-最近の業績-

(年代の新しいものから順に記す:1996以降)

2017

Fujiki, Y.: Functional complementation (version 3.0). In: Encyclopedia of Life Sciences, John Wiley & Sons, Chichester, UK, in press. (2017).

Honsho, M., and Fujiki, Y.: Plasmalogen homeostasis: regulation of plasmalogen biosynthesis and its physiological consequence in mammals. FEBS Lett. Published online 7 July (2017). doi: 10.1002/1873-3468.12743.

Fujiki, Y., Miyata, N., Mukai, S., Okumoto, K., and Cheng, E.H.: BAK regulates catalase release from peroxisomes. Mol. Cell. Oncol. article e1306610(2017). doi: 10.1080/23723556.2017.1306610

Hossain, Md. S., Abe, Y., Ali, F., Youssef, M., Honsho, M., Fujiki, Y., and Katafuchi, T.: Reduction of ether-type glycerophospholipids, plasmalogens, by NF-κB signal leading to microglial activation. J. Neurosci. 37: 4074-4092 (2017). doi: 10.1523/JNEUROSCI.3941-15.2017

Honsho, M., Abe, Y., and Fujiki, Y.: .Plasmalogen synthesis is spatiotemporally regulated by sensing plasmalogens in the inner leaflet of plasma membranes. Sci. Rep. 7: article 43936 (2017). doi: 10.1038/srep43936

Abe, S., Nagai, T., Masukawa, M., Okumoto, K., Homma, Y., Fujiki, Y., and Mizuno. K.: Localization of NDR2 to peroxisomes and its role in ciliogenesis. J. Biol. Chem. 292: 4089-4098 (2017). doi: 10.1074/jbc.M117.775916

Imoto, Y., Abe, Y., Okumoto, K., Honsho, M., Kuroiwa, H., Kuroiwa, T., and Fujiki, Y.: Defining dynamin-based ring organizing center on the peroxisome-dividing machinery isolated from Cyanidioschyzon merolae. J. Cell Sci. 130: 709-721(2017). doi: 10.1083/jcb.201605002

Hosoi, K., Miyata, N., Mukai, S., Furuki, S., Okumoto, K., Cheng, E. H., and Fujiki, Y.: The VDAC2-BAK axis regulates peroxisomal membrane permeability. J. Cell Biol. 216: 433-455 (2016). doi: 10.1111/tra.12376

Yagita, Y., Shinohara, K., Abe, Y., Nakagawa, K., Al-Owain, M., Alkuraya, F. S, and Fujiki, Y.: Deficiency of a retinal dystrophy protein, acyl-CoA binding domain-containing 5 (ACBD5), impairs peroxisomal β-oxidation of very-long-chain fatty acids. J. Biol. Chem. 292: 691-705 (2017). doi: 10.1074/jbc.M116.760090

Kinoshita, N., Matsuura, A., and Fujiki, Y.: Peroxisome biogenesis: a novel inducible PEX19 splicing variant is involved in early stages of peroxisome proliferation.J. Biochem. 161: 297-308 (2017). doi: 10.1093/jb/mvw075

Honsho, M., and Fujiki, Y.: Analysis of plasmalogen synthesis in cultured cells. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 55-61 (2017). doi: 10.1007/978-1-4939-6937-1_6

Yamashita, S., Oku, M., Sakai, Y., and Fujiki, Y.: Experimental systems to study yeast pexophagy. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 249-255 (2017). doi: 10.1007/978-1-4939-6937-1_24

Liu,Y., Honsho, M., and Fujiki, Y.: In vitro PMP import analysis using cell-free synthesized PMP and isolated peroxisomes. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 207-212 (2017). doi: 10.1007/978-1-4939-6937-1_19

Okumoto, K., and Fujiki, Y.: Generation of peroxisome-deficient somatic animal cell mutants. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 319-327 (2017). doi: 10.1007/978-1-4939-6937-1_29

Okumoto, K., Honsho, M., Liu, Y., and Fujiki, Y.: Peroxisomal membrane and matrix protein import using a semi-intact mammalian cell system. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 213-219 (2017). doi: 10.1007/978-1-4939-6937-1_20

Yamashita, S., and Fujiki, Y.: Assessing pexophagy in mammalian cells. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 243-248 (2017). doi: 10.1007/978-1-4939-6937-1_23

Okumoto, K., Tamura, S., and Fujiki, Y.: Blue-Native PAGE: Applications to study peroxisome biogenesis. In: Schrader, M. (ed.) Peroxisomes: Methods and Protocols, Methods in Molecular Biology (Series Ed.: Walker, J.M.), Springer, Humana Press, New York, USA. 1595: pp. 197-205 (2017). doi: 10.1007/978-1-4939-6937-1_18

2016

Fujiki, Y.: Peroxisome biogenesis and human peroxisome-deficiency disorders.Proc. Jpn. Acad., Ser. B 92: 463-477 (2016). doi: 10.2183/pjab.92.463

Liu, Y., Yagita, Y., and Fujiki, Y.: The Pex19p- and Pex3p-dependent direct pathway imports divergent membrane proteins to peroxisomes. Traffic 17: 433-455 (2016). doi: 10.1111/tra.12376

Honsho, M., Yamashita,S., and Fujiki, Y.: Peroxisome homeostasis: mechanisms of division and selective degradation of peroxisomes in mammals. Biochim. Biophys. Acta-Mol. Cell Res. 1863: 984-991 (2016). doi: 10.1016/j.bbamcr.2015.09.032

2015

Honsho, M., Abe, Y., and Fujiki, Y.: Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis. J. Biol. Chem. 290: 28822-28833 (2015). doi: 10.1074/jbc.M115.656983

Fujiki, Y., Okumoto, K., and Honsho, M.: Protein Import into Peroxisomes: the principles and methods of studying (version 2.0). Encyclopedia of Life Sciences, John Wiley & Sons, Chichester, UK, Published online: April 14, (2015). doi: 10.1002/9780470015902.a0002618.pub2

Yoshida, Y., Niwa, H., Honsho, M., Itoyama, A., and Fujiki,Y.: Pex11p mediates peroxisomal proliferation by promoting deformation of the lipid membrane. Biol. Open 4: 710-721 (2015). doi: 10.1242/bio.201410801

Jiang, L., Hara-Kuge, S., Yamashita, S., and Fujiki, Y.: The peroxin Pex14p is the key component for coordinated autophagic degradation of mammalian peroxisomes by direct binding to LC3-II. Genes Cells 20: 36-49 (2015). doi: 10.1111/gtc.12198

2014

Tamura, S., Matsumoto, N., Takeba, R., and Fujiki, Y.: AAA peroxins and their recruiter Pex26p modulate the interactions of peroxins involved in peroxisomal protein import. J. Biol. Chem. 289: 24336-24346 (2014). doi: 10.1074/jbc.M114.588038

Miyauchi-Nanri, Y., Mukai, S., Kuroda, K., and Fujiki, Y.: Cul4A-DDB1-Rbx1 E3 ligase controls the quality of the PTS2 receptor Pex7p. Biochem. J. 463: 65-74 (2014). doi:10.1042/BJ20130861

Fujiki, Y., Okumoto, K., Mukai, S., Honsho, M., and Tamura, S.: Peroxisome biogenesis in mammalian cells. Front. Physiol. 5: 307 (2014). doi: 10.3389/fphys.2014.00307

Yamashita, S., Abe, K., Tatemichi, Y., and Fujiki, Y.: The membrane peroxin PEX3 induces peroxisome-ubiquitination-linked pexophagy. Autophagy 10: 1549-1564 (2014). doi: 10.4161/auto.29329

Noguchi, M., Honsho, M., Abe, Y., Toyama, R., Niwa, H., Sato, Y., Ghaedi, K., Rahmanifar, A., Shafeghati, Y., and Fujiki, Y.: Mild reduction of plasmalogens causes rhizomelic chondrodysplasia punctata: Functional characterization of a novel mutation. J. Hum. Genet. 59: 387-392 (2014). doi: 10.1038/jhg.2014.39

Okumoto, K., Noda, H., and Fujiki, Y.: Distinct modes of ubiquitination of peroxisome-targeting signal type 1 (PTS1)-receptor Pex5p regulate PTS1 protein import. J. Biol. Chem. 289: 14089-14108 (2014). doi: 10.1074/jbc.M113.527937

Abe, Y., Honsho, M., Nakanishi, H., Taguchi, R., and Fujiki, Y.: Very-long-chain polyunsaturated fatty acids accumulate in phosphatidylcholine of fibroblasts from patients with Zellweger syndrome and acyl-CoA oxidase1 deficiency. Biochim. Biophys. Acta-Mol. Cell Biol. Lipids 1841: 610-619 (2014). doi: 10.1016/j.bbalip.2014.01.001

Fujiki, Y., Itoyama, A., Abe, Y., and Honsho, M.: Molecular complex coordinating peroxisome morphogenesis. In: Brocard, C. and Hartig, A. (eds) Molecular machines involved in peroxisome biogenesis and maintenance, Springer-Verlag, Wien, Austria. pp. 391-401 (2014). doi: 10.1007/978-3-7091-1788-0

Fujiki, Y., Okumoto, K., Mukai, S., and Tamura, S.: Molecular basis for peroxisome biogenesis disorders. In: Brocard, C. and Hartig, A. (eds) Molecular machines involved in peroxisome biogenesis and maintenance, Springer-Verlag, Wien, Austria. pp. 91-110 (2014). doi: 10.1007/978-3-7091-1788-0

2013

Fujiki, Y.: Functional complementation. In: Encyclopedia of Life Sciences, John Wiley & Sons, Chichester, UK, Published online: November 2013, DOI: 10.1002/9780470015902.a0005676.pub2

Honsho, M., Asaoku, S., Fukumoto, K., and Fujiki, Y.: Topogenesis and homeostasis of fatty acyl-CoA reductase 1. J. Biol. Chem. 288: 34588-34598 (2013). doi: 10.1074/jbc.M113.498345

Itoyama, A., Michiyuki, S., Honsho, M., Yamamoto, T., Moser, A., Yoshida, Y., and Fujiki, Y.: Mff functions with Pex11pβ and DLP1 in peroxisomal fission. Biol. Open 2: 998-1006 (2013). doi: 10.1242/bio.20135298

Noguchi, M., Okumoto, K., and Fujiki, Y.: System to quantify the import of peroxisomal matrix proteins by fluorescence intensity. Genes Cells 18: 476-492 (2013). doi: 10.1111/gtc.12051

Yagita, Y., Hiromasa,T., and Fujiki, Y.: Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway. J. Cell Biol. 200: 651-666 (2013). doi: 10.1083/jcb.201211077.

Natsuyama, R., Okumoto, K., and Fujiki, Y.: Peroxisome targeting signal type-1 receptor, Pex5p, stabilizes Pex14p: Study using a newly isolated pex5 CHO cell mutant, ZPEG101. Biochem. J. 449: 195-207 (2013). doi: 10.1042/BJ20120911.

2012

Jung, D., Abu-Elheiga, L., Ayuzawa, R., Gu, Z., Shirakawa, T., Fujiki, Y., Nakatsuji, N., Wakil, S.J., and Uesugi, M.: Mislocalization and inhibition of acetyl-CoA carboxylase 1 by a synthetic small molecule. Biochem. J. 448: 409-416 (2012). doi: 10.1042/BJ20121158.

Otera, H., and Fujiki, Y.: Pex5p imports folded terameric catalase by interaction with Pex13p. Traffic 13: 1364-1377 (2012) .

Fujiki, Y., Yagita, Y., and Matsuzaki, T.: Peroxisome biogenesis disorders: molecular basis for impaired peoxisomal membrane assembly. Biochim. Biophys. Acta-Mol. Basis Dis. 1822: 1337-1342 (2012).

Umemoto., T., and Fujiki, Y.: Ligand-dependent nucleo-cytoplasmic shuttling of peroxisome proliferators-activated receptors, PPARα and PPARγ. Genes Cells 17: 576-596 (2012).

Kanzawa, N., shimozawa, N., Wanders, R.J.A., Ikeda, K., Murakami, Y., Waterham, H.R., Mukai, S., Fujita, M., Maeda, Y., Taguchi, R., Fujiki, Y., and Kinoshita, T.: Defective lipid remodeling of GPI anchors in peroxisomal disorders, Zellweger syndrome and rhizomelic chondrodysplasia punctata. J. Lipid Res. 53: 653-663(2012).

Itoyama, A., Honsho, M., Abe, Y., Moser, A., Yoshida, Y., and Fujiki, Y.: Docosahexaenoic acid mediates peroxisomal elongation, a prerequisite for peroxisome division. J. Cell Sci. 125: 589-602 (2012).

Miyata, N., Okumoto, K., Noguchi, M., Mukai, S., and Fujiki, Y.: AWP1/ZFAND6 functions in Pex5 export by interacting with Cys-monoubiquitinated Pex5 and Pex6 AAA ATPase. Traffic 13: 168-183 (2012).

Fujiki, Y., Nashiro, C., Miyata, N., Tamura, S., Okumoto, K.: New insights into dynamic and funcional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p in shuttling of PTS1-receptor Pex5p during peroxisome biogenesis. Biochim. Biophys. Acta-Mol. Cell Biol. 1823:145-149 (2012).

2011

Okumoto, K., Kametani, Y., and Fujiki, Y.: Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid β-oxidation in peroxisomal matrix. J. Biol. Chem. 286: 44367-44379 (2011). doi: 10.1074/jbc.M111.285197.

Yonekawa, S., Furuno, A., Baba, T., Fujiki, Y., Ogasawara, Y., Yamamoto, A., Tagaya, M., and Tani, K.: Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells. Proc. Natl. Acad. Sci. USA 108: 12746-12751 (2011).

Okumoto, K., Misono, S., Miyata, N., Matsumoto, Y., Mukai, S., and Fujiki, Y.: Cysteine-ubiquitination of peroxisome-targeting-signal type 1 (PTS1)-receptor Pex5p regulated Pex5p recycling. Traffic 12: 1067-1083 (2011).

Nashiro, C., Kashiwagi, A., Matsuzaki, T., Tamura, S., and Fujiki, Y.: Recruiting mechanism of the AAA peroxins, Pex1p and Pex6p, to Pex26p on peroxisome membrane. Traffic 12: 774-788 (2011).

Fujiki, Y.: Peroxisome biogenesis Disorders. In: Encyclopedia of the Life Sciences, pp. 1-9, John Wiley & Sons, Chichester, UK (2011).

Iwamoto, F., Umemoto, T., Motojima, K., and Fujiki, Y.: Nuclear transport of peroxisome-proliferator activated receptor a. J. Biochem. 149: 311-319 (2011).

Honsho, M., Hashiguchi, Y., Ghaedi, K., and Fujiki, Y.: Interaction defect of the medium isoform of PTS1-receptor Pex5p with PTS2-receptor Pex7p abrogates the PTS2 protein import into peroxisomes in mammals. J. Biochem. 149: 203-210 (2011).

2010

Yano, T., Oku, M., Akeyama, N., Itoyama, A., Yurimoto, H., Kuge, S., Fujiki, Y., and Sakai, Y.: A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes. Mol. Cell. Biol. 30: 3758-3766 (2010).

Su, J.R., Takeda, K., Tamura, S., Fujiki, Y., and Miki, T.: Monomer-dimer transition of the conserved N-terminal domain of the mammalian peroxisomal matrix protein import receptor, Pex14p. Biochem. Biophys. Res. Commun. 394: 217-221 (2010).

Honsho, M., Asaoku, S., and Fujiki, Y.: Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis. J. Biol. Chem. 285: 8537-8542 (2010).

2009

Miyata, N., Hosoi, K., Mukai, S. and Fujiki, Y.: In vitro import of peroxisome-targeting signal type 2 (PTS2) receptor Pex7p into peroxisomes. Biochim. Biophys. Acta-Mol. Cell Res. 1793: 860-870 (2009).

Su, J.R., Takeda, K., Tamura, S., Fujiki, Y., and Miki, T.: Crystal structure of the conserved N-terminal domain of the peroxisomal matrix protein import receptor, Pex14p. Proc. Natl. Acad. Sci. USA 106: 417-421 (2009).

2008

Matsuzaki, T., and Fujiki, Y.: The peroxisomal membrane-protein import receptor Pex3p is direcly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway. J. Cell Biol. 183: 1275-1286 (2008).

Chalupnikova, K., Lattmann, S., Selak, N., Iwamoto, F., Fujiki, Y., and Nagamine, Y.: Recruitment of the RNA helicase RHAU to stress granules via a unique RNA-binding domain. J. Biol. Chem. 283: 35186-35198 (2008).

Hara-Kuge, S., and Fujiki, Y.: The peroxin Pex14p is involved in LC3-dependent degradation of mammalian peroxisomes. Exp. Cell Res. 314: 3531-3541 (2008).

Honsho, M., Yagita, Y., Kinoshita, N., and Fujiki, Y.: Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: Localization and transport of plasmalogens to post-Golgi compartments. Biochim. Biophys. Acta-Mol. Cell Res. 1783: 1857-1865 (2008).

Ghaedi, K., and Fujiki, Y.: Isolation and characterization of novel phenotype CHO cell mutants defective in peroxisome assembly, using ICR191 as a Potent mutagenic agent. Cell Biochem. Funct. 26: 684-691 (2008).

Sato, Y., Shibata, H., Nakano, H, Matsuzono, Y., Kashiwayama, Y., Kobayashi, Y., Fujiki, Y., Imanaka, T., and Kato, H.: Characterization of the interaction between recombinant human peroxin Pex3p and Pex19p: Identification of TRP104 in Pex3p as a Critical residue for the interaction. J. Biol. Chem. 283: 6136-6144 (2008).

Fujiki, Y., Miyata, N., Matsumoto, N., and Tamura, S.: Dynamic and Functional assembly of the AAA peroxins, Pex1p and Pex6p, their membrane receptor Pex26p involved in shuttling of th PTS1 receptor Pex5p in peroxisome biogenesis. Biochem. Soc. Trans. 36: 109-113 (2008).

2007

Saito, M., Horikawa, M., Iwamori, Y., Sakakihara, Y., Mizuguchi, M., Igarashi, T., Fujiki, Y., and Iwamori, M.: Alterations in the molecular species of plasmalogen phospholipids and glycolipids due to peroxisomal dysfunction in Chinese hamster ovary-mutant Z65 cells by FABMS method. J. Chromatogr. B 852: 367-373 (2007).

Kobayashi, S., Tanaka, A., and Fujiki, Y.: Fis1, DLP1, and Pex11p coordinately regulate peroxisome morphogenesis. Exp. Cell Res. 313: 1675-1686 (2007).

2006

Fujiki, Y,, Matsuzono, Y., Matsuzaki, T. and Fransen, M.: Import of peroxisomal membrane proteins: the interplay of Pex3p- and Pex19p-mediated interactions. Biochim. Biophys. Acta-Mol. Cell Res. 1763: 1639-1646 (2006).

Fujiki, Y. Okumoto, K., Kinosita, N., and Ghaedi, K.: Lessons from peroxisome-deficient Chinese hamster ovary (CHO) cell mutants. Biochim. Biophys. Acta-Mol. Cell Res. 1763: 1374-81 (2006).

Mukai, S., and Fujiki, Y.: Molecular mechanisms of import of peroxisome-targeting-signal type 2 (PTS2)-proteins by PTS2-receptor Pex7p and PTS1-receptor Pex5pL. J. Biol. Chem. 281: 37311-37320 (2006).

Tamura, S., Yasutake, S., Matsumoto, N., and Fujiki, Y.: Dynamic and functional assembly of the AAA peroxins, Pex1p and Pex6p, and their membrane receptor Pex26p. J. Biol. Chem. 281: 27693-27704 (2006).

Matsuzono, Y., Matsuzaki, T., and Fujiki, Y.: Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation. J. Cell Sci. 119: 3539-3550 (2006).

Fan, W., and Fujiki, Y.: A temperature-sensitive CHO pex1 mutant with a novel mutation in the AAA Walker A1 motif. Biochem. Biophys. Res. Commun. 345: 1434-1439 (2006).

Itoh, R., and Fujiki, Y.: Functional domains and dynamic assembly of the Peroxin Pex14p, the entry site of matrix proteins. J. Biol. Chem. 281: 10196-10205 (2006).

Tanaka, A., Kobayashi, S., and Fujiki, Y.: Peroxisome division is impaired in a CHO cell mutant with an inactivating point-mutation in dynamin-like protein 1 gene. Exp. Cell Res. 312: 1671-1684 (2006). *Adopted as 'Highlight paper'

Furuki, S., Tamura, S., Matsumoto, N., Miyata, N., Moser, A., Moser, H.W., and Fujiki, Y.: Mutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with Pex1p-Pex6p complex. J. Biol. Chem. 281: 1317-1323 (2006).

Matsuzono, Y., and Fujiki, Y.: In vitro transport of membrane proteins to peroxisomes by shuttling receptor Pex19p. J. Biol. Chem. 281: 36-42 (2006).

2005

Miyata, N., and Fujiki, Y.: Shuttling mechanism of peroxisome targeting signal type 1 receptor, Pex5p: ATP-independent import and ATP-dependent export. Mol. Cell. Biol. 25: 10822-10832 (2005).

2004

Ishizuka, M., Toyama, Y., Watanabe, H., Fujiki, Y., Takeuchi, A., Yamasaki, S., Yuasa, S., Miyazaki, M., Nakajima, N., Taki, S., and Saito, T.: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp. Cell Res. 297: 127-141 (2004).

2003

Matsumoto, N., Tamura, S., Furuki, S., Miyata, N., Moser, A., Shimozawa, N., Moser, H.W., Suzuki, Y., Kondo, N., and Fujiki, Y.: Mutations in novel peroxin gene PEX26 that cause peroxisome biogenesis disorders of complementation group 8 provide a genotype-phenotype correlation. Am. J. Hum. Genet. 73: 233-246 (2003).

Matsumoto, N., Tamura, S., and Fujiki, Y.: The pathogenic peroxin Pex26p recruits the Pex1p-Pex6p AAA-ATPase complexes to peroxisomes. Nat. Cell Biol. 5: 454-460 (2003).

Tanaka, A., Okumoto, K., and Fujiki, Y.: cDNA cloning and characterization of the third isoform of human peroxin Pex11p. Biochem. Biophys. Res. Commun. 300: 819-823 (2003).

Fujiki, Y.: Functional complementation. In: nature Encyclopedia of the Human Genome, Cooper, D.N. ed., vol. 2, pp. 539-543, Nature Publishing Group, London (2003).

Fujiki, Y.: Peroxisome biogenesis disorders. In: nature Encyclopedia of the Human Genome, Cooper, D.N. ed., vol. 4, pp. 541-547, Nature Publishing Group, London (2003).

2002

Honsho, M., Hiroshige, T., and Fujiki, Y.: The membrane biogenesis peroxin Pex16p: topogenesis and functional roles in peroxisomal membrane assembly. J. Biol. Chem. 277: 44513-44524 (2002).

Saito, M., Fukushima, Y., Tatsumi, K., Bei, L., Fujiki, Y., Iwamori, M., Igarashi, T., and Sakakihara, Y.: Molecular cloning of Chinese hamster ceramide glucosyltransferase and its enhanced expression in peroxisome-defective mutant Z65 cells. Arch. Biochem. Biophys. 403: 171-178 (2002).

Akiyama, N., Ghaedi, K., and Fujiki, Y.: A novel pex2 mutant: catalase-deficient but temperature-sensitive PTS1 and PTS2 import. Biochem. Biophys. Res. Commun. 293: 1523-1529 (2002).

Yanago, E., Hiromasa, T., Matsumura, T., Kinoshita, N., and Fujiki, Y.: Isolation of Chinese hamster ovary cell pex mutants: two PEX7-defective mutants. Biochem. Biophys. Res. Commun. 293: 225-230 (2002).

Shimozawa, N., Nagase, T., Takemoto, Y., Suzuki, Y., Fujiki, Y., Wanders, R.J.A.. and Kondo, N.: A novel aberrant splicing mutation of the PEX16 gene in two patients with Zellweger syndrome. Biochem. Biophys. Res. Commun. 292: 109-112 (2002).

Otera, H., Setoguchi, K., Hamasaki, M., Kumashiro, T., Shimizu, N., and Fujiki, Y.: Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. Mol. Cell. Biol. 22: 1639-1655 (2002).

Mukai, S., Ghaedi, K., and Fujiki, Y.: Intracellular localization, function, and dysfunction of the peroxisome-targeting signal type 2 receptor, Pex7p, in mammalian cells. J. Biol. Chem. 277: 9548-9561 (2002).

Fujiki, Y. Peroxisome assembly and peroxisome biogenesis disorders. In: Genome Science - Towards a New Paradaigm? (International Congress Series 1246) (H. Yoshikawa, N. Ogasawara, and N. Satoh, eds) pp 33-42 (Elsevier Science Amsterdam) (2002).

2001

Suzuki, Y., Shimozawa, N., Orii, T., Tsukamoto, T., Osumi, T., Fujiki, Y., and Kondo, N.: Genetic and molecular bases of peroxisome biogenesis disorders. Genet. Med. 3: 372-376 (2001).

Tamura, S., Matsumoto, N., Imamura, A., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Phenotype-genotype relationships in peroxisome biogenesis disorders of PEX1-defective complementation group 1 are defined by Pex1p-Pex6p interaction. Biochem. J. 357: 417-426 (2001).

Harano, T., Nose, S., Uezu, R., Shimizu, N., and Fujiki, Y.: Hsp70 regulates interaction of theperoxisome targeting signal type 1 (PTS1)-receptor Pex5p and PTS1. Biochem. J. 357: 157-165 (2001).

Matsumoto, N., Tamura, S., Moser, A., Moser, H.W., Braverman, N., Suzuki, Y., Shimozawa, N., Kondo, N., and Fujiki, Y.: The peroxin Pex6p gene is impaired in peroxisome biogenesis disorders of complementation group 6. J. Hum. Genet. 46: 273-277 (2001).

Honsho, M., and Fujiki, Y.: Topogenesis of peroxisomal membrane protein requires a short, positively charged intervening-loop sequence and flanking hydrophobic segments: STUDY USING HUMAN MEMBRANE PROTEIN PMP34. J. Biol. Chem. 276: 9375-9382 (2001).

Otera, H., Nishimura, M., Setoguchi, K., Mori, T., and Fujiki, Y.: Biogenesis of nonspecific lipid transfer protein and sterol carrier protein x: STUDIES USING PEROXISOME ASSEMBLY-DEFECTIVE pex CELL MUTANTS. J. Biol. Chem. 276: 2858-2864 (2001).

2000

Fujiki, Y., Okumoto, K., Otera, H., and Tamura, S.: Peroxisome biogenesis and molecular defects in peroxisome assembly disorders. Cell Biochem. Biophys. 32: 155-164 (2000).

Imamura, A., Shimozawa, N., Suzuki, Y., Zhang, Z., Tsukamoto, T., Fujiki, Y., Orii, T., Osumi, T., Wanders, R.J., and Kondo, N.: Temperature-sensitive mutation of PEX6 in peroxisome biogenesis disorders in complementation group C (CG-C): comparative study of PEX6 and PEX1. Pediatr. Res. 48: 541-545 (2000).

Ghaedi, K., Honsho, M., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: PEX3 is the causal gene responsible for peroxisome membrane assembly-defective Zellweger syndrome of complementation group G. Am. J. Hum. Genet. 67: 976-981 (2000).

Shimozawa, N., Suzuki, Y., Zhang, Z., Imamura, A., Ghaedi, K., Fujiki, Y., and Kondo, N.: Identification of PEX3 as the gene mutated in a Zellweger syndrome patient lacking peroxisomal remnant structures. Hum. Mol. Genet. 9: 1995-1999 (2000).

Fujiki, Y.: Review: Peroxisome biogenesis and peroxisome biogenesis disorders. FEBS Lett. 476: 42-46 (2000).

Ghaedi, K., Tamura, S., Okumoto, K., Matsuzono, Y., and Fujiki, Y.: The peroxin Pex3p initiates membrane assembly in peroxisome biogenesis. Mol. Biol. Cell 11: 2085-2102 (2000).

Okumoto, K., Abe, I., and Fujiki, Y.: Molecular anatomy of the Peroxin Pex12p: RING finger domain is essential for the Pex12p function and interacts with the peroxisome targeting signal type1-receptor Pex5p and a RING peroxin, Pex10p. J. Biol. Chem. 275: 25700-25710 (2000).

Matsumura, T., Otera, H., and Fujiki, Y.: Disruption of interaction of the longer iso form of Pex5p, Pex5pL, with Pex7p abolishes the PTS2 protein import in mammals. Study with a novel PEX5-impaired Chinese hamster ovary cell mutant. J. Biol. Chem. 275: 21715-21721 (2000).

Otera, H., Harano, H., Honsho, M., Tanaka, A., Kawai, A., Shimizu, N., and Fujiki, Y.: Pex5pL, the longer isoform of mobile PTS1-receptor, functions in a novel and pivotal, Pex7p-mediated PTS2 import pathway via its initial docking site Pex14p. J. Biol. Chem. 275: 21703-21714 (2000).

Imamura, A., Shimozawa, N., Suzuki, Y., Zhang, Z., Tsukamoto, T., Fujiki, Y., Orii, T., Osumi, T., and Kondo, N.: Restoration of biochemical function of the peroxisome in the temperature-sensitive mild forms of peroxisome biogenesis disorder in humans. Brain Dev. 22: 8-12 (2000).

Shimozawa, N., Zhang, Z., Imamura, A., Suzuki, Y., Fujiki, Y., Tsukamoto, T., Osumi, T., Aubourg, P., Wanders, R.J., and Kondo, N.: Molecular mechanism of detectable catalase-containing particles, peroxisomes, in fibroblasts from a PEX2-defective patient. Biochem. Biophys. Res. Commun. 268: 31-35 (2000).

1999

Shimozawa, N., Imamura, A., Zhang, Z., Suzuki, Y., Orii, T., Tsukamoto, T., Osumi, T., Fujiki, Y., Wanders, R.J., Besley, G., and Kondo, N.: Defective PEX gene products correlate with the protein import, biochemical abnormalities, and phenotypic heterogeneity in peroxisome biogenesis disorders. J. Med. Genet. 36: 779-781 (1999).

Shimozawa, N., Zhang, Z., Suzuki, Y., Imamura, A., Tsukamoto, T., Osumi, T., Fujiki, Y., Orii, T., Barth, P.G., Wanders, R.J., and Kondo, N.: Functional heterogeneity of C-terminal peroxisome targeting signal 1 in PEX5-defective patients. Biochem. Biophys. Res. Commun. 262: 504-508 (1999).

Toyama, R., Mukai, S., Itagaki, A., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., Wanders, R.J.A., and Fujiki, Y.: Isolation, characterization, and mutation analysis of PEX13-defective Chinese hamster ovary cell mutants. Hum. Mol. Genet. 8: 1673-1681 (1999).

Zhang, Z., Suzuki, Y., Shimozawa, N., Fukuda, S., Imamura, A., Tsukamoto, T., Osumi, T., Fujiki, Y., Orii, T., Wanders, R.J., Barth, P.G., Moser, H.W., Paton, B.C., Besley, G.T., and Kondo, N.: Genomic structure and identification of 11 novel mutations of the PEX6 (peroxisome assembly factor-2) gene in patients with peroxisome biogenesis disorders. Hum. Mutat. 13: 487-496 (1999).

Harano, T., Shimizu, N., Otera, H., and Fujiki, Y.: Transmembrane topology of the peroxin Pex2p, an essential component of peroxisome assembly. J. Biochem. 125: 1168-1174 (1999).

Shimozawa, N., Suzuki, Y., Zhang, Z., Imamura, A., Toyama, R., Mukai, S., Fujiki, Y., Tsukamoto, T., Osumi, T., Orii, T., Wanders, R.J., and Kondo, N.: Nonsense and temperature-sensitive mutations in PEX13 are the cause of complementation group H of peroxisome biogenesis disorders. Hum. Mol. Genet. 8: 1077-1083 (1999).

Ghaedi, K., Kawai, A., Okumoto, K., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Isolation and characterization of novel peroxisome biogenesis-defective Chinese hamster ovary cell mutants using green fluorescent protein. Exp. Cell Res. 248: 489-497 (1999).

Ghaedi, K., Itagaki, A., Toyama, R., Tamura, S., Matsumura, T., Kawai, A., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Newly identified Chinese hamster ovary cell mutants defective in peroxisome assembly represent complementation group A of human peroxisome biogenesis disorders and one novel group in mammals. Exp. Cell Res. 248: 482-488 (1999).

Saito, M., Iwamori, M., Lin, B., Oka, A., Fujiki, Y., Shimozawa, N., Kamoshita, S., Yanagisawa, M., and Sakakihara, Y.: Accumulation of glycolipids in mutant Chinese hamster ovary cells (Z65) with defective peroxisomal assembly and comparison of the metabolic rate of glycosphingolipids between Z65 cells and wild-type CHO-K1 cells. Biochim. Biophys. Acta 1438: 55-62 (1999).

Shimizu, N., Itoh, R., Hirono, H., Otera, H., Ghaedi, K., Tateishi, K., Tamura, S., Okumoto, K., Harano, T., Mukai, S., and Fujiki, Y.: The Peroxin Pex14p: cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis. J. Biol. Chem. 274: 12593-12604 (1999).

Matsuzono, Y., Kinoshita, N., Tamura, S., Shimozawa, N., Hamasaki, M., Ghaedi, K., Wanders, R. J. A., Suzuki, Y., Kondo, N., and Fujiki, Y.: Human PEX19: cDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome and potential role in peroxisomal membrane assembly. Proc. Natl. Acad. Sci. USA 96: 2116-2121 (1999).

1998

Shimozawa, N., Suzuki, Y., Zhang, Z., Imamura, A., Kondo, N., Kinoshita, N., Fujiki, Y., Tsukamoto, T., Osumi, T., Imanaka, T., Orii, T., Beemer, F., Mooijer, P., Dekker, C., and Wanders, R.J.A.: Genetic basis of peroxisome assembly mutants of humans, CHO cells and yeast: identification of a new complementation group of peroxisome biogenesis disorders, absent from peroxisomal membrane ghosts. Am. J. Hum. Genet. 63: 1898-1902 (1998).

Honsho, M., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y.: Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D. Am. J. Hum. Genet. 63: 1622-1630 (1998).

Abe, I., and Fujiki, Y.: cDNA cloning and characterization of a constitutively expressed isoform of the human peroxin Pex11p. Biochem. Biophys. Res. Commun. 252: 529-533 (1998).

Imamura, A., Tamura, S., Shimozawa, N., Suzuki, Y., Zhang, Z., Tsukamoto, T., Orii, T., Kondo, N., Osumi, T., and Fujiki, Y.: Temperature-sensitive mutation in PEX1 moderates the phenotypes of peroxisome deficiency disorders. Hum. Mol. Genet. 7: 2089-2094 (1998).

Kinoshita, N., Ghaedi, K., Shimozawa, N., Wanders, R. J. A., Matsuzono, Y., Imanaka, T., Okumoto, K., Suzuki, Y., Kondo, N., and Fujiki, Y.: Newly identified Chinese hamster ovary cell mutants are defective in biogenesis of peroxisomal membrane vesicles (peroxisomal ghosts), representing a novel complementation group in mammals. J. Biol. Chem. 273: 24122-24130 (1998).

Abe, I., Okumoto, K., Tamura, S., and Fujiki, Y.: Clofibrate-inducible, 28-kDa peroxisomal integral membrane protein is encoded by PEX11. FEBS Lett. 431: 468-472 (1998).

Okumoto, K., Itoh, R., Shimozawa, N., Suzuki, Y., Tamura, S., Kondo, N., and Fujiki, Y.: Mutation in PEX10 is the cause of Zellweger peroxisome-deficiency syndrome of complementation group B. Hum. Mol. Genet. 7: 1399-1405 (1998).

Okumoto, K., Shimozawa, N., Kawai, A., Tamura, S., Tsukamoto, T., Osumi, T., Moser, H., Wanders, R.J.A., Suzuki, Y., Kondo, N., and Fujiki, Y.: PEX12, the pathogenic gene of group III Zellweger syndrome: cDNA cloning by functional complementation on a CHO cell mutant, patient analysis, and characterization of Pex12p. Mol. Cell. Biol. 18: 4324-4336 (1998).

Imamura, A., Tsukamoto, T., Shimozawa, N., Suzuki, Y., Zhang, Z., Imanaka, T., Fujiki, Y., Orii, T., Kondo, N., and Osumi, T.: Temperature-sensitive phenotypes of peroxisome-assembly processes represent the milder forms of human peroxisome-biogenesis disorders. Am. J. Hum. Genet. 62: 1539-1543 (1998).

Tamura, S., Shimozawa, N., Suzuki, Y., Tsukamoto, T., Osumi, T., and Fujiki, Y.: A cytoplasmic AAA family peroxin, Pex1p, interacts with Pex6p. Biochem. Biophys. Res. Commun. 245: 883-886 (1998).

Tamura, S., Okumoto, K., Toyama, R., Shimozawa, N., Tsukamoto, T., Suzuki, Y., Osumi, T., Kondo, N., and Fujiki, Y.: Human PEX1 cloned by functional complementation on a CHO cell mutant is responsible for peroxisome-deficient Zellweger syndrome of complementation group I. Proc. Natl. Acad. Sci. USA 95: 4350-4355 (1998).

Shimozawa, N., Suzuki, Y., Zhang, Z., Imamura, A., Tsukamoto, T., Osumi, T., Tateishi, K., Okumoto, K., Fujiki, Y., Orii, T., Barth, P.G., Wanders, R.J., and Kondo, N.: Peroxisome biogenesis disorders: identification of a new complementation group distinct from peroxisome-deficient CHO mutants and not complemented by human PEX 13. Biochem. Biophys. Res. Commun. 243: 368-371 (1998).

Shimozawa, N., Suzuki, Y., Tomatsu, S., Nakamura, H., Kono, T., Takada, H., Tsukamoto, T., Fujiki, Y., Orii, T., and Kondo, N.: A novel mutation, R125X in peroxisome assembly factor-1 responsible for Zellweger syndrome. Hum. Mutat. Suppl. 1: S134-136 (1998).

Otera, T., Okumoto, K., Tateishi, K., Ikoma, Y., Matsuda, E., Nishimura, M., Tsukamoto, T., Osumi, T., Ohashi, K., Higuchi, O., and Fujiki, Y.: Peroxisome targeting signal type 1 (PTS1)- receptor is involved in import of both PTS1 and PTS2: Studies with PEX5-defective CHO cell mutants. Mol. Cell. Biol. 18: 388-399 (1998).

1997

Fujiki, Y.: Peroxisome biogenesis and peroxisome assembly disorders. In Membrane Proteins: Structure, Function and Expression Control (Mihara, K. and Hamasaki, N. eds.), Karger Press, Basel, pp.53-61 (1997) .

Fujiki, Y.: Review: Molecular defects in genetic diseases of peroxisomes. Biochim. Biophys. Acta 1361: 235-250 (1997).

Okumoto, K., and Fujiki, Y.:PEX12 encodes an integral membrane protein of peroxisomes. Nat. Genet. 17: 265-266 (1997).

Tateishi, K., Okumoto, K., Shimozawa, N., Tsukamoto, T., Osumi, T., Suzuki, Y., Kondo, N., Okano, I., and Fujiki, Y.: Newly identified CHO cell mutants defective in peroxisome biogenesis represent two novel complementation groups in mammals. Eur. J. Cell Biol. 73: 352-359 (1997).

Okumoto, K., Bogaki, A., TateishiI, K., Tsukamoto, T., Osumi, T., Shimozawa, N., Suzuki, Y., Orii, T., and Fujiki, Y.: Isolation and characterization of peroxisome-deficient Chinese hamster ovary (CHO) cell mutants representing human complementation group III. Exp. Cell Res. 233: 11-20 (1997).

Tsukamoto, T., Bogaki, A., Okumoto, K., Tateishi, K., Fujiki, Y., Shimozawa, N., Suzuki, Y., Kondo, N., and Osumi, T.: Isolation of a new peroxisome-deficient CHO cell mutant defective in peroxisome targeting signal-1 receptor. Biochem. Biophys. Res. Commun. 230: 402-406 (1997).

1996

Fujiki, Y.: Peroxisome biogenesis: topogenic signal, peroxisome assembly factor, and Zellweger syndrome. In Membrane Protein Transport (S. Rothman, ed.), Advances in Molecular and Cell Biology: Membrane Protein Transport, Vol. 3, pp. 213-229 (1996).

Fujiki, Y.: Approaches to studies on peroxisome biogenesis and human peroxisome-deficient disorders. Ann. N. Y. Acad. Sci. 804: 491-501 (1996).

Fukuda, S., Shimozawa, N., Suzuki, Y., Zhang, Z., Tomatsu, S., Tsukamoto, T., Hashiguchi, N., Osumi, T., Masuno, M., Imaizumi, K., Kuroki, Y., Fujiki, Y., Orii, T., and Kondo, N.: Human peroxisome assembly factor-2 (PAF-2): a gene responsible for group C peroxisome biogenesis disorder in humans. Am. J. Hum. Genet. 59: 1210-1220 (1996).

Distel, B., Erdmann, R., Gould, S.J., Blobel, G., Crane, D.I., Cregg, J.M., Dodt, G., Fujiki, Y., et al.: A unified nomenclature for peroxisome biogenesis factors. J. Cell Biol. 135: 1-3 (1996).

Shimozawa, N., Suzuki, Y., Tomatsu, S., Tsukamoto, T., Osumi, T., Fujiki, Y., Kamijo, K., Hashimoto, T., Kondo, N., and Orii, T.: Correction by gene expression of biochemical abnormalities in fibroblasts from Zellweger patients. Pediatr. Res. 39: 812-815 (1996).


邦文総説

(年代の新しいものから順に記す: 2000年以降)

1) 藤木幸夫、奥本寛治、本庄雅則: ペルオキシソーム形成異常と疾患. 特集「ストレスシグナルと疾患―細胞恒常性維持機構の破綻と病態」 医学のあゆみ 254: 397-401 (2015).

2) 藤木幸夫、本庄雅則: ペルオキシソームの脂質代謝. 特集「生命を支える脂質−最新の研究と臨床」 医学のあゆみ 248: 1143-1149 (2014).

3) 八木田悠一、藤木幸夫: テイルアンカー型ペルオキシソームタンパク質の輸送機構. 特集「テイルアンカー型タンパク質の細胞内輸送と膜挿入機構」 細胞工学 32: 857-862 (2013).

4) 藤木幸夫: テイルアンカー型タンパク質の細胞内輸送と膜挿入機構〜現代生物学に残された謎の一つがいま解かれる〜Overview. 特集「テイルアンカー型タンパク質の細胞内輸送と膜挿入機構」 細胞工学 32: 834-836 (2013).

5) 藤木幸夫、糸山彰徳、奥本寛治: ペルオキシソームの形成・制御とその障害−ユビキチンの関与. 日本応用酵素協会誌 47: 29-37 (2012).

6) 藤木幸夫、向井悟、宮田暖、宮内康弘: ペルオキシソーム移行シグナル2型(PTS2)タンパク質の輸送とその制御機構. 特集「細胞の分子構造と機能−核以外の細胞小器官」 生体の科学 63: 470-471(2012).

7) 藤木幸夫、宮田暖、奥本寛治、田村茂彦、糸山彰徳、本庄雅則: ペルオキシソームの形成・制御とその障害. 特集「細胞の分子構造と機能−核以外の細胞小器官」 生体の科学 63: 448-451 (2012).

8) 藤木幸夫、糸山彰徳、奥本寛治: ペルオキシソームの形成・制御の分子基盤. 特集「オルガネラ・モデリング〜ベールを脱ぐ分子設計図」 細胞工学 30: 1153-1159 (2011).

9) 藤木幸夫、宮田暖、松園裕嗣、松崎高志、本庄雅則: ペルオキシソームの形成・制御とその障害による高次機能の破綻. 特集「Protein Kinesisを解き明かすオルガネラの世界 細胞機能の制御と遺伝病発症・ウイルス感染のメカニズム」 実験医学 28: 2094-2101 (2010).

10) 藤木幸夫: Zellweger症候群. 小児科診療 2009年増刊号「小児の症候群」 72: 364-365 (2009).

11) 藤木幸夫: ペルオキシソームの形成機構とその破綻. 33: 9-16 (2008).

12) 藤木幸夫: ペルオキシソームの形成・分裂形態制御およびその障害の分子基盤. 日本応用酵素協会誌 42: 23-24 (2007).

13) 藤木幸夫: ペルオキシソームの形成機構とペルオキシソーム病. 蛋白質・核酸・酵素 増刊号「細胞における蛋白質の一生」 49: 1136-1142 (2004).

14) 藤木幸夫: ペルオキシソーム欠損症病因遺伝子PEX26. 医学のあゆみ 206: 922-923 (2003).

15) 藤木幸夫: ペルオキシソームの形成制御と病態. 特集「細胞機能の調節:タンパク質の細胞内トラフィックとオルガネラの形成と制御」 生化学 75: 459-654 (2003).

16) 藤木幸夫、大寺秀典、ガエディ・カムラン: ペルオキシソーム形成の分子機構と障害. 特集「細胞内タンパク質輸送:細胞質・オルガネラを結ぶネットワーク」 実験医学 20: 987-992 (2002).

17) 藤木幸夫: ペルオキシソームの形成とペルオキシソーム病. 特集「細胞内蛋白質輸送のダイナミクス」 細胞 33: 177-180 (2001).

18) 藤木幸夫: Peroxisome deficiency の分子機構. 遺伝子医学 4: 306-312 (2000).

19) 藤木幸夫、奥本寛治: ペルオキシソームの形成とその異常症. 蛋白質・核酸・酵素 45: 691-699 (2000).


著書

1) 藤木幸夫: 第2章:オルガネラ形成機構の研究法 2.ペルオキシソーム形成機構の研究法. 生物薬科学実験講座 第5巻 「細胞の構造とオルガネラ」 大熊勝治/中西義信(編)、廣川書店、pp. 148-171 (2010).

2) 藤木幸夫: ペルオキシソームの形成. わかる実験医学シリーズ 「細胞内輸送がわかる:タンパク質・核酸輸送の基本から最新の分子イメージング技術まで」 米田悦啓(編)、羊土社、pp. 61-67 (2002).

3) 藤木幸夫: ペルオキシソーム---- オルガネラ界の新スターは異端児か? シリーズ・バイオサイエンスの新世紀 第2巻「タンパク質の一生:タンパク質の誕生・成熟から死まで」 中野明彦・遠藤斗志也(編)、共立出版、pp. 137-152 (2000).


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