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The Ile35 Residue of the ALS-Associated Mutant SOD1 Plays a Crucial Role in the Intracellular Aggregation of the Molecule.

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Title: The Ile35 Residue of the ALS-Associated Mutant SOD1 Plays a Crucial Role in the Intracellular Aggregation of the Molecule.
Authors: Asai Y; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan., Yano K; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan., Higashino T; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan., Yoshihara D; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.; Labolatory of Biochemistry, School of Pharmacy, Hyogo Medical University, Kobe, Hyogo, 650-8530, Japan., Sakiyama H; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.; Faculty of Nutrition, Department of Food and Nutrition, Senri Kinran University, Suita, Osaka, 565-0873, Japan., Eguchi H; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan., Fukushima K; Department of Chemistry, School of Medicine, Hyogo Medical University, Nishinomiya, Hyogo, 663-8501, Japan., Suzuki K; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan., Fujiwara N; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan. noriko-f@hyo-med.ac.jp.
Source: Molecular neurobiology [Mol Neurobiol] 2025 Feb; Vol. 62 (2), pp. 2023-2038. Date of Electronic Publication: 2024 Jul 26.
Publication Type: Journal Article
Language: English
Journal Info: Publisher: Humana Press Country of Publication: United States NLM ID: 8900963 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1559-1182 (Electronic) Linking ISSN: 08937648 NLM ISO Abbreviation: Mol Neurobiol Subsets: MEDLINE
Imprint Name(s): Original Publication: Clifton, NJ : Humana Press, c1987-
MeSH Terms: Amyotrophic Lateral Sclerosis*/genetics , Amyotrophic Lateral Sclerosis*/enzymology , Amyotrophic Lateral Sclerosis*/pathology , Mutation*/genetics , Superoxide Dismutase*/genetics , Superoxide Dismutase*/metabolism , Superoxide Dismutase*/chemistry , Intracellular Space*/metabolism , Mutant Proteins*/metabolism , Mutant Proteins*/chemistry , Protein Aggregates* , Protein Aggregation, Pathological*, Green Fluorescent Proteins/metabolism ; Superoxide Dismutase-1 ; Humans ; Animals
Abstract: Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease with an unknown pathogenesis. It has been reported that mutations in the gene for Cu/Zn superoxide dismutase (SOD1) cause familial ALS. Mutant SOD1 undergoes aggregation and forms amyloid more easily, and SOD1-immunopositive inclusions have been observed in the spinal cords of ALS patients. Because of this, SOD1 aggregation is thought to be related to the pathogenesis of ALS. Some core regions of amyloid have been identified, but the issue of whether these regions form aggregates in living cells remains unclear, and the mechanism responsible for intracellular SOD1 aggregation also remains unclear. The findings reported in this study indicate that the aggregation of the ALS-linked mutant SOD1-EGFP was significantly enhanced when the BioID2 gene was fused to the N-terminus of the mutant SOD1-EGFP plasmid for cellular expression. Expression of a series of BioID2-(C-terminal deletion peptides of SOD1)-EGFP permitted us to identify 1-35 as a minimal N-terminal sequence and Ile35 as an essential amino acid residue that contributes to the intracellular aggregation of SOD1. The findings also showed that an additional substitution of Ile35 with Ser into the ALS mutant SOD1 resulted in the significant suppression of aggregate formation. The fact that no Ile35 mutations have been reported to date in ALS patients indicates that all ALS mutant SOD1s contain Ile35. Taken together, we propose that Ile35 plays a pivotal role in the aggregation of the ALS-linked SOD1 and that this study will contribute to our understanding of the mechanism responsible for SOD1 aggregation.
(© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Competing Interests: Declarations. Ethics Approval and Consent to Participate: Not applicable. Consent for Publication: Not applicable. Competing Interests: The authors declare no competing interests.
References: Genet Med. 2012 Sep;14(9):823-6. (PMID: 22595939)
Commun Biol. 2020 Jan 22;3(1):38. (PMID: 31969649)
Nature. 1993 Mar 4;362(6415):59-62. (PMID: 8446170)
Free Radic Res. 2016;50(11):1245-1256. (PMID: 27629432)
J Cell Biol. 2005 Oct 10;171(1):75-85. (PMID: 16216923)
Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):10934-9. (PMID: 23781106)
Proc Natl Acad Sci U S A. 2017 Aug 15;114(33):8770-8775. (PMID: 28760994)
Sci Rep. 2020 Nov 26;10(1):20738. (PMID: 33244158)
Annu Rev Cell Dev Biol. 2018 Oct 6;34:545-568. (PMID: 30044648)
J Biol Chem. 2007 Jun 1;282(22):16329-35. (PMID: 17389599)
Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8049-54. (PMID: 24843142)
Nat Neurosci. 2010 Nov;13(11):1396-403. (PMID: 20953194)
Biochim Biophys Acta. 2010 Feb;1804(2):245-62. (PMID: 19914407)
Biosci Rep. 2012 Dec;32(6):539-48. (PMID: 22804629)
Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3155-60. (PMID: 8610185)
Neurobiol Dis. 2019 Apr;124:297-310. (PMID: 30528257)
J Comp Neurol. 1998 Feb 2;391(1):64-77. (PMID: 9527542)
PLoS One. 2018 Oct 5;13(10):e0205090. (PMID: 30289953)
J Biol Chem. 2010 Jul 16;285(29):22221-31. (PMID: 20404329)
Annu Rev Neurosci. 2004;27:723-49. (PMID: 15217349)
Proc Natl Acad Sci U S A. 2011 Sep 27;108(39):16398-403. (PMID: 21930926)
Cell. 2003 Dec 12;115(6):727-38. (PMID: 14675537)
Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):197-201. (PMID: 24344300)
Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):689-93. (PMID: 7846037)
Hum Mol Genet. 2003 Apr 1;12(7):749-57. (PMID: 12651870)
J Mol Biol. 2012 Aug 24;421(4-5):491-8. (PMID: 22245492)
Nature. 2008 Aug 28;454(7208):1088-95. (PMID: 18756251)
Annu Rev Biochem. 2005;74:563-93. (PMID: 15952898)
Protein Sci. 2021 Jan;30(1):70-82. (PMID: 32881101)
Methods Mol Biol. 2019;2012:299-313. (PMID: 31161514)
J Mol Biol. 2003 Sep 19;332(3):601-15. (PMID: 12963370)
Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16607-12. (PMID: 12482932)
Nat Commun. 2022 Jun 17;13(1):3491. (PMID: 35715417)
PLoS One. 2020 Jan 30;15(1):e0227655. (PMID: 31999698)
J Biol Chem. 2005 Feb 11;280(6):5061-70. (PMID: 15522870)
Proc Natl Acad Sci U S A. 2011 Feb 8;108(6):2210-5. (PMID: 21257910)
Exp Neurol. 2017 Jun;292:154-167. (PMID: 28322742)
J Biol Chem. 2007 Dec 7;282(49):35933-44. (PMID: 17913710)
Proc Natl Acad Sci U S A. 2018 May 1;115(18):4661-4665. (PMID: 29666246)
J Biochem. 2016 Feb;159(2):247-60. (PMID: 26319711)
J Biol Chem. 2008 Jan 11;283(2):866-74. (PMID: 18006498)
J Cell Biol. 1998 Dec 28;143(7):1883-98. (PMID: 9864362)
EMBO J. 2021 May 17;40(10):e106389. (PMID: 33792056)
Sci Rep. 2018 Oct 22;8(1):15590. (PMID: 30349065)
Structure. 2016 Nov 1;24(11):1898-1906. (PMID: 27667694)
PLoS Biol. 2006 Dec;4(12):e417. (PMID: 17147470)
Grant Information: 22K11870 Japan Society for the Promotion of Science
Contributed Indexing: Keywords: Aggresomes; Amyotrophic lateral sclerosis (ALS); Cu/Zn superoxide dismutase (SOD1); Intracellular aggregation; Neurodegeneration
Substance Nomenclature: EC 1.15.1.1 (Superoxide Dismutase-1)
0 (SOD1 protein, human)
0 (Protein Aggregates)
EC 1.15.1.1 (Superoxide Dismutase)
147336-22-9 (Green Fluorescent Proteins)
0 (Mutant Proteins)
Entry Date(s): Date Created: 20240726 Date Completed: 20250423 Latest Revision: 20261010
Update Code: 20261010
DOI: 10.1007/s12035-024-04369-0
PMID: 39060907
Database: MEDLINE
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  Data: The Ile35 Residue of the ALS-Associated Mutant SOD1 Plays a Crucial Role in the Intracellular Aggregation of the Molecule.
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  Data: <searchLink fieldCode="AU" term="%22Asai+Y%22">Asai Y</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.<br /><searchLink fieldCode="AU" term="%22Yano+K%22">Yano K</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.<br /><searchLink fieldCode="AU" term="%22Higashino+T%22">Higashino T</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.<br /><searchLink fieldCode="AU" term="%22Yoshihara+D%22">Yoshihara D</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.; Labolatory of Biochemistry, School of Pharmacy, Hyogo Medical University, Kobe, Hyogo, 650-8530, Japan.<br /><searchLink fieldCode="AU" term="%22Sakiyama+H%22">Sakiyama H</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.; Faculty of Nutrition, Department of Food and Nutrition, Senri Kinran University, Suita, Osaka, 565-0873, Japan.<br /><searchLink fieldCode="AU" term="%22Eguchi+H%22">Eguchi H</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.<br /><searchLink fieldCode="AU" term="%22Fukushima+K%22">Fukushima K</searchLink>; Department of Chemistry, School of Medicine, Hyogo Medical University, Nishinomiya, Hyogo, 663-8501, Japan.<br /><searchLink fieldCode="AU" term="%22Suzuki+K%22">Suzuki K</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan.<br /><searchLink fieldCode="AU" term="%22Fujiwara+N%22">Fujiwara N</searchLink>; Department of Biochemistry, School of Medicine, Hyogo Medical University, 1-1 Mukogawa-Cho, Nishinomiya, Hyogo, 663-8501, Japan. noriko-f@hyo-med.ac.jp.
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  Data: <searchLink fieldCode="JN" term="%228900963%22">Molecular neurobiology</searchLink> [Mol Neurobiol] 2025 Feb; Vol. 62 (2), pp. 2023-2038. <i>Date of Electronic Publication: </i>2024 Jul 26.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Humana+Press%22">Humana Press </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>8900963 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1559-1182 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2208937648%22">08937648 </searchLink><i>NLM ISO Abbreviation: </i>Mol Neurobiol <i>Subsets: </i>MEDLINE
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  Data: <i>Original Publication</i>: Clifton, NJ : Humana Press, c1987-
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  Data: <searchLink fieldCode="MM" term="%22Amyotrophic+Lateral+Sclerosis%22">Amyotrophic Lateral Sclerosis*</searchLink>/<searchLink fieldCode="MM" term="%22Amyotrophic+Lateral+Sclerosis+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Amyotrophic+Lateral+Sclerosis%22">Amyotrophic Lateral Sclerosis*</searchLink>/<searchLink fieldCode="MM" term="%22Amyotrophic+Lateral+Sclerosis+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Amyotrophic+Lateral+Sclerosis%22">Amyotrophic Lateral Sclerosis*</searchLink>/<searchLink fieldCode="MM" term="%22Amyotrophic+Lateral+Sclerosis+pathology%22">pathology</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutation%22">Mutation*</searchLink>/<searchLink fieldCode="MM" term="%22Mutation+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Superoxide+Dismutase%22">Superoxide Dismutase*</searchLink>/<searchLink fieldCode="MM" term="%22Superoxide+Dismutase+genetics%22">genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Superoxide+Dismutase%22">Superoxide Dismutase*</searchLink>/<searchLink fieldCode="MM" term="%22Superoxide+Dismutase+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Superoxide+Dismutase%22">Superoxide Dismutase*</searchLink>/<searchLink fieldCode="MM" term="%22Superoxide+Dismutase+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Intracellular+Space%22">Intracellular Space*</searchLink>/<searchLink fieldCode="MM" term="%22Intracellular+Space+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutant+Proteins%22">Mutant Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Mutant+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Mutant+Proteins%22">Mutant Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Mutant+Proteins+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Protein+Aggregates%22">Protein Aggregates*</searchLink> <br /><searchLink fieldCode="MM" term="%22Protein+Aggregation%2C+Pathological%22">Protein Aggregation, Pathological*</searchLink><br /><searchLink fieldCode="MH" term="%22Green+Fluorescent+Proteins%22">Green Fluorescent Proteins</searchLink>/<searchLink fieldCode="MH" term="%22Green+Fluorescent+Proteins+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Superoxide+Dismutase-1%22">Superoxide Dismutase-1</searchLink> ; <searchLink fieldCode="MH" term="%22Humans%22">Humans</searchLink> ; <searchLink fieldCode="MH" term="%22Animals%22">Animals</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease with an unknown pathogenesis. It has been reported that mutations in the gene for Cu/Zn superoxide dismutase (SOD1) cause familial ALS. Mutant SOD1 undergoes aggregation and forms amyloid more easily, and SOD1-immunopositive inclusions have been observed in the spinal cords of ALS patients. Because of this, SOD1 aggregation is thought to be related to the pathogenesis of ALS. Some core regions of amyloid have been identified, but the issue of whether these regions form aggregates in living cells remains unclear, and the mechanism responsible for intracellular SOD1 aggregation also remains unclear. The findings reported in this study indicate that the aggregation of the ALS-linked mutant SOD1-EGFP was significantly enhanced when the BioID2 gene was fused to the N-terminus of the mutant SOD1-EGFP plasmid for cellular expression. Expression of a series of BioID2-(C-terminal deletion peptides of SOD1)-EGFP permitted us to identify 1-35 as a minimal N-terminal sequence and Ile35 as an essential amino acid residue that contributes to the intracellular aggregation of SOD1. The findings also showed that an additional substitution of Ile35 with Ser into the ALS mutant SOD1 resulted in the significant suppression of aggregate formation. The fact that no Ile35 mutations have been reported to date in ALS patients indicates that all ALS mutant SOD1s contain Ile35. Taken together, we propose that Ile35 plays a pivotal role in the aggregation of the ALS-linked SOD1 and that this study will contribute to our understanding of the mechanism responsible for SOD1 aggregation.<br /> (© 2024. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
– Name: Abstract
  Label: Competing Interests
  Group: Ab
  Data: Declarations. Ethics Approval and Consent to Participate: Not applicable. Consent for Publication: Not applicable. Competing Interests: The authors declare no competing interests.
– Name: Ref
  Label: References
  Group: RefInfo
  Data: Genet Med. 2012 Sep;14(9):823-6. (PMID: <searchLink fieldCode="PM" term="%2222595939%22">22595939)</searchLink><br />Commun Biol. 2020 Jan 22;3(1):38. (PMID: <searchLink fieldCode="PM" term="%2231969649%22">31969649)</searchLink><br />Nature. 1993 Mar 4;362(6415):59-62. (PMID: <searchLink fieldCode="PM" term="%228446170%22">8446170)</searchLink><br />Free Radic Res. 2016;50(11):1245-1256. (PMID: <searchLink fieldCode="PM" term="%2227629432%22">27629432)</searchLink><br />J Cell Biol. 2005 Oct 10;171(1):75-85. (PMID: <searchLink fieldCode="PM" term="%2216216923%22">16216923)</searchLink><br />Proc Natl Acad Sci U S A. 2013 Jul 2;110(27):10934-9. (PMID: <searchLink fieldCode="PM" term="%2223781106%22">23781106)</searchLink><br />Proc Natl Acad Sci U S A. 2017 Aug 15;114(33):8770-8775. (PMID: <searchLink fieldCode="PM" term="%2228760994%22">28760994)</searchLink><br />Sci Rep. 2020 Nov 26;10(1):20738. (PMID: <searchLink fieldCode="PM" term="%2233244158%22">33244158)</searchLink><br />Annu Rev Cell Dev Biol. 2018 Oct 6;34:545-568. (PMID: <searchLink fieldCode="PM" term="%2230044648%22">30044648)</searchLink><br />J Biol Chem. 2007 Jun 1;282(22):16329-35. (PMID: <searchLink fieldCode="PM" term="%2217389599%22">17389599)</searchLink><br />Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8049-54. (PMID: <searchLink fieldCode="PM" term="%2224843142%22">24843142)</searchLink><br />Nat Neurosci. 2010 Nov;13(11):1396-403. (PMID: <searchLink fieldCode="PM" term="%2220953194%22">20953194)</searchLink><br />Biochim Biophys Acta. 2010 Feb;1804(2):245-62. (PMID: <searchLink fieldCode="PM" term="%2219914407%22">19914407)</searchLink><br />Biosci Rep. 2012 Dec;32(6):539-48. (PMID: <searchLink fieldCode="PM" term="%2222804629%22">22804629)</searchLink><br />Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3155-60. (PMID: <searchLink fieldCode="PM" term="%228610185%22">8610185)</searchLink><br />Neurobiol Dis. 2019 Apr;124:297-310. (PMID: <searchLink fieldCode="PM" term="%2230528257%22">30528257)</searchLink><br />J Comp Neurol. 1998 Feb 2;391(1):64-77. (PMID: <searchLink fieldCode="PM" term="%229527542%22">9527542)</searchLink><br />PLoS One. 2018 Oct 5;13(10):e0205090. (PMID: <searchLink fieldCode="PM" term="%2230289953%22">30289953)</searchLink><br />J Biol Chem. 2010 Jul 16;285(29):22221-31. (PMID: <searchLink fieldCode="PM" term="%2220404329%22">20404329)</searchLink><br />Annu Rev Neurosci. 2004;27:723-49. (PMID: <searchLink fieldCode="PM" term="%2215217349%22">15217349)</searchLink><br />Proc Natl Acad Sci U S A. 2011 Sep 27;108(39):16398-403. (PMID: <searchLink fieldCode="PM" term="%2221930926%22">21930926)</searchLink><br />Cell. 2003 Dec 12;115(6):727-38. (PMID: <searchLink fieldCode="PM" term="%2214675537%22">14675537)</searchLink><br />Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):197-201. (PMID: <searchLink fieldCode="PM" term="%2224344300%22">24344300)</searchLink><br />Proc Natl Acad Sci U S A. 1995 Jan 31;92(3):689-93. (PMID: <searchLink fieldCode="PM" term="%227846037%22">7846037)</searchLink><br />Hum Mol Genet. 2003 Apr 1;12(7):749-57. (PMID: <searchLink fieldCode="PM" term="%2212651870%22">12651870)</searchLink><br />J Mol Biol. 2012 Aug 24;421(4-5):491-8. (PMID: <searchLink fieldCode="PM" term="%2222245492%22">22245492)</searchLink><br />Nature. 2008 Aug 28;454(7208):1088-95. (PMID: <searchLink fieldCode="PM" term="%2218756251%22">18756251)</searchLink><br />Annu Rev Biochem. 2005;74:563-93. (PMID: <searchLink fieldCode="PM" term="%2215952898%22">15952898)</searchLink><br />Protein Sci. 2021 Jan;30(1):70-82. (PMID: <searchLink fieldCode="PM" term="%2232881101%22">32881101)</searchLink><br />Methods Mol Biol. 2019;2012:299-313. (PMID: <searchLink fieldCode="PM" term="%2231161514%22">31161514)</searchLink><br />J Mol Biol. 2003 Sep 19;332(3):601-15. (PMID: <searchLink fieldCode="PM" term="%2212963370%22">12963370)</searchLink><br />Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16607-12. (PMID: <searchLink fieldCode="PM" term="%2212482932%22">12482932)</searchLink><br />Nat Commun. 2022 Jun 17;13(1):3491. (PMID: <searchLink fieldCode="PM" term="%2235715417%22">35715417)</searchLink><br />PLoS One. 2020 Jan 30;15(1):e0227655. (PMID: <searchLink fieldCode="PM" term="%2231999698%22">31999698)</searchLink><br />J Biol Chem. 2005 Feb 11;280(6):5061-70. (PMID: <searchLink fieldCode="PM" term="%2215522870%22">15522870)</searchLink><br />Proc Natl Acad Sci U S A. 2011 Feb 8;108(6):2210-5. (PMID: <searchLink fieldCode="PM" term="%2221257910%22">21257910)</searchLink><br />Exp Neurol. 2017 Jun;292:154-167. (PMID: <searchLink fieldCode="PM" term="%2228322742%22">28322742)</searchLink><br />J Biol Chem. 2007 Dec 7;282(49):35933-44. (PMID: <searchLink fieldCode="PM" term="%2217913710%22">17913710)</searchLink><br />Proc Natl Acad Sci U S A. 2018 May 1;115(18):4661-4665. (PMID: <searchLink fieldCode="PM" term="%2229666246%22">29666246)</searchLink><br />J Biochem. 2016 Feb;159(2):247-60. (PMID: <searchLink fieldCode="PM" term="%2226319711%22">26319711)</searchLink><br />J Biol Chem. 2008 Jan 11;283(2):866-74. (PMID: <searchLink fieldCode="PM" term="%2218006498%22">18006498)</searchLink><br />J Cell Biol. 1998 Dec 28;143(7):1883-98. (PMID: <searchLink fieldCode="PM" term="%229864362%22">9864362)</searchLink><br />EMBO J. 2021 May 17;40(10):e106389. (PMID: <searchLink fieldCode="PM" term="%2233792056%22">33792056)</searchLink><br />Sci Rep. 2018 Oct 22;8(1):15590. (PMID: <searchLink fieldCode="PM" term="%2230349065%22">30349065)</searchLink><br />Structure. 2016 Nov 1;24(11):1898-1906. (PMID: <searchLink fieldCode="PM" term="%2227667694%22">27667694)</searchLink><br />PLoS Biol. 2006 Dec;4(12):e417. (PMID: <searchLink fieldCode="PM" term="%2217147470%22">17147470)</searchLink>
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  Data: <i>Keywords: </i>Aggresomes; Amyotrophic lateral sclerosis (ALS); Cu/Zn superoxide dismutase (SOD1); Intracellular aggregation; Neurodegeneration
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  Data: EC 1.15.1.1 (Superoxide Dismutase-1)<br />0 (SOD1 protein, human)<br />0 (Protein Aggregates)<br />EC 1.15.1.1 (Superoxide Dismutase)<br />147336-22-9 (Green Fluorescent Proteins)<br />0 (Mutant Proteins)
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RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1007/s12035-024-04369-0
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 2023
    Subjects:
      – SubjectFull: Green Fluorescent Proteins metabolism
        Type: general
      – SubjectFull: Superoxide Dismutase-1
        Type: general
      – SubjectFull: Humans
        Type: general
      – SubjectFull: Animals
        Type: general
      – SubjectFull: Amyotrophic Lateral Sclerosis genetics
        Type: general
      – SubjectFull: Amyotrophic Lateral Sclerosis enzymology
        Type: general
      – SubjectFull: Amyotrophic Lateral Sclerosis pathology
        Type: general
      – SubjectFull: Mutation genetics
        Type: general
      – SubjectFull: Superoxide Dismutase genetics
        Type: general
      – SubjectFull: Superoxide Dismutase metabolism
        Type: general
      – SubjectFull: Superoxide Dismutase chemistry
        Type: general
      – SubjectFull: Intracellular Space metabolism
        Type: general
      – SubjectFull: Mutant Proteins metabolism
        Type: general
      – SubjectFull: Mutant Proteins chemistry
        Type: general
      – SubjectFull: Protein Aggregates
        Type: general
      – SubjectFull: Protein Aggregation, Pathological
        Type: general
    Titles:
      – TitleFull: The Ile35 Residue of the ALS-Associated Mutant SOD1 Plays a Crucial Role in the Intracellular Aggregation of the Molecule.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Asai Y
      – PersonEntity:
          Name:
            NameFull: Yano K
      – PersonEntity:
          Name:
            NameFull: Higashino T
      – PersonEntity:
          Name:
            NameFull: Yoshihara D
      – PersonEntity:
          Name:
            NameFull: Sakiyama H
      – PersonEntity:
          Name:
            NameFull: Eguchi H
      – PersonEntity:
          Name:
            NameFull: Fukushima K
      – PersonEntity:
          Name:
            NameFull: Suzuki K
      – PersonEntity:
          Name:
            NameFull: Fujiwara N
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 02
              Text: 2025 Feb
              Type: published
              Y: 2025
          Identifiers:
            – Type: issn-electronic
              Value: 1559-1182
          Numbering:
            – Type: volume
              Value: 62
            – Type: issue
              Value: 2
          Titles:
            – TitleFull: Molecular neurobiology
              Type: main
ResultId 1