Endo Lab.

遠藤斗志也研究室は、2014年より名古屋大学から京都産業大学に移りました。
京都産業大学、日本科学未来館(お台場)サテライトラボの2つの拠点に加え,
山形大学理学部の田村康研究室とも連携して大きく飛躍します。

Original paper

2018

  • Y. Tamura, S. Kawano, and T. Endo
  • Organelle contact zones as sites for lipid transfer
  • J. Biochem. in press (2018)

  • T. Jores, J. Lawatscheck, V. Beke, M. Franz-Wachtel, K. Yunoki, J.C. Fitzgerald, B. Macek, T. Endo, H. Kalbacher, J. Buchner, D. Rapaport
  • Cytosolic Hsp70 and Hsp40 chaperones enable the biogenesis of mitochondrial β-barrel proteins.
  • J. Cell Biol. 217(9), 3091-3108, doi: 10.1083/jcb.201712029


  • T. Endo, Y. Tamura, and S. Kawano
  • Phospholipid transfer by ERMES components (Editorial)
  • Aging 10, 528-529 (2018)
  • doi.org/10.18632/aging.101434 (online published on April 28, 2018)

  • Y. Kakimoto, S. Tashiro, R. Kojima, Y. Morozumi, T. Endo, and Y. Tamura
  • Visualizing multiple inter-organelle contact sites using the organelle-targeted split-GFP system
  • Sci. Rep. 8, 6175 (2018)


  • A. Matsumura, J. Higuchi, Y. Watanabe, K. Aoki, S. Akabane, T. Endo, and T. Oka
  • Inactivation of cardiolipin synthase triggers changes in mitochondrial morphology
  • FEBS Lett. 592, 209-218 (2018)

  • S. Kawano, Y. Tamura, R. Kojima, S. Bala, E. Asai, A. H. Michel., B. Kornmann, I. Riezman, H. Riezman, Y. Sakae, Y. Okamoto., and T. Endo
  • Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.
  • J. Cell Biol. 217, 959-974 (2018)

2016

  • Suzuki T, Iida N, Suzuki J, Watanabe Y, Endo T, Hisabori T, Yoshida M.
  • Expression of mammalian mitochondrial F1-ATPase in Escherichia coli depends on two chaperone factors, AF1 and AF2.
  • FEBS Open Bio. 2016 Oct 25;6(12):1267-1272. doi: 10.1002/2211-5463.12143.

  • R. Kojima, S. Kajiura, H. Sesaki, T. Endo, and Y. Tamura
  • Identification of multi‐copy suppressors for endoplasmic reticulum‐mitochondria tethering proteins in Saccharomyces cerevisiae.
  • FEBS Lett., 590, 3061-3070 (2016) DOI: 10.1002/1873-3468.12358

  • S. Arakawa, K. Yunoki, T. Izawa, Y. Tamura, S. Nishikawa, and T. Endo
  • Quality control of nonstop membrane proteins at the ER membrane and in the cytosol.
  • Sci. Rep. 6, Article number: 30795, doi:10.1038/srep30795 (2016)

  • R. Kojima, T. Endo, and Y. Tamura
  • A phospholipid transfer function of ER-mitochondria encounter structure revealed in vitro
  • Sci. Rep. 6, Article number 20777, doi:10.1038/srep30777 (2016)

  • T. Jores, A. Klinger, L. E. Groß, S. Kawano, N. Flinner, E. Duchardt-Ferner, J. Wo ̈hnert, H. Kalbacher, T. Endo, E. Schleiff, and D. Rapaport
  • Characterization of the targeting signal in mitochondrial β-barrel proteins
  • Nature Commun. 7, Article number 12036, doi:10.1038/ncomms12036 (2016)

  • N. Miyata, Y. Watanabe, Y. Tamura, T. Endo, and O. Kuge
  • Phosphatidylserine transport by Ups2–Mdm35 in respiration-active mitochondria
  • J. Cell Biol. 214, 77-88, doi:10.1083/jcb.201601082 (2016)
  • ---featured by Bruno Mesmin, "Mitochondrial lipid transport and biosynthesis: A complex balance"(Spotlight), J. Cell Biol. 214, 9-11 (2016)

2015

  • T. Shiota, K. Imai, J. Qiu, V. L. Hewitt, K. Tan, H. Shen, N. Sakiyama, Y. Fukasawa, S. Hayat, M. Kamiya, A. Elofsson, K. Tomii, P. Horton, N. Wiedemann, N. Pfanner, T Lithgow, T. Endo
  • Molecular architecture of the active mitochondrial protein gate
  • Science 349 (6255), 1544-1548 (2015)
  • (featured by D. Mokranjac and W. Neupert, Architecture of a protein entry gate (News and Views), Nature 528, 201-202 (2015))

  • Y. Watanabe, Y. Tamura, S. Kawano, and T. Endo
  • Structural and mechanistic insights into phospholipid transfer by Ups1–Mdm35 in mitochondria
  • Nature Commun. 6, Article number: 7922 (2015)

  • D. Maruyama, T. Endo, and S. Nishikawa
  • BiP3 supports the early stages of female gametogenesis in the absence of BiP1 and BiP2 in Arabidopsis thaliana
  • Plant Signal Behav. 10 (7) e1035853 (2015)

  • A. Takano, T. Kajita, M. Mochizuki, T. Endo, and T. Yoshihisa
  • Cytosolic Hsp70 and co-chaperones constitute a novel system for tRNA import into the nucleus.
  • eLife 4, e04659 (2015)

2014

  • D. Maruyama, M. Yamamoto, T. Endo, and S. Nishikawa*
  • Different sets of ER-resident J-proteins regulate distinct polar nuclear-membrane fusion events in Alabidopsis thaliana
  • Plant Cell Physiol. 55(11),1937-1944 (2014)

  • Y. Tamura*, H. Sesaki and T. Endo
  • Phospholipid transport via mitochondria.
  • Traffic 15 (9), 933-945 (2014)

  • Q. Zhang, Y. Tamura, M. Roy, Y. Adachi, M. Iijima, H. Sesaki
  • Biosynthesis and roles of phospholipids in mitochondrial fusion, division and mitophagy.
  • Cellular and Molecular Life Sciences 71, 3767-3778(2014)

  • F. Koyano, K.Okatsu, H. Kosako, Y. Tamura, E. Go, M. Kimura, Y. Kimura, H.Tsuchiya, H. Yoshihara, T. Hirokawa, T. Endo, E. A. Fon, J. F. Trempe, Y. Saeki, K. Tanaka, and N. Matsuda
  • Ubiquitin is phosphorylated by PINKI to activate parkin.
  • Nature 510, 162-166 (2014)

  • Jiyao Song, Yasushi Tamura, Tohru Yoshihisa, and Toshiya Endo
  • A novel import route for an N-anchor mitochondrial outer membrane protein aided by the TIM23 complex
  • EMBO Rep. 15, 670-677 (2014)

  • H. Okamoto, A. Miyagawa, T. Shiota, Y. Tamura and T. Endo
  • Intra-molecular disulfide bond of Tim22 maintains integrity of the TIM22 complex in the mitochondrial inner membrane
  • J. Biol. Chern. 289, 4827-4838 (2014)

  • D. Maruyama, T. Sugiyama, T. Endo, and S. Nishikawa
  • Multiple BiP genes of Alabidopsis
    thaliana are required for male garnetogenesis and pollen competitiveness.
  • Plant Cell Physiol. 55, 801-810 (2014)

  • B. Rahman, S. Kawano, K. Yunoki-Esaki, T. Anzai, and T. Endo
  • NMR analyses on the interactions of the yeast Tim50 C-terminal region with the presequence and Tim50 core domain
  • FEBS Lett. 588, 678-684 (2014)

2013

  • Y. Tamura and T. Endo
  • Unveiling the last missing link of the cardiolipin synthetic pathway in mitochondria (Editorial)
  • Aging 6, 392-393 (2013) (online published on June 26, 2013)

  • K. Itoh, Y. Tamura, M. Iijima, and H. Sesaki
  • Effects of Fcj1-Mos1 and Mitochondrial Division on Aggregation of Mitochondrial DNA Nucleoids and Organelle Morphology
  • Mol. Biol. Cell 24, 1842-1851 (2013)

  • Y. Tamura, Y. Harada, S. Nishikawa, K. Yamano, M. Kamiya, T. Shiota, T. Kuroda, O. Kuge, H. Sesaki, K. Imai, K. Tomii, and T. Endo
  • Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria
  • Cell Metab. 17, 709-718 (2013)

  • O. Nureki, R. Ishitani, T. Yoshihisa, M. Sato, N. Dohmae, D. Mangroo, H. Becker, K. Nozawa, F. Arisaka, S. Kanamaru, and S. Bruno,
  • Crystal structure of Cex1p reveals the mechanism of tRNA trafficking between nucleus and cytoplasm
  • Nuc. Acid Res. (2013)41, 3901-3914

  • T. Shiota, S. Nishikawa, and T. Endo
  • Analyses of protein-protein interactions by in vivo photocrosslinking in budding yeast
  • in Meth. Mol. Biol. "Membrane Biogenesis" (eds. D. Rapaport and J. M. Herrmann)pp207-217
  • Springer (2013)

2012

  • Y. Tamura, O. Onguka, K. Itoh, T. Endo, M. Iijima, S. M. Claypool, H. Sesaki
  • Phosphatidylethanolamine biogenesis in mitochondria: phosphatidylserine (PS) trafficking is independent of a PS decarboxylase and intermembrane space proteins, Ups1p and Ups2p.
  • J. Biol. Chem. 287, 43961-43971 (2012)

  • T. Shiota*, M. Maruyama*, M. Miura*, Y. Tamura*, K. Yamano, M. Esaki, and T. Endo
  • (* These authors contributed equally to this work.)
  • The Tom40 assembly process probed using the attachment of different intra-mitochondrial sorting signals.
  • Mol. Biol. Cell 23,3936-3947 (2012)

  • T. Izawa, T. Tsuboi, K. Kuroha, T. Inada, S. Nishikawa, and T. Endo
  • Role of Dom34:Hbs1 in non-stop protein clearance for normal organelle protein influx
  • Cell Reports 2, 447-453 (2012)

  • T. Izawa, H. Nagai, T. Endo, and S. Nishikawa
  • Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation
  • Mol. Biol. Cell 23, 1283-1293 (2012)

2011

  • T. Shiota, H. Mabuchi, S. Tanaka-Yamano, K. Yamano, and T. Endo
  • In vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work
  • Proc. Natl. Acad. Sci. USA 108, 15179-15183 (2011)

  • S. Mori, T. Kajita, T. Endo, and T. Yoshihisa
  • The intron of tRNA-TrpCCA is dispensable for growth and translation of Saccharomyces cerevisiae.
  • RNA 17,1760-1769 (2011)

  • T. Endo, S. Kawano, and K. Yamano
  • BamE structure: the assembly of β-barrel proteins in the outer membranes of bacteria and mitochondria
  • EMBO Rep. (hot off the press) 12, 94-95 (2011)

  • S.C. Botelho, M. Osterberg, A.S. Reichert, K. Yamano, P. Bjorkholm, T. Endo, G. von Heijne, and H. Kim
  • TIM23-mediated insertion of transmembrane α-helices into the mitochondrial inner membrane
  • EMBO J. 30, 1003-1011 (2011)

  • H. Yamamoto, N. Itoh, S. Kawano, Y. Yatsukawa, T. Momose, T. Makio, M. Matsunaga, M. Yokota, M. Esaki, T. Shodai, D. Kohda, A.E.A. Hobbs, R.E. Jensen, and T. Endo
  • Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria
  • Proc. Natl. Acad. Sci. USA 108, 91-96 (2011)

2010

  • K. Yamano, S. Tanaka-Yamano, and T. Endo
  • Tom7 regulates Mdm10-mediated assembly of the mitochondrial import channel protein Tom40
  • J. Biol. Chem. 285, 41222-41231 (2010)

  • T. Mori, C. Ogasawara, T. Inada, M. Englert, H. Beier, M. Takezawa, T. Endo, and T. Yoshihisa
  • Dual functions of yeast tRNA ligase in the unfolded protein response: unconventional cytoplasmic splicing of HAC1 pre-mRNA is not sufficient to release translational attenuation
  • Mol. Biol. Cell 21, 3722-3734 (2010). (A Highlights from MBoC Selection)

  • M. Ruprecht, T. Bionda, T. Sato, M.S. Sommer, T. Endo, and E. Schleiff
  • On the impact of precursor unfolding during protein import into chloroplasts
  • Mol. Plant 3, 499-508 (2010)

  • M. Yamamoto, M. Kawanabe, Y. Hayashi, T. Endo, and S. Nishikawa
  • A vacuolar carboxypeptidase mutant of Arabidopsis thaliana is degraded by the ERAD pathway independently of its N-glycan.
  • Biochem. Biophys. Res. Commun. 393, 384-389(2010)

  • K. Yagawa, K. Yamano, T. Oguro, M. Maeda, T. Sato, T. Momose, S. Kawano, and T. Endo
  • Structural basis for unfolding pathway-dependent stability of proteins: vectorial unfolding vs. global unfolding
  • Protein Science, 19, 693-702 (2010)

  • Y. Harada, Y. Tamura, and T. Endo
  • Identification of yeast Art5 as a multicopy suppressor for the mitochondrial translocator maintenance protein Tam41.
  • Biochem. Biophys. Res. Commun. 392, 228-233 (2010)

  • K. Yamano, S. Tanaka-Yamano, and T. Endo
  • Mdm10 as a dynamic constituent of the TOB/SAM complex directs coordinated assembly of Tom40.
  • EMBO Rep. 11, 187-193 (2010)


  • D. Maruyama, T. Endo, and S. Nishikawa
  • Bip-mediated polar nuclei fusion is essential for the regulation of endosperm nuclei proliferation in Arabidopsis thaliana.
  • Proc. Natl. Acad. Sci. USA 107, 1684-1689 (2010)

2009

  • S. Mano, T. Miwa, S. Nishikawa, T. Mimura, and M. Nishimura
  • Seeing is believing: on the use of image databases for visually exploring plant organelle dynamics.
  • Plant Cell Physiol. 50, 2000-2014 (2009)

  • H. Yamamoto, K. Fukui, H. Takahashi, S. Kitamura, T. Shiota, K. Terao, M. Uchida, M. Esaki, S. Nishikawa, T. Yoshihisa, K. Yamano, and T. Endo
  • Roles of TOM70 in import of presequence-containing mitochondrial proteins
  • J. Biol. Chem. 284, 31635-31646 (2009)

  • Dobrista, A. A., Nishikawa, S., Preuss, D., Urbanczyk-Wochniak, E., Sumner, L. W., Hammond, A., Carlson, A., and Swanson, R. J.
  • LAP3, a novel plant protein required for pollen development, is essential for proper exine formation.
  • Sex. Plant Reprod. 22,167-177(2009)

  • S. Kawano, K. Yamano, M. Naoe, T. Momose, K. Terao, S. Nishikawa, N. Watanabe, and T. Endo
  • Structural basis of yeast Tim40 as an oxidative translocator in the mitochondrial intermembrane space
  • Proc. Natl. Acad. Sci. USA 106,14403-14407(2009)

  • T. Endo and K. Yamano
  • Multiple pathways for mitochondrial protein traffic
  • Biol. Chem. 390, 723-730 (2009)

  • Y. Tamura, T. Endo, M. Iijima, and H.Sesaki
  • Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria
  • J. Cell Biol. 185, 1029-1045 (2009)

  • T. Endo
  • Control and alteration of protein traffic in the cell
  • in Systems Biology - The Challenge of Complexity
  • (eds. S. Nakanishi, R. Kageyama, and D. Watanabe) pp129-134, Elsevier Science, Amsterdam (2009)

  • M. Sakoh-Nakatogawa, S. Nishikawa, and T. Endo
  • Roles of protein disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in ER-associated degradation.
  • J. Biol. Chem. 284, 11815-11825 (2009)

  • Y. Tamura, Y. Harada, T. Shiota, K. Yamano, K. Watanabe, M. Yokota, H. Yamamoto, H. Sesaki, and T. Endo
  • Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import.
  • J. Cell Biol. 184, 129-141 (2009)

  • T. Oguro, K. Yagawa, T. Momose, T. Sato, K. Yamano, and T. Endo
  • Structural stabilities of different regions of the titin I27 domain contribute differently to unfolding upon mitochondrial protein import.
  • J. Mol. Biol. 385. 811-819 (2009)

2008

  • S. Nishikawa, A. Hirata, and T. Endo
  • Nuclear inner membrane fusion facilitated by yeast Jem1p is required for spindle pole body fusion but not for the first mitotic nuclear division during yeast mating.
  • Genes Cells, 13, 1185-1195 (2008)

  • M. Yamamoto, D. Maruyama, T. Endo, and S. Nishikawa
  • Arabidopsis thaliana has a set of J proteins in the endoplasmic reticulum that are conserved from yeast to animals and plants.
  • Plant Cell Physiol. 49, 1547-1562 (2008)

  • K. Yamano, M. Kuroyanagi-Hasegawa, M. Esaki, M. Yokota, and T. Endo
  • Step size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation
  • J. Biol. Chem. 283, 27325-27332 (2008)

  • S. Mano, T. Miwa, S. Nishikawa, T. Miura, and M. Nishimura
  • The plant organelles database (PODB): a collection of visualized plant organelles and protocols for plant organelle research.
  • Nucleic Acids Res. 36, D929-D937 (2008)

  • T. Makio, S. Nishikawa, T. Nakayama, H. Nagai, and T. Endo
  • Identification and characterization of a Jem1p ortholog of Candida albicans: dissection of Jem1p functions in karyogamy and protein quality control in Saccharomyces cerevisiae.
  • Genes Cells, 13, 1015-1026 (2008)

  • K. Yamano*, Y. Yatsukawa*, M. Esaki, A. E. A Hobbs, R. E. Jensen, and T. Endo
  • Tom20 and Tom22 share the common signal recognition pathway in mitochondrial protein import.
  • J. Biol. Chem. 283, 3799-3807 (2008)
  • * These authors contributed equally to this paper.

  • T. Saitoh, M. Igura, T. Obita, T. Ose, R. Kojima, K. Maenaka, T. Endo, and D. Kohda
  • Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states
  • EMBO J. 26, 4777-4787 (2007)

1991-2007

  • T. Momose, C. Ohshima, M. Maeda, T. Endo
  • Structural basis of functional cooperation of Tim15/Zim17 with yeast mitochondrial Hsp70.
  • EMBO Rep. 8, 664-670(2007)

  • T. Yoshihisa, C. Ohshima, K. Yunoki-Esaki, and T. Endo
  • Cytoplasmic splicing of tRNA in Saccharomyces cerevisiae
  • Genes Cells 12,285-297 (2007)

  • T. Yoshihisa
  • tRNA, new aspects in intracellular dynamics
  • Cell Mol. Life Sci 63, 1813-1818 (2006)

  • *Y. Tamura, *Y. Harada, K. Yamano, K. Watanabe, D. Ishikawa, C. Ohshima, S. Nishikawa, H. Yamamoto, and T. Endo
  • Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
  • J. Cell Biol. 174, 615-623(2006)
  • * : These authors contributed equally to this paper.

  • T. Sato, M. Esaki, J. M.Fernandez, and T. Endo
  • Comparison of the protein unfolding pathways between mitochondrial protein import and atomic force microscopy measurements
  • Proc. Natl. Acad. Sci. USA, 102, 17999-18004 (2005)

  • S.Nishikawa, G.M.Zinkl, R.J.Swanson, D.Maruyama and D.Preuss
  • Callose (β-1,3 glucan) is essential for Arabidopsis pollen wall patterning,but not tube growth
  • BMC Plant Biology. 5,22(2005)

  • S. Nishikawa, J.L. Brodsky, and K. Nakatsukasa
  • Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD).
  • J. Biochem. 137, 551-555 (2005)

  • A. Takano, T. Endo, and T. Yoshihisa
  • tRNA actively shuttles between the nucleus and cytosol in yeast.
  • Science 309, 140-142 (2005)

  • M. Igura, T. Ose, T. Obita, C. Sato, K. Maenaka, T. Endo, and D. Kohda
  • Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from ALDH
  • Acta Cryst Section F61, 514-517 (2005)

  • K. Yamano, D. Ishikawa, M. Esaki, and T. Endo
  • Phosphate carrier has an ability to be sorted to either the TIM22 pathway or TIM23 pathway for its import into yeast mitochondria.
  • J. Biol. Chem. 280, 10011-10017(2005)

  • H. Yamamoto, T. Momose, Y. Yatsukawa, C. Ohshima, D. Ishikawa, T. Sato, Y. Tamura, Y. Ohwa and T. Endo
  • Identification of a novel member of yeast mitochondrial Hsp70-associated motor and chaperone proteins that facilitates protein translocation across the inner membrane.
  • FEBS Lett. 579, 507-511 (2005)

  • T. Endo
  • Protein transport to and within plant chloroplasts
  • Endocytobiosis Cell Res. 15, 294-299 (2004)

  • K. Nakatsukasa, S. Okada, K. Umebayashi, R. Fukuda, S. Nishikawa, and T. Endo
  • Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast
  • J. Biol. Chem. 279, 49762-49772 (2004 )

  • M. Naoe, Y. Ohwa, D. Ishikawa, C. Ohshima, S. Nishikawa, H. Yamamoto, and T. Endo
  • Identification of Tim40 that mediates protein sorting to the mitochondrial intermembrane space
  • J. Biol. Chem. 279, 47815-47821 (2004)

  • M. Esaki, H. Shimizu, T. Ono, H. Yamamoto, T. Kanamori, S. Nishikawa, and T. Endo
  • Mitochondrial protein import: Requirement of the presequence elements and TOM components for precursor binding to the TOM complex
  • J. Biol. Chem. 279, 45701-45707 (2004)

  • D. Ishikawa, H. Yamamoto, Y. Tamura, K. Moritoh, and T. Endo
  • Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly
  • J. Cell Biol. 166, 621-627 (2004)

  • T. Asai, T. Takahashi, M. Esaki, S. Nishikawa, K. Ohtsuka, M. Nakai, and T. Endo
  • Re-investigation of the requirement of cytosolic ATP for mitochondrial protein import
  • J. Biol. Chem. 279, 19464-19470 (2004)

  • M. Esaki, T. Kanamori, S. Nishikawa, I. Shin, P. G. Schultz, and T. Endo
  • Tom40 protein import channel binds to non-native proteins and prevents their aggregation
  • Nature Struct. Biol. 10, 988-994 (2003)

  • T. Yoshihisa, K. Esaki, C. Ohshima, N. Tanaka, and T. Endo
  • Possibility of Cytoplasmic pre-tRNA Splicing: the Yeast tRNA Splicing Endonuclease Mainly Localizes on the Mitochondria
  • Mol. Biol. Cell<14, 3266-3279 (2003)

  • T. Endo, H. Yamamoto, and M. Esaki
  • Functional cooperation and separation of translocators in protein import into mitochondria, the double-membrane bounded organelles. (Commentary Article)
  • J. Cell Science 116. 3259-67 (2003)

  • T. Obita, T. Muto, T. Endo and D. Kohda
  • Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences.
  • J. Mol. Biol. 328, 495-504 (2003)

  • S. Nishikawa, Y. Terazawa, T. Nakayama, A. Hirata, T. Makio and T. Endo
  • Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion
  • J. Biol. Chem. 278, 9938-9943 (2003)

  • T. Endo
  • Mitochondrial protein flux
  • in Genome Science - Towards a New paradigm?
  • (eds. H. Yoshikawa, N. Ogasawara, and N. Satoh) pp27-32, Elsevier Science, Amsterdam (2002)

  • H. Yamamoto, M. Esaki, T. Kanamori, Y. Tamura, S. Nishikawa, and T. Endo :
  • Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes
  • Cell 111, 519-528 (2002)

  • A. Kawai, S. Nishikawa, A. Hirata, and T. Endo
  • Loss of the mitochondrial Hsp70 functions causes aggregation of mitochondria in yerast cells.
  • J. Cell Sci. 114, 3565-3574 (2001)

  • S. Nishikawa, S. W. Fewell, Y. Kato, J. L. Brodsky, and T. Endo
  • Molecular chaperones in the yeast ER maintain the solubility of proteins for retro-translocation and degradation.
  • J. Cell Biol. 153, 1061-1070 (2001)

  • K. Nakatsukasa, S. Nishikawa, N. Hosokawa, K. Nagata, and T. Endo
  • Mnl1p, an (alpha)-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins.
  • J. Biol. Chem. 276, 8635-8638(2001)

  • T. Muto, T. Obita, Y. Abe, T. Shodai, T. Endo, and D. Kohda
  • NMR identification of the Tom20 binding segment in mitochondrial presequences.
  • J. Mol. Biol. 306, 137-143 (2001)

  • Y. Abe, T.Shodai, T. Muto, K. Mihara, H. Torii, S. Nishikawa, T. Endo, and D. Kohda
  • Structural basis of presequence recognition by the mitochondrial protein receptor Tom20
  • Cell100, 551-560 (2000)

  • T. Kurihara, S. Hamamoto, R. E. Gimeno, C. A. Kaiser, R. Schekman, and T. Yoshihisa
  • Sec24p and Iss1p Function Interchangeably in Transport Vesicle Formation from the Endoplasmic Reticulum in Saccharomyces cerevisiae
  • Mol. Biol. Cell 11, 983-998 (2000)

  • K. Saeki, H. Suzuki, M. Tsuneoka, M. Maeda, R. Iwamoto, H. Hasuwa, S. Shida, T. Takahashi, M. Sakaguchi, T. Endo, Y Miura, E. Mekada, and K. Mihara
  • Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane.
  • J. Biol. Chem. 275, 31996-32002 (2000)

  • M. Esaki, T. Kanamori, S. Nishikawa, and T. Endo
  • Two distinct mechanisms drive protein translocation across the mitochndrial outer membrane in the late step of the cytochrome b2 import pathway
  • Proc. Natl. Acad. Sci. USA 96, 11770-11775 (1999)

  • T. Asai, Y. Shinoda, T. Nohara, T. Yoshihisa, and T. Endo
  • Sec-dependent pathway and ΔpH-dependent pathway do not share a common translocation pore in thylakoidal protein transport
  • J. Biol. Chem. 274, 20075-20078(1999)

  • T. Kanamori, S. Nishikawa, M. Nakai, I. Shin, P. G. Schultz, and T. Endo
  • Uncoupling of transfer of the presequence and unfolding of the mature domain in precursor translocation across the mitochondrial outer membrane
  • Proc. Natl. Acad. Sci. USA 96, 3634-3639 (1999)

  • Y. Kubo, T. Tsunehiro, S. Nishikawa, M. Nakai, E. Ikeda, A. Toh-e, N. Morishima, T. Shibata, and T. Endo
  • Two distinct mechanisms Operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system
  • J. Mol. Biol. 286, 447-464(1999)

  • M. Yoshida, T. Endo, K. Ito, N. Hosokawa, and K. Nagata
  • Dynamics and regulation of the stress response: meeting report on the stress response and molecular chaperones from Kyoto.
  • Cell Stress &amp; Chaperones 4, 66-74 (1999)

  • S. Nishikawa and T. Endo
  • Reinvestigation of the functions of the hydrophobic segment of Jem1p, a yeast endoplasmic reticulum membrane protein mediating nuclear fusion
  • Biochem. Biophys. Res. Commun. 244, 785-789(1998)

  • M. Oka, M. Nakai, T. Endo, C. R. Lim, Y. Kimata and K. Khono
  • Loss of hsp70-hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae.
  • J. Biol. Chem. 273, 29727-29737 (1998)

  • T. Nohara, T. Yoshihisa, M. Nakai, and T. Endo
  • Cloning and characterization of chloroplast SecY proteins
  • Photosynthesis: Mechanisms and Effects vol. IV, 3, 3115-3118
  • G. Gerab Kluwer (1998)

  • S. Nishikawa and T. Endo
  • The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion
  • J. Biol. Chem. 272, 12889-12892 (1997)

  • T. Endo
  • Roles of molecular chaperones in mitochondrial protein import
  • Molecular Chaperones in Proteins: Structure, Function, and Mode of Ation, 435-466
  • A. Fink and Y. Goto, Marcel Dekker Inc., New York(1997)

  • T. Endo
  • Assembly of thylakoid membrane proteins in chlorplasts
  • Membrane Proteins: Structure, Function and Expression Control, 191-197
  • N. Hamasaki and K. Mihara, Kyushu University Press / S. Karger AG, Fukuoka / Basel (1997)

  • T. Kanamori, S. Noshikawa, I. Shin, P. G. Schultz, and T. Endo
  • Probing the exviroment along the protein import pathways in yeast mitochondria by site-specific photocrosslinking
  • Proc. Natl. Acad. Sci. USA 94, 485-490 (1997)

  • J. Iwahashi, S.Yamazaki, T. Komiya, N. Nomura, S. Nishikawa, T. Endo, and K. Mihara
  • Analysis of the functional domain of the rat liver mitochondrial import receptor Tom20
  • J. Biol. Chem. 272, 18467-18472 (1997)

  • M. Sugita, H. Sugishita, T. Fujishiro, M. Tsuboi, C. Sugita, T. Endo, and M. Sugiura
  • Organization of a large gene cluster encoding ribosomal proteins in the cyanobacterium Synechococcus sp. strain PCC 6301: comparison of gene clusters among cyanobateria, eubacteria and chloroplast genomes.
  • Genes 195, 73-79 (1997)

  • T. Nohara, T. Asai, M. Nakai, M. Sugiura, and T. Endo
  • Cytochrome f encoded by the chloroplast genome is imported into thylakoids via the SecA-dependent pathway.
  • Biochem. Biophys. Res. Commun. 224, 474-478 (1996)

  • T. Endo, S. Mitsui, M. Nakai, and D. Roise
  • Binding of mitochondrial presequences to yeast cytosolic hsp70 depends on the amphiphilicity of the presequence.
  • J. Biol. Chem. 271, 4161-4167 (1996)

  • N. Pfanner, M. G. Douglas, T. Endo, N. J. Hoogenraad, R. E. Jensen, M. Meijer, W. Neupert, G.
  • Schatz, U. K. Schmitz, and G. C. Shore
  • Uniform nomenclature for the protein transport machinery of the mitochondrial membranes.
  • Trends Biochem. Sci. 21, 51-52 (1996)

  • T. Endo, T. Nohara, A. Goto, and M. Nakai
  • Roles of Sec proteins in protein transport within chloroplasts.
  • in: Research in Photosynthesis: from light to biosphere, vol. III (P. Mathis ed.) pp811-814,
  • Kluwer, Amsterdam. (1995)

  • M. Nakai, T. Nohara, D. Sugita, and T. Endo
  • Cloning and characterization of sec and ffh genes from the cyanobacterium Synechococcus PCC7942.
  • in: Research in Photosynthesis: from light to biosphere, vol. III (P. Mathis ed.) pp505-508,
  • Kluwer, Amsterdam. (1995)

  • M. Nakai and T. Endo
  • Identification of yeast MAS17 encoding the functional counterpart of the mitochondrial receptor complex protein MOM22 of Neurospora crassa.
  • FEBS Lett. 357, 202-206 (1995)

  • T. Endo, S. Mitsui and D. Roise
  • Mitochondrial presequences can induce aggregation of unfolded proteins.
  • FEBS Lett. 359, 93-96 (1995)

  • T. Nohara, M. Nakai, A. Goto, and T. Endo
  • Isolation and characterization of the cDNA for pea chloroplast SecA: evolutionary conservation of the bacterial-type SecA-dependent protein transport within chloroplasts.
  • FEBS Lett. 364, 305-308 (1995)

  • T. Endo, Y. Nakayama, and M. Nakai
  • Avidin fusion protein as a tool to generate a stable translocation intermediate spanning the mitochondrial membranes.
  • J. Biochem. 118, 753-759 (1995)

  • M. Nakai, K. Kinoshita, and T. Endo
  • Mitochondrial receptor complex protein: the intermembrane-space domain of yeast MAS17 is not essential for its targeting or function.
  • J. Biol. Chem. 270, 30571-30575 (1995)

  • M. Nakai, Y. Kato, E. Ikeda, A. Toh-e and T. Endo
  • Yge1p, a eukaryotic GrpE homolog, is localized in the mitochondrial matrix and interacts with mitochondrial hsp70.
  • Biochem. Biophys. Res. Commun. 200, 435-442 (1994)

  • M. Nakai, T. Nohara, D. Sugita and T. Endo
  • Identification and characterization of the SecA protein homologue in the cyanobacterium Synechococcus PCC7942.
  • Biochem. Biophys. Res. Commun. 200, 844-851 (1994)

  • T. Endo, M. Kawakami, A. Goto, T. America, P. Weisbeek and M. Nakai
  • Chloroplast protein import: chloroplast envelopes and thylakoids have different abilities to unfold proteins.
  • Eur. J. Biochem. 225, 403-409 (1994)

  • M. Nakai, A. Goto, T. Nohara, D. Sugita, and T. Endo
  • Identification of the SecA protein homolog in pea chloroplasts and its possible involvement in thylakoidal protein transport.
  • J. Biol. Chem. 269, 31338-31341(1994)

  • M. Nakai, T. Endo, T. Hase, Y. Tanaka, B. L. Trumpower, H. Ishiwatari, A. Asada, M. Bogaki, and H.Matsubara
  • Acidic regions of cytochrome c1 are essencial for ubiquinol-cytochrome c reductase activity in yeast cells lacking the acidic QCR6 protein
  • J. Biochem. (Tokyo) 114, 919-925 (1993)

  • M. Nakai, A. Takeda, M. L. Cleary, and T. Endo
  • The Bcl-2 protein is inserted into the outer membrane but not into the inner membrane of rat liver mitochondria in vitro
  • Biochem. Bophys. Res. Commun. 196, 233-239(1993)

  • M. Nakai, T. Endo, T. Hase, and H. Matsubara
  • Intermitochondrial protein sorting: isolation and characterization of the yeast MSP1 gene which belongs to a novel family of putative ATPase
  • <i>J. Biol. Chem.</i> 268, 24262-24269 (<b>1993</b>)

  • M. Nakai, T. Takada, and T. Endo
  • Cloning of the YAP19 gene encoding a putative yeast homolog of AP19, the mammalian small chain of the clathrin-assembly proteins
  • Biochem. Biophys. Acta 1174, 282-284(1993)

  • M. Nakai, D. Sugita, T. Omata, and T. Endo
  • SecY protein is localized in both the cytoplasmic and thylakoid membrane in the cyanobacterium Synechococcus PCC7942
  • Biochem. Biophys. Res. Commun. 193, 228-234(1993)

  • M. Nakai, A. Tanaka, T. Omata, and T. Endo
  • Cloning and characterization of secY gene from the cyanobacterium Synechococcus PC7942
  • Biochem. Biophys. Acta 1171, 113-116 (1992)

  • T. Endo, K. Kawamura, H. Torii, and M. Nakai
  • Conformation of the chloroplast-targeting domain of plastocyanin transit peptide and its interaction with lipid bilayers
  • Research in Photosynthesis, Vol. III, 181-184
  • Norio Murata, Kluwer, Amsterdam (1992)

  • T. Endo, K. Kawamura, and M. Nakai
  • Chloroplast targeting domain of plastocyanin transit peptide can form a herical structure but does not have a high affinity for lipid bilayers
  • Eur. J. Biochem. 207, 671-675 (1992)

  • T. Endo
  • Co-operative binding of hsp60 may promote transfer from hsp70 and correct folding of imported proteins in mitochondria
  • FEBS Lett. 293, 1-3(1991)

Review

  • Endo T, Tamura Y.
    Shuttle mission in the mitochondrial intermembrane space.
    EMBO J. 37(4). e98993 (2018)
    doi:10. 15252/embj. 201898993. Epub 2018 Jan 30.

  • Y.Tamura and T. Endo
    Role of intra- and inter-mitochondrial membrane contact sites in yeast phospholipid biogenesis
    Adv. Exp. Med. Biol. 997, 121-133 (2017)
    In "Organelle Contact Sites: From Molecular Mechanism to Disease, Advances in Experimental Medicine and Biology" (eds Mitsuo Tagaya, Thomas Simmen), Springer, pp121-133.

  • T. Endo, K. Yamano, and S. Kawano
    Structural insight into the mitochondrial protein import system
    Biochim. Biophys. Acta (Biomembranes) 1808, 955-970 (2011)

  • T. Endo and K. Yamano
    Transport of proteins across or into the mitochondrial outer membrane
    Biochim. Biophys. Acta (Molecular Cell Research), 1803, 706-714 (2010)

  • T. Endo, K. Yamano, and T. Yoshihisa
    Mitochondrial matrix reloaded with RNA
    Cell (Preview) 142, 362-363 (2010)

  • T. Endo, K. Yamano, and S. Kawano
    Structural basis for the disulfide relay system in the mitochondrial intermembrane space
    Antioxid. Redox Signal. 13, 1359-1373 (2010)


    • T. Endo and D. Kohda:
      Functions of outer membrane receptors in mitochondrial protein import (Review article).
      Biochim. Biophys. Acta 1592, 3-14 (2002)

日本語総説・著書

2018

  • 田村康,河野慎,遠藤斗志也
  • ミトコンドリアと小胞体間のオルガネラコンタクト
  • 生体の科学 69,577-580 (2018)

  • 河野慎,遠藤斗志也
  • (最新のトピックス)膜間コンタクトサイトで働く脂質輸送タンパク質:SMPドメインとSTART(-like)
  • 化学 73,66-67 (2018)

  • 田村康,河野慎,遠藤斗志也
  • ミトコンドリアと小胞体のクロストーク
  • 月刊細胞 50, No.8, 412-415 (2018)

  • 八木達彦, 遠藤斗志也, 神田大輔
  • 「化学の要点シリーズ25: 生化学の論理,物理化学の視点」
  • 共立出版(2018)

2017

  • 遠藤斗志也
  • ミトコンドリア蛋白質の配送機構
  • (週刊)医学のあゆみ 260, 37-41 (2017.1.7)

2016

  • 塩田拓也,遠藤斗志也
  • 作動するミトコンドリアタンパク質搬入口の分子構造
  • Japanese Scientists in Science 2015, 59 (2016)

  • 塩田拓也,今井賢一郎,遠藤斗志也
  • (カレントトピックス)部位特異的光架橋で明らかになったインテリジェントなミトコンドリアタンパク質膜透過機構
  • 実験医学 34,591-595 (2016)

2015

  • 塩田拓也,遠藤斗志也
  • ミトコンドリアタンパク質の入口の分子構造
  • ライフサイエンス新着レビュー (2015年10月20日)
  • DOI: 10.7875/first.author.2015.112

2013

  • 吉久 徹
  • tRNA型スプライシングの新展開
  • 生化学 85, 89-92 (2013)

  • 遠藤斗志也
  • (私のメンター) Gottfried Schatz ミトコンドリア生合成研究の先駆者
  • 実験医学 31, 937-942 (2013)

2012

  • 塩田拓也,西川周一, 遠藤斗志也
  • (Close Up実験法)動的なタンパク質相互作用の「スナップショット」を撮る〜in vivoにおける部位特異的光架橋法
  • 実験医学30, 1799-1805 (2012)

2010

  • 遠藤斗志也,山野晃史,原田佳宗,河野 慎
  • ミトコンドリアタンパク質の配送と機能化
  • 実験医学 28, 2059-2064 (2010)

2009

  • 遠藤斗志也,西川周一
  • 第8章 タンパク質の一生:誕生から死まで
  • 医学のための細胞生物学(永田和宏,塩田浩平編)83-96,南山堂(2009.8)

  • 吉久 徹
  • tRNAの「ダイナミクス」
  • 蛋白質核酸酵素 54, 2121-2126 (2009)

2008

  • 西川周一
  • カルボキシペプチダーゼY
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)921 (2008)

  • 遠藤斗志也
  • 局在化シグナル
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編) 925 (2008)

  • 遠藤斗志也
  • ジヒドロ葉酸レダクターゼ
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編) 941(2008)

  • 西川周一
  • 蛋白質ジスルフィドイソメラーゼ
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)966 (2008)

  • 遠藤斗志也
  • トランスロコン
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編) 976 (2008)

  • 遠藤斗志也
  • パワーストロークモデルとブラウニアンラチェットモデル
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編) 982 (2008)

  • 遠藤斗志也
  • ブルーネイティブ電気泳動
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編) 992 (2008)

  • 遠藤斗志也
  • ミトコンドリア
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編) 1008 (2008)

  • 遠藤斗志也
  • 両親媒性ヘリックス
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)1020 (2008)

  • 西川周一
  • Jem1p
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)1066 (2008)

  • 遠藤斗志也
  • TIM複合体
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)1093 (2008)

  • 遠藤斗志也
  • TOM複合体
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)1095 (2008)

  • 遠藤斗志也
  • βバレル型膜蛋白質
  • 「キーワード:蛋白質の一生」蛋白質核酸酵素2008年6月号増刊(遠藤斗志也,小椋光,永田和宏,森和俊,田口英樹,吉田賢右編)1103 (2008)

  • 遠藤斗志也
  • ミトコンドリアを舞台とするタンパク質の交通
  • 生物物理 48, 4-10 (2008)

1991-2007

  • 西川周一,遠藤斗志也
  • 3.8 ミトコンドリア (第III章 真核生物としての細胞体制)
  • 酵母のすべて:系統,細胞から分子まで (大隅良典,下田 親編) 65-76,シュプリンガージャパン(2007)

  • 吉久徹,遠藤斗志也
  • 4.1 細胞の構造:概論
  • 生物物理学ハンドブック (石渡信一,桂勲,桐野豊,美宅成樹編) 193-197,朝倉書店(2007)

  • 遠藤斗志也,吉久徹,森和俊,田口英樹
  • 研究の歴史:渾沌の前史から「タンパク質の一生」研究が開花するまで
  • タンパク質の一生:集中マスター(遠藤斗志也,森和俊,田口英樹編)12-23,羊土社(2007)

  • 遠藤斗志也,吉久徹,森和俊,田口英樹
  • ブレイクスルーとなった実験法を中心に:そのとき「タンパク質の一生」研究の歴史が動いた
  • タンパク質の一生:集中マスター (遠藤斗志也,森和俊,田口英樹編) 25-35,羊土社(2007)

  • 遠藤斗志也
  • ブローベル・コード:交通管制という問題
  • タンパク質の一生:集中マスター (遠藤斗志也,森和俊,田口英樹編) 58-66,羊土社(2007)

  • 遠藤斗志也
  • トランスロコンはどうやって組立てられるのか
  • タンパク質の一生:集中マスター (遠藤斗志也,森和俊,田口英樹編) 130,羊土社(2007)

  • 遠藤斗志也
  • 私のチャレンジしたい化学の未解決問題:オルガネラ構造を自在に操り自らの手で細胞をつくりたい
  • 化学62, 20-21 (2007)

  • 吉久 徹
  • tRNAの成熟化と細胞内ダイナミクス:RNAの一生における新展開
  • 蛋白質核酸酵素増刊「RNAと生命」51, 2568-2873 (2006)

  • 吉久 徹,高野 晃,遠藤斗志也
  • 核内tRNAの生理的意義
  • 蛋白質核酸酵素増刊「細胞核の世界」51, 2232-2234 (2006)

  • 吉久 徹
  • 核-細胞質間を行き来するtRNA
  • 蛋白質核酸酵素 51,48-53 (2006)

  • 西川周一,遠藤斗志也
  • 第11章(1) タンパク質の膜透過装置
  • タンパク質科学:構造,物性,機能, 485-494
  • 後藤祐児,桑島邦博,谷澤克行,化学同人 (2005)

  • 遠藤斗志也
  • 生体膜:脂質と二分子膜
  • 物質環境科学I「分子から機能性物質・生体まで」,208-225
  • 田隅三生,浜田嘉昭,放送大学教育振興会 (2005)

  • 遠藤斗志也
  • 生体膜:膜タンパク質と膜輸送
  • 物質環境科学I「分子から機能性物質・生体まで」,226-239
  • 田隅三生,浜田嘉昭,放送大学教育振興会 (2005)

  • 永田和宏,遠藤斗志也
  • 「タンパク質社会学」とは何か
  • 実験医学増刊23「細胞内タンパク質の社会学」(永田和宏,遠藤斗志也編),2213-2214 (2005)

  • 遠藤斗志也,永田和宏
  • 概論:タンパク質の一生とタンパク質社会学
  • 実験医学増刊23「細胞内タンパク質の社会学」(永田和宏,遠藤斗志也編),2228-2233 (2005)

  • 遠藤斗志也
  • 概説:タンパク質の配送・搬入とタンパク質が通る孔
  • 実験医学増刊23「細胞内タンパク質の社会学」(永田和宏,遠藤斗志也編),2272-2275 (2005)

  • 遠藤斗志也,山本林
  • ミトコンドリアの外膜内膜の孔
  • 実験医学増刊23(永田和宏,遠藤斗志也編),2297-2301 (2005)

  • 西川周一,遠藤斗志也
  • ミトコンドリアの膜透過装置
  • 細胞工学24,786-790 (2005)

  • 遠藤斗志也
  • ミトコンドリア内にタンパク質が取込まれる仕掛け
  • 現代化学 2月号,28-33 (2005)

  • 佐藤健大, 西川周一
  • ミトコンドリアへの輸送とフォールディング
  • 細胞工学 23, 1390-1393 (2004)

  • 西川周一,中務邦雄,遠藤斗志也
  • 小胞体品質管理におけるシャペロンと糖鎖の役割:何が異常で何を除去すべきか
  • 蛋白質核酸酵素増刊「細胞における蛋白質の一生」49, 988-991 (2004)

  • 遠藤斗志也,吉久徹
  • 総論 蛋白質の移動(真核生物):細胞内の交通管制システムがはたらく仕組み
  • 蛋白質核酸酵素増刊「細胞における蛋白質の一生」49, 877-888 (2004)

  • 遠藤斗志也,江崎雅俊,山本 林,吉久 徹
  • ミトコンドリアをめぐるタンパク質フラックス
  • 実験医学増刊「細胞内輸送研究の最前線」 21, 1889-1895 (2003)

  • 遠藤斗志也
  • 特集:細胞内タンパク質の運命と翻訳から分解までを監視・制御する細胞内システム
  • 序にかえて:細胞内タンパク質の運命
  • 実験医学 21, 866-868 (2003)

  • 山本 林・江崎雅俊・遠藤斗志也
  • ミトコンドリアトランスロケータの連係プレー:タンパク質配送の迷宮 2つの膜で囲まれたミトコンドリアの問題
  • 実験医学 21, 880-885 (2003)

  • 吉久 徹・遠藤 斗志也
  • 葉緑体包膜およびチラコイド膜を介する物質輸送とその制御
  • 朝倉植物生理学講座 3:光合成, 109-116
  • 佐藤公行, 朝倉書店 (2002)

  • 遠藤 斗志也
  • オルガネラ形成と分子シャペロン - 細胞が用意したタンパク質支援システム
  • 生物の科学 遺伝 14, 96-106 (2002)

  • 西川 周一
  • カリオガミー - 生殖における最後の関門
  • 生物の科学 遺伝 14, 127-137 (2002)

  • 遠藤斗志也・小代俊浩・江崎雅俊
  • ミトコンドリアへのタンパク質移行:難問/論争にいかに決着をつけたか
  • 実験医学 20, 7, 980-986 (2002)

  • 河合明美・西川周一・遠藤斗志也
  • ミトコンドリアの形態学
  • ミトコンドリアとミトコンドリア病
  • 日本臨床 60, 増刊号4, 9-13 (2002)

  • 西川 周一・遠藤 斗志也
  • 輸送:小胞体
  • 分子シャペロンによる細胞機能制御, 66-74
  • 永田和宏・森正敬・吉田賢右, シュプリンガー・フェアラーク東京(2001)

  • 吉久 徹・遠藤斗志也
  • 葉緑体の蛋白質輸送
  • 蛋白質核酸酵素 45, 139-146 (2000)

  • 中井正人、西川周一、遠藤斗志也
  • 分子シャペロン hsp70 とオルガネラ形成
  • 生化学 67, 108-122 (1995)

  • 遠藤斗志也
  • プロテイントラフィックの第一歩 - 生まれたタンパク質は,どこに,どうやって行けばよいのか
  • タンパク質の一生:タンパク質の誕生,成熟から死まで (シリーズ バイオサイエンスの新世紀2), 62-74
  • 中野明彦・遠藤斗志也, 共立出版 (2000)

  • 西川周一,遠藤斗志也
  • 6.2.5 酵母の細胞内構造体の調製法
  • 新版 微生物学実験法, 121-125
  • 大和田紘一・黒岩常祥・杉山純多・高橋秀夫・徳田 元・渡辺 信, 講談社サイエンティフィック (1999)

  • 遠藤斗志也
  • 葉緑体への輸送
  • 細胞内物質のダイナミズム, pp 65-73
  • 米田悦啓・中野明彦, 学会出版センター (1999)

  • 西川周一・遠藤斗志也
  • 無細胞蛋白質生合成系:蛋白質生産システム
  • 生物学実験法シリーズ: 遺伝子発現研究法, 43, 257-264
  • 江尻慎一郎・平秀晴・堤賢一・志村憲助, 学会出版センター (1999)

  • 西川周一・遠藤斗志也
  • IV オルガネラの機能解析 4 ミトコンドリア
  • 酵母ラボマニュアル 酵母分子細胞生物学実験法, pp.191-211
  • 山本正幸・大矢禎一, シュプリンガー・フェアラーク東京 (1998)

  • 野原哲矢・遠藤斗志也
  • in vitro転写・翻訳系を用いたタンパク質合成
  • 細胞工学別冊 9 (植物細胞工学シリーズ9), 37-45
  • 中村研三、西村幹夫、長谷俊治、前島正義 監修, 秀潤社 (1998)

  • 遠藤斗志也、淺井健好、金森崇、西川周一
  • ミトコンドリアへのターゲティングと膜透過
  • 細胞工学 6, 1275-1281 (1997)

  • 遠藤斗志也
  • 研究室へようこそ:名古屋大学理学部遠藤斗志也研究室
  • 化学 52, 39-42 (1997)

  • 遠藤斗志也
  • ミトコンドリアへのタンパク質輸送におけるストレスタンパク質の役割
  • 生体の科学 46, 324-327 (1995)

  • 遠藤斗志也
  • フレッシュマンのための分野別化学研究の見方、考え方:生物化学分野
  • in vitro と in vivo 実験の意味と限界を認識しよう
  • 化学 50, 210-212 (1995)

  • 遠藤斗志也
  • 1994 年の化学:タンパク質の水素原子交換を引き起こす「揺らぎ」の実体
  • 化学 49, 302-303 (1994)

  • 遠藤斗志也
  • ミトコンドリア移行
  • Annual Review 細胞生物学 1994, 32-44 (1994)
  • 矢原一郎、御子芝克彦、月田承一郎

  • 遠藤斗志也
  • 1993 年の化学:タンパク質のミトコンドリア内での仕分け経路
  • 化学 48, 68-69 (1993)

  • 遠藤斗志也
  • DHFR 融合タンパク質を用いたミトコンドリアタンパク質局在化機構の解析
  • 新生化学実験講座6 生体膜と膜輸送(下) 733-738, 東京化学同人、東京 (1992)

  • 遠藤斗志也
  • アンチフォールディング、アンフォールディングによるタンパク質の機能化
  • 高分子 40, 620-623 (1991)

  • 遠藤斗志也
  • 1991 年の化学:タンパク質の膜透過チャネルの電気生理学的な検出
  • 化学 46, 651 (1991)

  • 遠藤斗志也、中井正人
  • ミトコンドリア膜透過実験法
  • 蛋白質核酸酵素 36, 1951-1956 (1991)

  • 遠藤斗志也
  • ミトコンドリアタンパク質の膜透過のメカニズム:前駆体の高次構造変化、膜電位の役割など
  • 生物物理 31, 13-18 (1991)

  • 遠藤斗志也
  • 細胞内での蛋白質の折れたたみと局在化
  • 蛋白質核酸酵素 36, 28-36 (1991)