1305 related articles for article (PubMed ID: 23508986)
1. Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.
Mulligan VK; Chakrabartty A
Proteins; 2013 Aug; 81(8):1285-303. PubMed ID: 23508986
[TBL] [Abstract][Full Text] [Related]
2. Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis.
Broom HR; Rumfeldt JA; Meiering EM
Essays Biochem; 2014; 56():149-65. PubMed ID: 25131593
[TBL] [Abstract][Full Text] [Related]
3. SOD1 aggregation and ALS: role of metallation states and disulfide status.
Sheng Y; Chattopadhyay M; Whitelegge J; Valentine JS
Curr Top Med Chem; 2012; 12(22):2560-72. PubMed ID: 23339308
[TBL] [Abstract][Full Text] [Related]
4. From molecule to molecule and cell to cell: prion-like mechanisms in amyotrophic lateral sclerosis.
Grad LI; Fernando SM; Cashman NR
Neurobiol Dis; 2015 May; 77():257-65. PubMed ID: 25701498
[TBL] [Abstract][Full Text] [Related]
5. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form.
Kerman A; Liu HN; Croul S; Bilbao J; Rogaeva E; Zinman L; Robertson J; Chakrabartty A
Acta Neuropathol; 2010 Mar; 119(3):335-44. PubMed ID: 20111867
[TBL] [Abstract][Full Text] [Related]
6. The prion-like nature of amyotrophic lateral sclerosis.
McAlary L; Yerbury JJ; Cashman NR
Prog Mol Biol Transl Sci; 2020; 175():261-296. PubMed ID: 32958236
[TBL] [Abstract][Full Text] [Related]
7. Genotype-property patient-phenotype relations suggest that proteome exhaustion can cause amyotrophic lateral sclerosis.
Kepp KP
PLoS One; 2015; 10(3):e0118649. PubMed ID: 25798606
[TBL] [Abstract][Full Text] [Related]
8. Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS.
Mulligan VK; Kerman A; Laister RC; Sharda PR; Arslan PE; Chakrabartty A
J Mol Biol; 2012 Aug; 421(4-5):631-52. PubMed ID: 22542526
[TBL] [Abstract][Full Text] [Related]
9. Superoxide Dismutase 1 Folding Stability as a Target for Molecular Tweezers in SOD1-Related Amyotrophic Lateral Sclerosis.
Samanta N; Ruiz-Blanco YB; Fetahaj Z; Gnutt D; Lantz C; Loo JA; Sanchez-Garcia E; Ebbinghaus S
Chembiochem; 2022 Nov; 23(21):e202200396. PubMed ID: 36083789
[TBL] [Abstract][Full Text] [Related]
10. A role of small heat shock protein B8 (HspB8) in the autophagic removal of misfolded proteins responsible for neurodegenerative diseases.
Crippa V; Carra S; Rusmini P; Sau D; Bolzoni E; Bendotti C; De Biasi S; Poletti A
Autophagy; 2010 Oct; 6(7):958-60. PubMed ID: 20699640
[TBL] [Abstract][Full Text] [Related]
11. Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells.
Oh YK; Shin KS; Yuan J; Kang SJ
J Neurochem; 2008 Feb; 104(4):993-1005. PubMed ID: 18233996
[TBL] [Abstract][Full Text] [Related]
12. [Prion-like Properties of Misfolded Cu/Zn-superoxide Dismutase in Amyotrophic Lateral Sclerosis: Update and Perspectives].
Tokuda E; Marklund SL; Furukawa Y
Yakugaku Zasshi; 2019; 139(7):1015-1019. PubMed ID: 31257248
[TBL] [Abstract][Full Text] [Related]
13. Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis.
Khare SD; Ding F; Dokholyan NV
J Mol Biol; 2003 Nov; 334(3):515-25. PubMed ID: 14623191
[TBL] [Abstract][Full Text] [Related]
14. [SOD1 gene mutations in patients with amyotrophic lateral sclerosis: potential for the method of molecular].
Lysogorskaia EV; Rossokhin AV; Abramycheva NIu; Zakharova MN; Illarioshkin SN
Mol Biol (Mosk); 2013; 47(5):861-7. PubMed ID: 25509359
[TBL] [Abstract][Full Text] [Related]
15. SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS.
Hayashi Y; Homma K; Ichijo H
Adv Biol Regul; 2016 Jan; 60():95-104. PubMed ID: 26563614
[TBL] [Abstract][Full Text] [Related]
16. Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis.
Tokuda E; Takei YI; Ohara S; Fujiwara N; Hozumi I; Furukawa Y
Mol Neurodegener; 2019 Nov; 14(1):42. PubMed ID: 31744522
[TBL] [Abstract][Full Text] [Related]
17. Extracellular wildtype and mutant SOD1 induces ER-Golgi pathology characteristic of amyotrophic lateral sclerosis in neuronal cells.
Sundaramoorthy V; Walker AK; Yerbury J; Soo KY; Farg MA; Hoang V; Zeineddine R; Spencer D; Atkin JD
Cell Mol Life Sci; 2013 Nov; 70(21):4181-95. PubMed ID: 23765103
[TBL] [Abstract][Full Text] [Related]
18. ALS-causing SOD1 mutations promote production of copper-deficient misfolded species.
Ip P; Mulligan VK; Chakrabartty A
J Mol Biol; 2011 Jun; 409(5):839-52. PubMed ID: 21549128
[TBL] [Abstract][Full Text] [Related]
19. Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis?
Furukawa Y; Tokuda E
Transl Neurodegener; 2020 Aug; 9(1):33. PubMed ID: 32811540
[TBL] [Abstract][Full Text] [Related]
20. Effects of Cellular Pathway Disturbances on Misfolded Superoxide Dismutase-1 in Fibroblasts Derived from ALS Patients.
Keskin I; Forsgren E; Lange DJ; Weber M; Birve A; Synofzik M; Gilthorpe JD; Andersen PM; Marklund SL
PLoS One; 2016; 11(2):e0150133. PubMed ID: 26919046
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
