• Ohhashi Y., Yamaguchi Y., Kurahashi H., Kamatari Y.O., Sugiyama S., Uluca B., Piechatzek T., Komi Y., Shida T., Müller H., Hanashima S., Heise H., Kuwata K, and Tanaka M. Molecular basis for diversification of yeast prion strain conformation, Proc. Natl. Acad. Sci. U. S. A., in press (2018)


  • Tanaka, M., Ishizuka, K., Nekooki-Machida, Y., Endo, R., Takashima, N., Sasaki, H., Komi, Y., Gathercole, A., Huston, E., Ishii, K., Hui, K.K., Kurosawa, M., Kim, S.H., Nukina, N.,Takimoto, E., Houslay, M.D., Sawa, A. Aggregation of scaffolding protein DISC1 dysregulates phosphodiesterase 4 in Huntington's disease. J. Clin. Invest., 127, 1438-50 (2017)


  • Toyoshima, M., Akamatsu, W., Okada, Y., Ohnishi, T., Balan, S., Hisano, Y., Iwayama, Y.,Toyota, T., Matsumoto, T., Itasaka, N., Sugiyama, S., Tanaka, M., Yano, M., Dean, B., Okano, H., Yoshikawa, T. Analysis of induced pluripotent stem cells carrying 22q11.2 deletion. Transl. Psychiatry, 6, e934 (2016)


  • Suzuki, G., Weissman, J.S. and Tanaka, M. [KIL-d] protein element confers antiviral activity via catastrophic viral mutagenesis. Mol. Cell, 60, 651-660 (2015).
  • Tanaka, M. and Komi, Y. Layers of structure and function in protein aggregation. Nat. Chem. Biol., 11, 373-377 (2015).


  • Nilsson, P., Sekiguchi, M., Akagi, T., Izumi, S., Komori, T., Hui, K., Sörgjerd, K., Tanaka, M., Saito, T., Iwata, N., Saido, T.C. Autophagy-related protein 7 deficiency in APP transgenic mice decreases Aβ in multivesicular bodies and induces Aβ accumulation in the Golgi. Am. J. Pathol., 185(2), 305-13 (2015).
  • Sugiyama, S. and Tanaka, M. Self-propagating amyloid as a critical regulator for diverse cellular functions. J. Biochem, 155, 345-351 (2014).


  • Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., and Saido, T.C. Aβ secretion and plaque formation depend on autophagy. Cell Reports, 5, 61-69 (2013).
  • Suzuki, G. and Tanaka, M. Active conversion to the prion state as a molecular switch for cellular adaptation to environmental stress. Bioessays, 35, 12-16 (2013).
  • Suzuki, G. and Tanaka, M. Expanding the yeast prion world: Active prion conversion of non-glutamine/asparagine-rich Mod5 for cell survival. Prion, 7, 109-113 (2013).


  • Suzuki, G., Shimazu, N., and Tanaka, M. A Yeast Prion, Mod 5, Promotes Acquired Drug Resistance and Cell Survival Under Environmental Stress. Science 336, 355-359 (2012).


  • Tanaka, M. Tracking a toxic polyglutamine epitope. Nat. Chem. Biol. 7, 861-862 (2011).
  • Tonoki, A., Kuranaga, E., Ito, N., Nekooki-Machida, Y., Tanaka, M., and Miura, M. Aging causes distinct characteristics of polyglutamine amyloids in vivo. Genes Cells 16, 557-564 (2011).
  • Foo, C.K., Ohhashi, Y., Kelly, M.J., Tanaka, M., and Weissman, J.S. Radically Different Amyloid Conformations Dictate the Seeding Specificity of a Chimeric Sup35 Prion. J. Mol. Biol. 408, 1-8 (2011).


  • Ohhashi, Y., Ito, K., Toyama, B.H., Weissman, J.S., and Tanaka M. Differences in prion strain conformations result from non-native interactions in a nucleus. Nat. Chem. Biol. 6, 225-230 (2010).
  • Tanaka, M. A protein transformation protocol for introducing yeast prion particles into yeast. Methods in Enzymology (Guide to Yeast Genetics: Functional Genomics, Proteomics and Other Systems Analysis), 470, 681-693 (2010).


  • Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., and Tanaka, M. Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity. Proc. Natl. Acad. Sci. U. S. A., 106, 9678-9684(2009).


  • McDobald, M., Kendall, A., Tanaka, M., Weissman, J.S., and Stubbs, G. Enclosed chambers for humidity control and sample containment in fiber diffraction. J. Appl. Cryst.,41, 206-209 (2008).

~2007 (selected publications)

  • Krzewska, J., Tanaka, M., Burston, S.G., and Melki, R. Biochemical and functional analysis of the assembly of full-length Sup35p and its prion-forming domain. J. Biol. Chem., 282, 1679-1686 (2007).
  • Tanaka, M., Collins, S.R., Toyama, B.H., and Weissman, J.S. The Physical Basis of How Prion Conformations Determine Strain Phenotypes. Nature, 442, 585-589 (2006).
  • Tanaka, M., Chien, P., Yonekura, K., Weissman, J.S. Mechanism of cross-species prion transmission: An infectious conformation compatible with two highly divergent yeast prion proteins. Cell 121, 49-62 (2005).
  • Tanaka, M., Machida, Y., and Nukina, N. A novel therapeutic strategy for polyglutamine diseases by stabilizing aggregation-prone proteins with small molecules. J. Mol. Med. 83, 343-352 (2005).
  • Tanaka, M., Chien, P., Naber, N., Cooke, R., and Weissman, J.S. Conformational Variations in an Infectious Protein Determine Prion Strain Differences. Nature 428, 323-328 (2004).
  • Venkatraman, P. Wetzel, R. Tanaka, M., Nukina, M., and Goldberg, A.L. Eukaryotic Proteasomes Cannot Digest Polyglutamine Sequences and Release Them Intact during Degradation of Polyglutamine-Containing Proteins. Mol. Cell 14, 95-104 (2004).
  • Tanaka, M., Machida, Y., Niu, S., Ikeda, T., Jana, N.R., Doi, H., Kurosawa, M., Nekooki, M., and Nukina, N. Trehalose alleviates polyglutamine-mediated pathology in a mouse model of Huntington disease. Nat. Med. 10, 148-154 (2004).
  • Tanaka, M., Machida, Y., Nishikawa, Y., Akagi, T., Hashikawa, T., Fujisawa, T. and Nukina, N. Expansion of polyglutamine induces the formation of quasi-aggregate in the early stage of protein fibrillization. J. Biol. Chem. 278, 34717–34724 (2003).
  • Tanaka, M., Matsuura, K., Yoshioka, S., Takahashi, S., Ishimori, K., Hori, H., and Morishima, I. Activation of Hydrogen Peroxide in Horseradish Peroxidase Occurs within approximately 200μs Observed by a New Freeze-Quench Device. Biophys. J. 84, 1998-2004 (2003).

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