• 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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