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348 related items for PubMed ID: 33923808
1. A Metal-Free, Disulfide Oxidized Form of Superoxide Dismutase 1 as a Primary Misfolded Species with Prion-Like Properties in the Extracellular Environments Surrounding Motor Neuron-Like Cells. Takashima C, Kosuge Y, Inoue M, Ono SI, Tokuda E. Int J Mol Sci; 2021 Apr 16; 22(8):. PubMed ID: 33923808 [Abstract] [Full Text] [Related]
2. Intercellular Prion-Like Conversion and Transmission of Cu/Zn Superoxide Dismutase (SOD1) in Cell Culture. Grad LI, Pokrishevsky E, Cashman NR. Methods Mol Biol; 2017 Apr 16; 1658():357-367. PubMed ID: 28861801 [Abstract] [Full Text] [Related]
3. [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 Apr 16; 139(7):1015-1019. PubMed ID: 31257248 [Abstract] [Full Text] [Related]
4. TDP-43 or FUS-induced misfolded human wild-type SOD1 can propagate intercellularly in a prion-like fashion. Pokrishevsky E, Grad LI, Cashman NR. Sci Rep; 2016 Mar 01; 6():22155. PubMed ID: 26926802 [Abstract] [Full Text] [Related]
5. 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 19; 14(1):42. PubMed ID: 31744522 [Abstract] [Full Text] [Related]
6. MS785-MS27 Reactive Misfolded/Non-Native Zn-Deficient SOD1 Species Exhibit Cytotoxicity and Adopt Heterozygous Conformations in Motor Neurons. Tokuda E, Sakashita Y, Tokoro N, Date A, Kosuge Y, Miyasaka T. Int J Mol Sci; 2024 May 21; 25(11):. PubMed ID: 38891791 [Abstract] [Full Text] [Related]
7. Disease Mechanisms in ALS: Misfolded SOD1 Transferred Through Exosome-Dependent and Exosome-Independent Pathways. Silverman JM, Fernando SM, Grad LI, Hill AF, Turner BJ, Yerbury JJ, Cashman NR. Cell Mol Neurobiol; 2016 Apr 21; 36(3):377-81. PubMed ID: 26908139 [Abstract] [Full Text] [Related]
8. SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS. Hayashi Y, Homma K, Ichijo H. Adv Biol Regul; 2016 Jan 21; 60():95-104. PubMed ID: 26563614 [Abstract] [Full Text] [Related]
9. Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis. Tokuda E, Anzai I, Nomura T, Toichi K, Watanabe M, Ohara S, Watanabe S, Yamanaka K, Morisaki Y, Misawa H, Furukawa Y. Mol Neurodegener; 2017 Jan 05; 12(1):2. PubMed ID: 28057013 [Abstract] [Full Text] [Related]
10. Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Kabashi E, Valdmanis PN, Dion P, Rouleau GA. Ann Neurol; 2007 Dec 05; 62(6):553-9. PubMed ID: 18074357 [Abstract] [Full Text] [Related]
11. Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis? Furukawa Y, Tokuda E. Transl Neurodegener; 2020 Aug 19; 9(1):33. PubMed ID: 32811540 [Abstract] [Full Text] [Related]
12. Prion-like propagation of mutant SOD1 misfolding and motor neuron disease spread along neuroanatomical pathways. Ayers JI, Fromholt SE, O'Neal VM, Diamond JH, Borchelt DR. Acta Neuropathol; 2016 Jan 19; 131(1):103-14. PubMed ID: 26650262 [Abstract] [Full Text] [Related]
13. Misfolded SOD1 Accumulation and Mitochondrial Association Contribute to the Selective Vulnerability of Motor Neurons in Familial ALS: Correlation to Human Disease. Abu-Hamad S, Kahn J, Leyton-Jaimes MF, Rosenblatt J, Israelson A. ACS Chem Neurosci; 2017 Oct 18; 8(10):2225-2234. PubMed ID: 28715630 [Abstract] [Full Text] [Related]
14. Intercellular propagated misfolding of wild-type Cu/Zn superoxide dismutase occurs via exosome-dependent and -independent mechanisms. Grad LI, Yerbury JJ, Turner BJ, Guest WC, Pokrishevsky E, O'Neill MA, Yanai A, Silverman JM, Zeineddine R, Corcoran L, Kumita JR, Luheshi LM, Yousefi M, Coleman BM, Hill AF, Plotkin SS, Mackenzie IR, Cashman NR. Proc Natl Acad Sci U S A; 2014 Mar 04; 111(9):3620-5. PubMed ID: 24550511 [Abstract] [Full Text] [Related]
15. Exosome-dependent and independent mechanisms are involved in prion-like transmission of propagated Cu/Zn superoxide dismutase misfolding. Grad LI, Pokrishevsky E, Silverman JM, Cashman NR. Prion; 2014 Mar 04; 8(5):331-5. PubMed ID: 25551548 [Abstract] [Full Text] [Related]
16. A copper-deficient form of mutant Cu/Zn-superoxide dismutase as an early pathological species in amyotrophic lateral sclerosis. Tokuda E, Nomura T, Ohara S, Watanabe S, Yamanaka K, Morisaki Y, Misawa H, Furukawa Y. Biochim Biophys Acta Mol Basis Dis; 2018 Jun 04; 1864(6 Pt A):2119-2130. PubMed ID: 29551730 [Abstract] [Full Text] [Related]
17. 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 04; 26(3):484-496. PubMed ID: 27977888 [Abstract] [Full Text] [Related]
18. 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 04; 70(21):4181-95. PubMed ID: 23765103 [Abstract] [Full Text] [Related]
19. Tryptophan 32 mediates SOD1 toxicity in a in vivo motor neuron model of ALS and is a promising target for small molecule therapeutics. DuVal MG, Hinge VK, Snyder N, Kanyo R, Bratvold J, Pokrishevsky E, Cashman NR, Blinov N, Kovalenko A, Allison WT. Neurobiol Dis; 2019 Apr 04; 124():297-310. PubMed ID: 30528257 [Abstract] [Full Text] [Related]
20. A hyperthermophilic protein G variant engineered via directed evolution prevents the formation of toxic SOD1 oligomers. Dagan B, Oren O, Banerjee V, Taube R, Papo N. Proteins; 2019 Sep 04; 87(9):738-747. PubMed ID: 31017342 [Abstract] [Full Text] [Related] Page: [Next] [New Search]