Yoshiaki Furukawa, PhD - Publications

Affiliations: 
Chemistry Keio University, Kanagwaw, Japan 
Area:
Mechanistic Chemistry of Biomolecules
Website:
http://www.chem.keio.ac.jp/~furukawa/

47 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
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  0.4
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  0.4
2018 Okuzumi A, Kurosawa M, Hatano T, Takanashi M, Nojiri S, Fukuhara T, Yamanaka T, Miyazaki H, Yoshinaga S, Furukawa Y, Shimogori T, Hattori N, Nukina N. Rapid dissemination of alpha-synuclein seeds through neural circuits in an in-vivo prion-like seeding experiment. Acta Neuropathologica Communications. 6: 96. PMID 30231908 DOI: 10.1186/s40478-018-0587-0  0.4
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  0.4
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  0.4
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  0.4
2016 Furukawa Y, Suzuki Y, Fukuoka M, Nagasawa K, Nakagome K, Shimizu H, Mukaiyama A, Akiyama S. A molecular mechanism realizing sequence-specific recognition of nucleic acids by TDP-43. Scientific Reports. 6: 20576. PMID 26838063 DOI: 10.1038/srep20576  1
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  1
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  0.4
2015 Watanabe H, Shiomi H, Nakatsuma K, Morimoto T, Taniguchi T, Furukawa Y, Nakagawa Y, Horie M, Kimura T, Kimura T, Sakata R, Marui A, Matsuda M, Mitsuoka H, ... ... Furukawa Y, et al. Clinical efficacy of thrombus aspiration on 5-year clinical outcomes in patients with ST-segment elevation acute myocardial infarction undergoing percutaneous coronary intervention. Journal of the American Heart Association. 4: e001962. PMID 26077588 DOI: 10.1161/JAHA.115.001962  0.4
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: 1196-1202. DOI: 10.1016/j.bbrc.2015.06.084  1
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  1
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  1
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  1
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  1
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  1
2014 Sadykov AF, Gerashchenko AP, Piskunov YV, Ogloblichev VV, Smol’nikov AG, Verkhovskii SV, Buzlukov AL, Arapova IY, Furukawa Y, Yakubovskii AY, Bush AA. Magnetic structure of the low-dimensional magnet NaCu2O2: 63,65Cu and 23Na NMR studies Journal of Experimental and Theoretical Physics. 119: 870-879. DOI: 10.1134/S1063776114110107  0.01
2014 Sadykov AF, Gerashchenko AP, Piskunov YV, Ogloblichev VV, Smol’nikov AG, Verkhovskii SV, Buzlukov AL, Arapova IY, Furukawa Y, Yakubovskii AY, Bush AA. Magnetic structure of the low-dimensional magnet NaCu2O2: 63,65Cu and 23Na NMR studies Journal of Experimental and Theoretical Physics. 119: 870-879. DOI: 10.1134/S1063776114110107  0.01
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  1
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  1
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  1
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  1
2013 Furukawa Y. Polymorphism of Tau Fibrils Bio-Nanoimaging: Protein Misfolding and Aggregation. 213-222. DOI: 10.1016/B978-0-12-394431-3.00019-5  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2005 Furukawa Y, Ban T, Hamada D, Ishimori K, Goto Y, Morishima I. Electron transfer reaction in a single protein molecule observed by total internal reflection fluorescence microscopy. Journal of the American Chemical Society. 127: 2098-103. PMID 15713086 DOI: 10.1021/ja0478173  1
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  1
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  1
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  1
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  1
2002 Furukawa Y, Ishimori K, Morishima I. Oxidation-state-dependent protein docking between cytochrome c and cytochrome b(5): high-pressure laser flash photolysis study. Biochemistry. 41: 9824-32. PMID 12146948 DOI: 10.1021/bi0257890  1
2002 Furukawa Y, Matsuda F, Ishimori K, Morishima I. Investigation of the electron-transfer mechanism by cross-linking between Zn-substituted myoglobin and cytochrome b(5). Journal of the American Chemical Society. 124: 4008-19. PMID 11942839 DOI: 10.1021/ja0171916  1
2001 Furukawa Y, Morishima I. The role of water molecules in the association of cytochrome P450cam with putidaredoxin. An osmotic pressure study Journal of Biological Chemistry. 276: 12983-12990. PMID 11278642 DOI: 10.1074/jbc.M010217200  1
2000 Furukawa Y, Ishimori K, Morishima I. Electron transfer reactions in Zn-substituted cytochrome P450cam Biochemistry. 39: 10996-11004. PMID 10998236 DOI: 10.1021/bi000874y  1
2000 Furukawa Y, Ishimori K, Morishima I. Pressure Dependence of the Intramolecular Electron Transfer Reaction in Myoglobin Reinvestigated Journal of Physical Chemistry B. 104: 1817-1825.  1
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