004-D5AC-4763-A08B-282FFAB108DA Q33772493-518282B4-A4D6-4646-AC30-F23D9746A477 Q33790747-9AA392FE-772D-4ED3-8514-87418C6FED4D Q33895940-08C00AA3-27D3-44E5-96D9-17E72277176F Q33928500-2EFE44ED-9E25-467D-8226-C2110C5D492D Q34082710-8CC90770-D608-481C-B7BD-391421F58EBE Q34228226-AABE5910-84DC-4CB4-A270-F938AEE7C402 Q34232041-55E0922E-102C-46A9-971C-0E8BE8822908 Q34257147-87FEC688-26F8-4F60-B97D-9017B2DF4047 Q34572921-03359645-9049-41E5-B218-DE9882907623 Q34771957-9A4074B3-1DFC-4CC8-94FD-1CE0A4696F85 Q34788369-44A4C03E-5DB7-4D0D-8676-869F0FA838EF Q35021849-807A065B-4EC3-4B94-84B2-FED86BF70FF4

P2860

Folding of human superoxide dismutase: disulfide reduction prevents dimerization and produces marginally stable monomers

http://www.wikidata.org/entity/Q37619322

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh

2004年學術文章

@zh-hant

name

Folding of human superoxide di ...... ces marginally stable monomers

@en

Folding of human superoxide di ...... es marginally stable monomers.

@nl

type

label

Folding of human superoxide di ...... ces marginally stable monomers

@en

Folding of human superoxide di ...... es marginally stable monomers.

@nl

prefLabel

Folding of human superoxide di ...... ces marginally stable monomers

@en

Folding of human superoxide di ...... es marginally stable monomers.

@nl

P1433

Q37619322-DD79B13A-540D-43D7-95F6-977D5CA955B7

P1476

Q37619322-E90E6AF7-D004-4588-80A0-79A535312F9E

P2093

Q37619322-73605ABA-800A-4056-AFF8-CC3BEBFD4C4C

Q37619322-AE0BBEE0-92D3-4FA2-84F5-56BE86A6F258

Q37619322-C317F8B2-3C88-4B8C-92F1-4D37D5BAC7A7

Q37619322-E7CE4252-26F1-467B-9CA0-3282F8D8031D

P2860

Q37619322-03EA2555-89EB-4822-94BE-1465F09EDD59

Q37619322-0A051FAB-D09A-46F9-BF8A-AFF74A460DAA

Q37619322-0ED009BE-4D44-4F04-8E50-CAEFCDA7F77E

Q37619322-14B495DE-2BA6-40CF-8DB5-4BFEF9B98A38

Q37619322-1EC2B260-BB07-4770-BF87-094D3AB86EEB

Q37619322-1FC89147-9A1A-496C-97D4-35397E26E2D6

Q37619322-23942E0C-D89B-40EF-861E-FDACE10EEDE4

Q37619322-27868D78-5DE9-4FB2-A2E0-93A03675B631

Q37619322-316EE95D-AD05-4A1B-88F7-E2EB3631EB92

Q37619322-341569DC-B241-4331-A4AC-BE67FBDA6F8F

P304

Q37619322-7FC31693-23FE-4759-B30B-D3FB37C645F7

P31

Q37619322-A8BDA5AA-935A-43D2-A44D-6D8519D5A5B2

P356

Q37619322-582CB3AB-30AD-470C-A703-F4F431334190

P407

Q37619322-50EDB0B8-C238-49FF-8557-A9FCCB9F12A3

P433

Q37619322-7A63A306-CF11-421E-80EA-ECDD44AA687F

P478

Q37619322-6F14A284-20BD-4AB6-89FD-2E8960F55175

P577

Q37619322-6026C18A-D54C-45E9-BB29-A30B3876E5C5

P5875

Q37619322-42E69FEF-014E-42BF-B446-4CAF9730C561

P698

Q37619322-B6F8BEAF-678E-46DC-BBFD-57858F082155

P932

Q37619322-FE4048A8-212B-4856-A380-6B5C0C8CCB56

P356

PNAS.0403979101

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Folding of human superoxide di ...... ces marginally stable monomers

@en

P2093

Arne Holmgren

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

Johanna Normark

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

Mikael J Lindberg

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

Mikael Oliveberg

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

P2860

Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1

Misfolded CuZnSOD and amyotrophic lateral sclerosis

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

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease

ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization

Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase

Origin of unusual phi-values in protein folding: evidence against specific nucleation sites

Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding

Protein folding and misfolding

P304

15893-15898

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

P31

scholarly article

P356

10.1073/PNAS.0403979101

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

P407

P433

45

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

P478

101

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

P577

2004-11-02T00:00:00Z

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

P5875

8197585

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

P698

15522970

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

P932

528748

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