212 related articles for article (PubMed ID: 19828437)
1. Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.
Teilum K; Smith MH; Schulz E; Christensen LC; Solomentsev G; Oliveberg M; Akke M
Proc Natl Acad Sci U S A; 2009 Oct; 106(43):18273-8. PubMed ID: 19828437
[TBL] [Abstract][Full Text] [Related]
2. Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V.
Schmidlin T; Kennedy BK; Daggett V
Biophys J; 2009 Sep; 97(6):1709-18. PubMed ID: 19751676
[TBL] [Abstract][Full Text] [Related]
3. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.
Kayatekin C; Zitzewitz JA; Matthews CR
J Mol Biol; 2010 Apr; 398(2):320-31. PubMed ID: 20184893
[TBL] [Abstract][Full Text] [Related]
4. The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.
Chattopadhyay M; Nwadibia E; Strong CD; Gralla EB; Valentine JS; Whitelegge JP
J Biol Chem; 2015 Dec; 290(51):30624-36. PubMed ID: 26511321
[TBL] [Abstract][Full Text] [Related]
5. Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.
Furukawa Y; Anzai I; Akiyama S; Imai M; Cruz FJ; Saio T; Nagasawa K; Nomura T; Ishimori K
J Biol Chem; 2016 Feb; 291(8):4144-55. PubMed ID: 26694608
[TBL] [Abstract][Full Text] [Related]
6. Disulfide scrambling in superoxide dismutase 1 reduces its cytotoxic effect in cultured cells and promotes protein aggregation.
Leinartaitė L; Johansson AS
PLoS One; 2013; 8(10):e78060. PubMed ID: 24143259
[TBL] [Abstract][Full Text] [Related]
7. Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1.
Banci L; Bertini I; D'Amelio N; Libralesso E; Turano P; Valentine JS
Biochemistry; 2007 Sep; 46(35):9953-62. PubMed ID: 17683122
[TBL] [Abstract][Full Text] [Related]
8. Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.
Strange RW; Yong CW; Smith W; Hasnain SS
Proc Natl Acad Sci U S A; 2007 Jun; 104(24):10040-4. PubMed ID: 17548825
[TBL] [Abstract][Full Text] [Related]
9. Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation.
Cohen NR; Zitzewitz JA; Bilsel O; Matthews CR
J Biol Chem; 2019 Sep; 294(37):13708-13717. PubMed ID: 31341015
[TBL] [Abstract][Full Text] [Related]
10. A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.
Anzai I; Tokuda E; Mukaiyama A; Akiyama S; Endo F; Yamanaka K; Misawa H; Furukawa Y
Protein Sci; 2017 Mar; 26(3):484-496. PubMed ID: 27977888
[TBL] [Abstract][Full Text] [Related]
11. Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.
Sekhar A; Rumfeldt JA; Broom HR; Doyle CM; Bouvignies G; Meiering EM; Kay LE
Elife; 2015 Jun; 4():e07296. PubMed ID: 26099300
[TBL] [Abstract][Full Text] [Related]
12. SOD1 exhibits allosteric frustration to facilitate metal binding affinity.
Das A; Plotkin SS
Proc Natl Acad Sci U S A; 2013 Mar; 110(10):3871-6. PubMed ID: 23431152
[TBL] [Abstract][Full Text] [Related]
13. Mechanical probes of SOD1 predict systematic trends in metal and dimer affinity of ALS-associated mutants.
Das A; Plotkin SS
J Mol Biol; 2013 Mar; 425(5):850-74. PubMed ID: 23291526
[TBL] [Abstract][Full Text] [Related]
14. Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.
Kitamura F; Fujimaki N; Okita W; Hiramatsu H; Takeuchi H
Biochemistry; 2011 May; 50(20):4242-50. PubMed ID: 21506602
[TBL] [Abstract][Full Text] [Related]
15. Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.
Furukawa Y; O'Halloran TV
J Biol Chem; 2005 Apr; 280(17):17266-74. PubMed ID: 15691826
[TBL] [Abstract][Full Text] [Related]
16. Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants.
Banci L; Bertini I; Boca M; Calderone V; Cantini F; Girotto S; Vieru M
Proc Natl Acad Sci U S A; 2009 Apr; 106(17):6980-5. PubMed ID: 19369197
[TBL] [Abstract][Full Text] [Related]
17. Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.
Leal SS; Cristóvão JS; Biesemeier A; Cardoso I; Gomes CM
Metallomics; 2015 Feb; 7(2):333-46. PubMed ID: 25554447
[TBL] [Abstract][Full Text] [Related]
18. Dimerization, oligomerization, and aggregation of human amyotrophic lateral sclerosis copper/zinc superoxide dismutase 1 protein mutant forms in live cells.
Kim J; Lee H; Lee JH; Kwon DY; Genovesio A; Fenistein D; Ogier A; Brondani V; Grailhe R
J Biol Chem; 2014 May; 289(21):15094-103. PubMed ID: 24692554
[TBL] [Abstract][Full Text] [Related]
19. Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1.
Broom HR; Rumfeldt JA; Vassall KA; Meiering EM
Protein Sci; 2015 Dec; 24(12):2081-9. PubMed ID: 26362407
[TBL] [Abstract][Full Text] [Related]
20. Oxidative misfolding of Cu/Zn-superoxide dismutase triggered by non-canonical intramolecular disulfide formation.
Anzai I; Tokuda E; Handa S; Misawa H; Akiyama S; Furukawa Y
Free Radic Biol Med; 2020 Feb; 147():187-199. PubMed ID: 31863908
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]