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Yoshiaki Furukawa, PhD - Publications

Affiliations: 
Chemistry Keio University, Kanagwaw, Japan 
Area:
Mechanistic Chemistry of Biomolecules
Website:
http://www.chem.keio.ac.jp/~furukawa/
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77 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Furukawa Y, Shintani A, Narikiyo S, Sue K, Akutsu M, Muraki N. Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond. The Journal of Biological Chemistry. 105040. PMID 37442237 DOI: 10.1016/j.jbc.2023.105040  0.302
2023 Hashimoto K, Watanabe S, Akutsu M, Muraki N, Kamishina H, Furukawa Y, Yamanaka K. Intrinsic structural vulnerability in the hydrophobic core induces species-specific aggregation of canine SOD1 with degenerative myelopathy-linked E40K mutation. The Journal of Biological Chemistry. 104798. PMID 37156398 DOI: 10.1016/j.jbc.2023.104798  0.321
2022 Furukawa Y. A pathological link between dysregulated copper binding in Cu/Zn-superoxide dismutase and amyotrophic lateral sclerosis. Journal of Clinical Biochemistry and Nutrition. 71: 73-77. PMID 36213785 DOI: 10.3164/jcbn.22-42  0.396
2020 Furukawa Y, Tokuda E. Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis? Translational Neurodegeneration. 9: 33. PMID 32811540 DOI: 10.1186/S40035-020-00209-Y  0.435
2019 Anzai I, Tokuda E, Handa S, Misawa H, Akiyama S, Furukawa Y. Oxidative misfolding of Cu/Zn-superoxide dismutase triggered by non-canonical intramolecular disulfide formation. Free Radical Biology & Medicine. 147: 187-199. PMID 31863908 DOI: 10.1016/J.Freeradbiomed.2019.12.017  0.429
2019 Tokuda E, Takei YI, Ohara S, Fujiwara N, Hozumi I, Furukawa Y. Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis. Molecular Neurodegeneration. 14: 42. PMID 31744522 DOI: 10.1186/S13024-019-0341-5  0.443
2019 Tokuda E, Marklund SL, Furukawa Y. [Prion-like Properties of Misfolded Cu/Zn-superoxide Dismutase in Amyotrophic Lateral Sclerosis: Update and Perspectives]. Yakugaku Zasshi : Journal of the Pharmaceutical Society of Japan. 139: 1015-1019. PMID 31257248 DOI: 10.1248/Yakushi.18-00165-5  0.491
2019 Tanaka G, Yamanaka T, Furukawa Y, Kajimura N, Mitsuoka K, Nukina N. Sequence- and seed-structure-dependent polymorphic fibrils of alpha-synuclein. Biochimica Et Biophysica Acta. Molecular Basis of Disease. PMID 30790619 DOI: 10.1016/J.Bbadis.2019.02.013  0.359
2019 Tanaka G, Yamanaka T, Furukawa Y, Kajimura N, Mitsuoka K, Nukina N. Biochemical and morphological classification of disease-associated alpha-synuclein mutants aggregates. Biochemical and Biophysical Research Communications. 508: 729-734. PMID 30528390 DOI: 10.1016/J.Bbrc.2018.11.200  0.389
2018 Fujiwara N, Wagatsuma M, Oba N, Yoshihara D, Tokuda E, Sakiyama H, Eguchi H, Ichihashi M, Furukawa Y, Inoue T, Suzuki K. Cu/Zn-superoxide dismutase forms fibrillar hydrogels in a pH-dependent manner via a water-rich extended intermediate state. Plos One. 13: e0205090. PMID 30289953 DOI: 10.1371/Journal.Pone.0205090  0.389
2018 Tamaki Y, Shodai A, Morimura T, Hikiami R, Minamiyama S, Ayaki T, Tooyama I, Furukawa Y, Takahashi R, Urushitani M. Elimination of TDP-43 inclusions linked to amyotrophic lateral sclerosis by a misfolding-specific intrabody with dual proteolytic signals. Scientific Reports. 8: 6030. PMID 29662239 DOI: 10.1038/S41598-018-24463-3  0.386
2018 Tokuda E, Nomura T, Ohara S, Watanabe S, Yamanaka K, Morisaki Y, Misawa H, Furukawa Y. A copper-deficient form of mutant cu/Zn-superoxide dismutase as an early pathological species in amyotrophic lateral sclerosis. Biochimica Et Biophysica Acta. PMID 29551730 DOI: 10.1016/J.Bbadis.2018.03.015  0.436
2017 Fukuoka M, Tokuda E, Nakagome K, Wu Z, Nagano I, Furukawa Y. An essential role of N-terminal domain of copper chaperone in the enzymatic activation of Cu/Zn-superoxide dismutase. Journal of Inorganic Biochemistry. 175: 208-216. PMID 28780408 DOI: 10.1016/J.Jinorgbio.2017.07.036  0.353
2017 Tokuda E, Furukawa Y. Abnormal protein oligomers for neurodegeneration. Oncotarget. PMID 28537921 DOI: 10.18632/Oncotarget.18030  0.364
2017 Ishiguro T, Sato N, Ueyama M, Fujikake N, Sellier C, Kanegami A, Tokuda E, Zamiri B, Gall-Duncan T, Mirceta M, Furukawa Y, Yokota T, Wada K, Taylor JP, Pearson CE, et al. Regulatory Role of RNA Chaperone TDP-43 for RNA Misfolding and Repeat-Associated Translation in SCA31. Neuron. PMID 28343865 DOI: 10.1016/J.Neuron.2017.02.046  0.31
2017 Tokuda E, Anzai I, Nomura T, Toichi K, Watanabe M, Ohara S, Watanabe S, Yamanaka K, Morisaki Y, Misawa H, Furukawa Y. Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis. Molecular Neurodegeneration. 12: 2. PMID 28057013 DOI: 10.1186/S13024-016-0145-9  0.478
2016 Anzai I, Tokuda E, Mukaiyama A, Akiyama S, Endo F, Yamanaka K, Misawa H, Furukawa Y. A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis. Protein Science : a Publication of the Protein Society. PMID 27977888 DOI: 10.1002/Pro.3094  0.474
2016 Anzai I, Toichi K, Tokuda E, Mukaiyama A, Akiyama S, Furukawa Y. Screening of Drugs Inhibiting In vitro Oligomerization of Cu/Zn-Superoxide Dismutase with a Mutation Causing Amyotrophic Lateral Sclerosis. Frontiers in Molecular Biosciences. 3: 40. PMID 27556028 DOI: 10.3389/Fmolb.2016.00040  0.441
2016 Furukawa Y, Tokuda E. Aggregation of FET Proteins as a Pathological Change in Amyotrophic Lateral Sclerosis. Advances in Experimental Medicine and Biology. PMID 27311318 DOI: 10.1007/5584_2016_32  0.473
2016 Tokuda E, Furukawa Y. Copper Homeostasis as a Therapeutic Target in Amyotrophic Lateral Sclerosis with SOD1 Mutations. International Journal of Molecular Sciences. 17. PMID 27136532 DOI: 10.3390/Ijms17050636  0.468
2015 Furukawa Y, Anzai I, Akiyama S, Imai M, Cruz FJ, Saio T, Nagasawa K, Nomura T, Ishimori K. Conformational Disorder of the Most Immature Cu,Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis. The Journal of Biological Chemistry. PMID 26694608 DOI: 10.1074/Jbc.M115.683763  0.45
2015 Ogawa M, Shidara H, Oka K, Kurosawa M, Nukina N, Furukawa Y. Cysteine residues in Cu,Zn-superoxide dismutase are essential to toxicity in Caenorhabditis elegans model of amyotrophic lateral sclerosis. Biochemical and Biophysical Research Communications. 463: 1196-202. PMID 26086102 DOI: 10.1016/J.Bbrc.2015.06.084  0.505
2014 Sakurai Y, Anzai I, Furukawa Y. A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase. The Journal of Biological Chemistry. 289: 20139-49. PMID 24917671 DOI: 10.1074/Jbc.M114.567677  0.413
2014 Ogawa M, Furukawa Y. A seeded propagation of Cu, Zn-superoxide dismutase aggregates in amyotrophic lateral sclerosis. Frontiers in Cellular Neuroscience. 8: 83. PMID 24672430 DOI: 10.3389/Fncel.2014.00083  0.418
2014 Ogawa M, Furukawa Y. A seeded propagation of Cu, Zn-superoxide dismutase aggregates in amyotrophic lateral sclerosis. Frontiers in Cellular Neuroscience. 8: 83. PMID 24672430 DOI: 10.3389/Fncel.2014.00083  0.418
2014 Nomura T, Watanabe S, Kaneko K, Yamanaka K, Nukina N, Furukawa Y. Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 289: 1192-202. PMID 24280224 DOI: 10.1074/Jbc.M113.516492  0.305
2014 Nomura T, Watanabe S, Kaneko K, Yamanaka K, Nukina N, Furukawa Y. Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 289: 1192-202. PMID 24280224 DOI: 10.1074/Jbc.M113.516492  0.305
2014 Ogawa M, Shidara H, Oka K, Furukawa Y. 2P074 Investigating the Role of SOD1 Cysteine Residues in Neurodegeneration using C. elegans(01D. Protein: Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Seibutsu Butsuri. 54. DOI: 10.2142/Biophys.54.S207_2  0.344
2014 Lim CT, Furukawa Y. 2P071 An activation mechanism of human Cu,Zn-superoxide dismutase by its copper chaperone, CCS(01D. Protein: Function,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Seibutsu Butsuri. 54. DOI: 10.2142/Biophys.54.S206_5  0.411
2014 Anzai I, Toichi K, Mukaiyama A, Akiyama S, Furukawa Y. 2P060 Disulfide shuffling in Cu,Zn-superoxide dismutase is a key to develop potential drugs for neurodegeneration(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Seibutsu Butsuri. 54. DOI: 10.2142/Biophys.54.S204_6  0.388
2013 Furukawa Y. Redox environment is an intracellular factor to operate distinct pathways for aggregation of Cu,Zn-superoxide dismutase in amyotrophic lateral sclerosis. Frontiers in Cellular Neuroscience. 7: 240. PMID 24348334 DOI: 10.3389/Fncel.2013.00240  0.493
2013 Furukawa Y, Kaneko K, Watanabe S, Yamanaka K, Nukina N. Intracellular seeded aggregation of mutant Cu,Zn-superoxide dismutase associated with amyotrophic lateral sclerosis. Febs Letters. 587: 2500-5. PMID 23831581 DOI: 10.1016/J.Febslet.2013.06.046  0.473
2013 Furukawa Y, Nukina N. Functional diversity of protein fibrillar aggregates from physiology to RNA granules to neurodegenerative diseases. Biochimica Et Biophysica Acta. 1832: 1271-8. PMID 23597596 DOI: 10.1016/J.Bbadis.2013.04.011  0.439
2013 Toichi K, Yamanaka K, Furukawa Y. Disulfide scrambling describes the oligomer formation of superoxide dismutase (SOD1) proteins in the familial form of amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 288: 4970-80. PMID 23264618 DOI: 10.1074/Jbc.M112.414235  0.479
2013 Nishiura Y, Furukawa Y. 2P036 A yeast model for testing roles of aging process in neurodegenerative diseases(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S164_6  0.324
2013 Anzai I, Toichi K, Furukawa Y. 2P035 Oligomerization mechanism of mutant SOD1 proteins in a familial form of amyotrophic lateral sclerosis(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S164_5  0.421
2013 Wakahara Y, Honda K, Furukawa Y. 2P034 Zinc ion regulates molecular recognition in copper chaperone system(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S164_4  0.36
2013 Nakagome K, Mitomi Y, Furukawa Y. 2P033 A protein network regulating an intracellular copper transfer to superoxide dismutase(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S164_3  0.377
2013 Nomura T, Furukawa Y. 2P032 Aberrant monomer-dimer equilibrium of mutant SOD1 in ALS: Development of peptides probing protein quaternary structures(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S164_2  0.395
2013 Ogawa M, Shidara H, Oka K, Furukawa Y. 2P031 A worm model describing propagation of protein aggregates in neurodegenerative diseases(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S164_1  0.394
2013 Sakurai Y, Furukawa Y. 2P030 Folding mechanism of bacterial SOD1 regulated by disulfide formation(01B. Protein: Structure & Function,Poster) Seibutsu Butsuri. 53. DOI: 10.2142/Biophys.53.S163_6  0.374
2013 Nomura T, Watanabe S, Kaneko K, Yamanaka K, Nukina N, Furukawa Y. 1P065 A new pathomechanism of amyotrophic lateral sclerosis regulated by aggregation of FUS/TLS protein(01C. Protein:Property,Poster) Seibutsu Butsuri. 53: S116. DOI: 10.2142/Biophys.53.S116_5  0.404
2012 Mitomi Y, Nomura T, Kurosawa M, Nukina N, Furukawa Y. Post-aggregation oxidation of mutant huntingtin controls the interactions between aggregates. The Journal of Biological Chemistry. 287: 34764-75. PMID 22891249 DOI: 10.1074/Jbc.M112.387035  0.451
2012 Furukawa Y. Pathological roles of wild-type cu, zn-superoxide dismutase in amyotrophic lateral sclerosis. Neurology Research International. 2012: 323261. PMID 22830015 DOI: 10.1155/2012/323261  0.433
2012 Ding F, Furukawa Y, Nukina N, Dokholyan NV. Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates. Journal of Molecular Biology. 421: 548-60. PMID 22210350 DOI: 10.1016/J.Jmb.2011.12.029  0.426
2012 Toichi K, Furukawa Y. 2B1610 Destabilization of SOD1 facilitates abnormal scrambling of its disulfide bond in the familial form of amyotrophic lateral sclerosis(Proteins:Structure & Function II:Theory, Aggregation,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 52. DOI: 10.2142/Biophys.52.S41_6  0.375
2012 Mitomi Y, Nomura T, Kurosawa M, Nukina N, Furukawa Y. 2B1558 A mechanism controlling the morphologies of protein aggregates by "post-aggregation oxidation"(Proteins:Structure & Function II:Theory, Aggregation,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 52: S41. DOI: 10.2142/Biophys.52.S41_5  0.412
2012 Sakurai Y, Furukawa Y. 2B1546 A copper chaperone-independent mechanism for activation of Cu, Zn-superoxide dismutase(Proteins:Structure & Function II:Theory, Aggregation,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 52. DOI: 10.2142/Biophys.52.S41_4  0.429
2012 Furukawa Y. 2B1534 Redox environment is an intracellular factor to operate distinct pathways for protein aggregation(Proteins:Structure & Function II:Theory, Aggregation,Oral Presentation,The 50th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 52. DOI: 10.2142/Biophys.52.S41_3  0.383
2011 Furukawa Y, Kaneko K, Nukina N. Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site. Biochimica Et Biophysica Acta. 1812: 1577-83. PMID 21946215 DOI: 10.1016/J.Bbadis.2011.09.005  0.327
2011 Furukawa Y, Kaneko K, Nukina N. Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties. The Journal of Biological Chemistry. 286: 27236-46. PMID 21659525 DOI: 10.1074/Jbc.M111.248963  0.343
2011 Furukawa Y, Kaneko K, Watanabe S, Yamanaka K, Nukina N. A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions. The Journal of Biological Chemistry. 286: 18664-72. PMID 21454603 DOI: 10.1074/Jbc.M111.231209  0.405
2011 Toichi K, Furukawa Y. 1D1412 A thiol-disulfide status in SOD1 controls distinct pathways for aggregate formation in amyotrophic lateral sclerosis(Protein: Property 1,The 49th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51. DOI: 10.2142/Biophys.51.S37_2  0.395
2011 Mitomi Y, Furukawa Y. 1D1348 P19 Morphological and biochemical properties of protein aggregates controlled by "post-aggregation modifications"(Protein: Property 1,The 49th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51. DOI: 10.2142/Biophys.51.S37_1  0.396
2011 Furukawa Y. 2SJ-06 Polymorphism of protein aggregates produced by genetic and chemical modifications(2SJ New developments in protein complex research: From molecules to supramolecules and aggregates,The 49th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 51. DOI: 10.2142/Biophys.51.S23_3  0.37
2010 Furukawa Y, Kaneko K, Yamanaka K, Nukina N. Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 285: 22221-31. PMID 20404329 DOI: 10.1074/Jbc.M110.113597  0.457
2010 Yamanaka T, Tosaki A, Miyazaki H, Kurosawa M, Furukawa Y, Yamada M, Nukina N. Mutant huntingtin fragment selectively suppresses Brn-2 POU domain transcription factor to mediate hypothalamic cell dysfunction. Human Molecular Genetics. 19: 2099-112. PMID 20185558 DOI: 10.1093/Hmg/Ddq087  0.337
2010 Furukawa Y, Kaneko K, Yamanaka K, Nukina N. 2P048 1E1420 Structural polymorphism of protein aggregates and its pathological relevance(The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 50: S90. DOI: 10.2142/Biophys.50.S90_3  0.354
2010 Furukawa Y. Cross-seeded Fibrillation of Q/N-rich Proteins Offers New Pathomechanism of Polyglutamine Diseases Seibutsu Butsuri. 50: 242-243. DOI: 10.2142/Biophys.50.242  0.317
2009 Furukawa Y, Kaneko K, Matsumoto G, Kurosawa M, Nukina N. Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 29: 5153-62. PMID 19386911 DOI: 10.1523/Jneurosci.0783-09.2009  0.432
2009 Furukawa Y, Kaneko K, Kurosawa M, Matsumoto G, Nukina N. 1P-058 Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases(Protein:Property, The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S72. DOI: 10.2142/Biophys.49.S72_3  0.353
2009 Furukawa Y, Kaneko K, Kurosawa M, Matsumoto G, Nukina N. 1YP1-08 Cross-seeding fibrillation of Q/N-rich proteins offers new pathomechanism of polyglutamine diseases(1YP1 Early Research in Biophysics Award Candidate Presentations,The 47th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 49: S2. DOI: 10.2142/Biophys.49.S2_2  0.31
2009 Furukawa Y. Post-translational Modifications Regulate Activation and Aggregation of Cu, Zn-superoxide Dismutase Seibutsu Butsuri. 49: 90-91. DOI: 10.2142/Biophys.49.090  0.421
2008 Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N. Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 283: 24167-76. PMID 18552350 DOI: 10.1074/Jbc.M802083200  0.655
2008 Doi H, Okamura K, Bauer PO, Furukawa Y, Shimizu H, Kurosawa M, Machida Y, Miyazaki H, Mitsui K, Kuroiwa Y, Nukina N. RNA-binding protein TLS is a major nuclear aggregate-interacting protein in huntingtin exon 1 with expanded polyglutamine-expressing cells. The Journal of Biological Chemistry. 283: 6489-500. PMID 18167354 DOI: 10.1074/Jbc.M705306200  0.413
2008 Furukawa Y, Kaneko K, Nukina N. 2P-076 Molecular dissection of SOD1 aggregation and its structural rationale(The 46th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 48: S86-S87. DOI: 10.2142/Biophys.48.S86_6  0.331
2007 Furukawa Y, Kaneko K, Yamanaka K, Nukina N. 3P059 Elimination of post-translational modifications in SOD1 leads to form pathological amyloid-like aggregates in familial ALS(Proteins-stability, folding, and other physicochemical properties,Oral Presentations) Seibutsu Butsuri. 47: S217. DOI: 10.2142/Biophys.47.S217_4  0.447
2006 Furukawa Y, O'Halloran TV. Posttranslational modifications in Cu,Zn-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. Antioxidants & Redox Signaling. 8: 847-67. PMID 16771675 DOI: 10.1089/Ars.2006.8.847  0.647
2006 Deng HX, Shi Y, Furukawa Y, Zhai H, Fu R, Liu E, Gorrie GH, Khan MS, Hung WY, Bigio EH, Lukas T, Dal Canto MC, O'Halloran TV, Siddique T. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proceedings of the National Academy of Sciences of the United States of America. 103: 7142-7. PMID 16636275 DOI: 10.1073/Pnas.0602046103  0.639
2006 Furukawa Y, Fu R, Deng HX, Siddique T, O'Halloran TV. Disulfide cross-linked protein represents a significant fraction of ALS-associated Cu, Zn-superoxide dismutase aggregates in spinal cords of model mice. Proceedings of the National Academy of Sciences of the United States of America. 103: 7148-53. PMID 16636274 DOI: 10.1073/Pnas.0602048103  0.656
2006 Furukawa Y, Nukina N. 2P102 Is ALS an amyloid disease? : Molecular mechanism of SOD1 fibrillization(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) Seibutsu Butsuri. 46: S321. DOI: 10.2142/Biophys.46.S321_2  0.407
2005 Furukawa Y, O'Halloran TV. Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation. The Journal of Biological Chemistry. 280: 17266-74. PMID 15691826 DOI: 10.1074/Jbc.M500482200  0.65
2005 Furukawa Y, O'Halloran T. 2P064 Post-translational control of the SOD1 maturation and its relevance to ALS Seibutsu Butsuri. 45: S135. DOI: 10.2142/Biophys.45.S135_4  0.53
2004 Arnesano F, Banci L, Bertini I, Martinelli M, Furukawa Y, O'Halloran TV. The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. The Journal of Biological Chemistry. 279: 47998-8003. PMID 15326189 DOI: 10.1074/Jbc.M406021200  0.629
2004 Furukawa Y, Torres AS, O'Halloran TV. Oxygen-induced maturation of SOD1: a key role for disulfide formation by the copper chaperone CCS. The Embo Journal. 23: 2872-81. PMID 15215895 DOI: 10.1038/Sj.Emboj.7600276  0.722
2003 Field LS, Furukawa Y, O'Halloran TV, Culotta VC. Factors controlling the uptake of yeast copper/zinc superoxide dismutase into mitochondria. The Journal of Biological Chemistry. 278: 28052-9. PMID 12748182 DOI: 10.1074/Jbc.M304296200  0.57
2003 Furukawa Y, Brown NM, O'Halloran TV. Metallochaperone protein, CCS, has sulfhydryl oxidase activity: Post-translational modification of superoxide dismutase Journal of Inorganic Biochemistry. 96: 44. DOI: 10.1016/S0162-0134(03)80480-4  0.577
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