Calpain Project Publication, as of 2021.1.1

(To: Review papers in English or in Japanese)

Original papers in English
(Underlined: current Calpain Project members; [pdf] link to our original articles for recent publications (Please note that some of them are large (>4 MB) files))

[136] Shinkai-Ouchi F, Shindo M, Doi N, Hata S, Ono Y (2020) Calpain-2 participates in the process of calpain-1 inactivation. Biosci Rep 40(11):BSR20200552.

[128] Ono Y, Shindo M, Doi N, Kitamura F, Gregorio CC, Sorimachi H (2014) The N- and C-terminal autolytic fragments of CAPN3/p94/calpain-3 restore proteolytic activity by intermolecular complementation. Proc Natl Acad Sci USA 111:E5527-5536.

[127] Ojima K, Ono Y, Hata S, Noguchi S, Nishino I, Sorimachi H (2014) Muscle-specific calpain-3 is phosphorylated in its unique insertion region for enrichment in a myofibril fraction. Genes Cells 19:830-841.

[126] Buck D, Smith JE, 3rd, Chung CS, Ono Y, Sorimachi H, Labeit S, Granzier HL (2014) Removal of immunoglobulin-like domains from titin's spring segment alters titin splicing in mouse skeletal muscle and causes myopathy. J Gen Physiol 143:215-230.

[125] Maemoto Y, Ono Y, Kiso S, Shibata H, Takahara T, Sorimachi H, Maki M (2014) Involvement of calpain-7 in epidermal growth factor receptor degradation via the endosomal sorting pathway. FEBS J 281:3642-3655.

[124] Tonami K, Hata S, Ojima K, Ono Y, Kurihara Y, Amano T, Sato T, Kawamura Y, Kurihara H, Sorimachi H (2013) Calpain-6 Deficiency Promotes Skeletal Muscle Development and Regeneration. PLoS Genet., 9:1003668[pdf].

[123] Ono Y, Iemura S, Novak SM, Doi N, Kitamura F, Natsume T, Gregorio CC, Sorimachi H (2013) PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal muscle-specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1. J Mol Biol, 425:2955-2972[pdf].

[122] Hata S, Kitamura F, Sorimachi H (2013) Efficient expression and purification of recombinant human μ-calpain using an Escherichia coli expression system. Genes Cells, 18:753-763.

[121]   Hata S, Ueno M, Kitamura F, Sorimachi H (2012) Efficient expression and purification of recombinant human m-calpain using an Escherichia coli expression system at low temperature. J Biochem, 151:417-422[pdf].

[120]   Ozaki T, Nakazawa M, Yamashita T, Sorimachi H, Hata S, Tomita H, Isago H, Baba A, Ishiguro SI (2012) Intravitreal injection or topical eye-drop application of a mu-calpain C2L domain peptide protects against photoreceptor cell death in Royal College of Surgeons' rats, a model of retinitis pigmentosa. Biochim Biophys Acta 1822:1783-1795.

[119] Hara H, Okemoto-Nakamura Y, Shinkai-Ouchi F, Hanada K, Yamakawa Y, Hagiwara K (2012) Mouse prion protein (PrP) segment 100 to 104 regulates conversion of PrP(C) to PrP(Sc) in prion-infected neuroblastoma cells. J Virol 86:5626-5636.

[118]   Harada E, Nakagawa J, Asano T, Taoka M, Sorimachi H, Ito Y, Aigaki T, Matsuo T (2012) Functional evolution of duplicated odorant-binding protein genes, Obp57d and Obp57e, in Drosophila. PLoS One, 7:e29710 (Open Access).

[117]   duVerle DA, Ono Y, Sorimachi H, Mamitsuka H (2011) Calpain cleavage prediction using multiple kernel learning. PLoS One, 6:e19035 (Open Access).

[116]   Ojima K, Ono Y, Ottenheijm C, Hata S, Suzuki H, Granzier H, Sorimachi H (2011) Non-proteolytic functions of calpain-3 in sarcoplasmic reticulum in skeletal muscles. J Mol Biol 407:439-449.

[115]   Tonami K, Kurihara Y, Arima S, Nishiyama K, Uchijima Y, Asano T, Sorimachi H, Kurihara H (2011) Calpain-6, a microtubule-stabilizing protein, regulates Rac1 activity and cell motility through interaction with GEF-H1. J Cell Sci, 124:1214-1223.

[114]  Sáenz A*, Ono Y*(*equally contributed first authors), Sorimachi H, Goicoechea M, Leturcq F, Blazquez L, Garcia-Bragado F, Marina A, Poza JJ, Azpitarte M, Doi N, Urtasun M, Kaplan JC, Lopez de Munain A (2011) Does the severity of the LGMD2A phenotype in compound heterozygotes depend on the combination of mutations? Muscle Nerve, 44:710-714 [pdf].

[113]   Ojima K*, Kawabata Y*(*equally contributed first authors), Nakao H, Nakao K, Doi N, Kitamura F, Ono Y, Hata S, Suzuki H, Kawahara H, Bogomolovas J, Witt C, Ottenheijm C, Labeit S, Granzier H, Toyama-Sorimachi N, Sorimachi M, Suzuki K, Maeda T, Abe K, Aiba A, Sorimachi H (2010) Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy. J Clin Invest, 120:2672–2683.

[112]   Hata S, Abe M, Suzuki H, Kitamura F, Toyama-Sorimachi N, Abe K, Sakimura K, Sorimachi H (2010) Calpain 8/nCL-2 and calpain 9/nCL-4 constitute an active protease complex, G-calpain, involved in gastric mucosal defense.PLoS Genet, 6:e1001040 (Open Access).

[111]   Ono Y*, Ojima K*(*equally contributed first authors), Torii F, Takaya E, Doi N, Nakagawa K, Hata S, Abe K, Sorimachi H (2010) Skeletal muscle-specific calpain is an intracellular Na⁺-dependent protease. J Biol Chem, 285:22986-22998.

[110]   duVerle DA, Takigawa I, Ono Y, Sorimachi H, Mamitsuka H (2010) CaMPDB: a resource for calpain and modulatory proteolysis. Genome Inform 22:202-213 (Open Access).

[109]   Ono Y, Ojima K, Torii F, Takaya E, Doi N, Nakagawa K, Hata S, Abe K, Sorimachi H (2010) Redundant and non-redundant effects of Ca²⁺ and Na⁺ on the activation of p94/calpain-3. Neuromuscul Disord 20:608.

[108]   Ojima K, Ono Y, Doi N, Kitamura F, Kawabata Y, Suzuki K, Maeda T, Abe K, Nakao H, Aiba A, Suzuki H, Kawahara H, Witt C, Ottenheijm C, Labeit S, Ottenheijm C, Granzier H, Toyama-Sorimachi N, Sorimachi M, Sorimachi H (2010) Skeletal muscle-specific calpain, p94/calpain-3, dynamically distributes in skeletal muscle cells to adapt to physical stress, defects of which cause muscular dystrophy. Neuromuscul Disord 20:598-599.

[107]  Yamada M, Yoshida Y, Mori D, Takitoh T, Kengaku M, Umeshima H, Takao K, Miyakawa T, Sato M, Sorimachi H, Wynshaw-Boris A, Hirotsune S (2009) Inhibition of calpain increases LIS1 expression and partially rescues in vivo phenotypes in a mouse model of lissencephaly. Nat Med 15:1202-1207.

[106]   Sasuga Y, Iwasawa T, Terada K, Oe Y, Sorimachi H, Ohara O, Harada Y (2008) Single-cell chemical lysis method for analyses of intracellular molecules using an array of picoliter-scale microwells. Anal Chem 80:9141-9149.

[105]   Ono Y, Hayashi C, Doi N, Tagami M, Sorimachi H (2008) The importance of conserved amino acid residues in p94 protease sub-domain IIb and the IS2 region for constitutive autolysis. FEBS Lett 582:691-698.[pdf]

[104]   Koyama S*, Hata S*, Witt CC*(*equally contributed first authors), Ono Y, Lerche S, Ojima K, Chiba T, Doi N, Kitamura F, Tanaka K, Abe K, Witt SH, Rybin V, Gasch A, Franz T, Labeit S, Sorimachi H (2008) Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis. J Mol Biol 376:1224-1236.[pdf]

[103]   Hayashi C*, Ono Y*(*equally contributed first authors), Doi N, Kitamura F, Tagami M, Mineki R, Arai T, Taguchi H, Yanagida M, Hirner S, Labeit D, Labeit S, Sorimachi H (2008) Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle. J Biol Chem 283:14801-14814.[pdf] [suppl]

[102]   Kamei H, Saito T, Ozawa M, Fujita Y, Asada A, Bibb JA, Saido TC, Sorimachi H, Hisanaga S (2007) Suppression of calpain-dependent cleavage of the CDK5 activator p35 to p25 by site-specific phosphorylation. J Biol Chem 282:1687-1694.

[101]   Ono Y, Hayashi C, Doi N, Kitamura F, Shindo M, Kudo K, Tsubata T, Yanagida M, Sorimachi H (2007) Comprehensive survey of p94/calpain 3 substrates by comparative proteomics--possible regulation of protein synthesis by p94. Biotech J 2:565-576. (Free funded access!) [pdf] (This article was selected as “Most Accessed Articles” of Biotech J in May, June, and July of 2007.)

[100]   Ojima K, Ono Y, Doi N, Yoshioka K, Kawabata Y, Labeit S, Sorimachi H (2007) Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain. J Biol Chem 282:14493-14504.[pdf]

[99]      Hata S, Doi N, Kitamura F, Sorimachi H (2007) Stomach-specific calpain, nCL-2/calpain 8, is active without calpain regulatory subunit and oligomerizes through C2-like domains. J Biol Chem 282:27847-27856.[pdf]

[98]      Sorimachi H, Ojima K, Yanagida M, Ogawa H, Hayashi C, Doi N, Ono Y (2006) How do defects in proteolytic functions of skeletal muscle-specific calpain, p94/calpain 3, cause calpainopathy/LGMD2A? Neuromuscul Disord 16:S148.

[97]      Ono Y, Ojima K, Doi N, Hayashi C, Torii F, Yoshioka K, Labeit D, Labeit S, Suzuki K, Abe K, Maeda T, Sorimachi H (2006) Relationships between p94/CAPN3 and N2A connectin/titin in skeletal muscle under the normal and dystrophic conditions. Neuromuscul Disord 16:S72.

[96]      Ojima K, Ono Y, Doi N, Labeit S, Sorimachi H (2006) Spatio-temporal expression of muscle-specific calpain, p94/calpain 3, during myogenesis. Neuromuscul Disord 16:S56.

[95]      Ono Y, Torii F, Ojima K, Doi N, Yoshioka K, Labeit D, Labeit S, Suzuki K, Abe K, Maeda T, Sorimachi H (2006) Effect of N2A connectin/titin on disassembly of p94/CAPN3 caused by auaolysis in IS2. FEBS Journal 273 Suppl.:50-51.

[94]      Hata S, Koyama S, Kawahara H, Doi N, Maeda T, Toyama-Sorimachi N, Abe K, Suzuki K, Sorimachi H (2006) Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP. J Biol Chem 281:11214-11224.[pdf]

[93]      Nakajima K, Asakura T, Oike H, Morita Y, Shimizu-Ibuka A, Misaka T, Sorimachi H, Arai S, Abe K (2006) Neoculin, a taste-modifying protein, is recognized by human sweet taste receptor. Neuroreport 17:1241-1244.

[92]      Ono Y, Torii F, Ojima K, Doi N, Yoshioka K, Kawabata Y, Labeit D, Labeit S, Suzuki K, Abe K, Maeda T, Sorimachi H (2006) Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system. J Biol Chem 281:18519-18531.[pdf]

[91]      Nakajima K, Asakura T, Maruyama J, Morita Y, Oike H, Shimizu-Ibuka A, Misaka T, Sorimachi H, Arai S, Kitamoto K, Abe K (2006) Extracellular production of neoculin, a sweet-tasting heterodimeric protein with taste-modifying activity, by Aspergillus oryzae. Appl Environ Microbiol 72:3716-3723.

[90]      Shimizu-Ibuka A, Morita Y, Terada T, Asakura T, Nakajima K, Iwata S, Misaka T, Sorimachi H, Arai S, Abe K (2006) Crystal structure of neoculin: insights into its sweetness and taste-modifying activity. J Mol Biol 359:148-158.

[89]      Yajima Y, Sato M, Sorimachi H, Inomata M, Maki M, Kawashima S (2006) Calpain system regulates the differentiation of adult primitive mesenchymal ST-13 adipocytes. Endocrinology 147:4811-4819.

[88]      Takahara T, Hara K, Yonezawa K, Sorimachi H, Maeda T (2006) Nutrient-dependent multimerization of the mammalian target of rapamycin through the N-terminal HEAT repeat region. J Biol Chem 281:28605-28614.

[87]      Sorimachi H, Ono Y, Ojima K, Kawabata Y, Witt CC, Nakao H, Kawahara H, Hata S, Koyama S, Granzier H, Gregorio CC, Labeit S, Aiba A, Abe K, Suzuki K (2005) Calpain and connectin/titin in health and disease of skeletal muscle. FEBS Journal 272 Suppl.:177-178.

[86]      Ono Y, Ojima K, Kawabata Y, Doi N, Witt CC, Witt S, Labeit D, Granzier H, Gregorio CC, Labeit S, Suzuki K, Sorimachi H (2005) Functional properties of p94/calpain3 and connectin/titin in mdm mouse skeletal muscle. FEBS Journal 272 Suppl.:182.

[85]      Ojima K, Ono Y, Hata S, Koyama S, Doi N, Sorimachi H (2005) Possible functions of p94 in connectin-mediated signaling pathways in skeletal muscle cells. J Muscle Res Cell Motil 26:409-417.[pdf]

[84]      Toyama-Sorimachi N, Omatsu Y, Onoda A, Tsujimura Y, Iyoda T, Kikuchi-Maki A, Sorimachi H, Dohi T, Taki S, Inaba K, Karasuyama H (2005) Inhibitory NK receptor Ly49Q is expressed on subsets of dendritic cells in a cellular maturation- and cytokine stimulation-dependent manner. J Immunol 174:4621-4629.

[83]      Hayashi M, Fukuzawa T, Sorimachi H, Maeda T (2005) Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway. Mol Cell Biol 25:9478-9490.

[82]      Sato K, Hattori S, Irie S, Sorimachi H, Inomata M, Kawashima S (2004) Degradation of fodrin by m-calpain in fibroblasts adhering to fibrillar collagen I gel. J Biochem 136:777-785.

[81]      Witt CC, Ono Yecfa, Puschmann E, McNabb M, Wu Y, Gotthardt M, Witt SH, Haak M, Labeit D, Gregorio CC, Sorimachi H, Granzier H, Labeit S (2004) Induction and myofibrillar targeting of CARP, and suppression of the Nkx2.5 pathway in the MDM mouse with impaired titin-based signaling. J Mol Biol 336:145-154.

[80]      Ono Y, Kakinuma K, Torii F, Irie A, Nakagawa K, Labeit S, Abe K, Suzuki K, Sorimachi H (2004) Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3. J Biol Chem 279:2761-2771.[pdf]

[79]      Shirasuka Y, Nakajima K, Asakura T, Yamashita H, Yamamoto A, Hata S, Nagata S, Abo M, Sorimachi H, Abe K (2004) Neoculin as a new taste-modifying protein occurring in the fruit of Curculigo latifolia. Biosci Biotechnol Biochem 68:1403-1407.

[78]      Kimura E, Abe K, Suzuki K, Sorimachi H (2003) Heterogeneous nuclear ribonucleoprotein K interacts with and is proteolyzed by calpain in vivo. Biosci Biotechnol Biochem 67:1786-1796.

[77]      Kawabata Y, Hata S, Ono Y, Ito Y, Suzuki K, Abe K, Sorimachi H (2003) Newly identified exons encoding novel variants of p94/calpain 3 are expressed ubiquitously and overlap the alpha-glucosidase C gene. FEBS Lett 555:623-630.

[76]      McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC (2002) Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 157:125-136.

[75]      Spencer MJ, Guyon JR, Sorimachi H, Potts A, Richard I, Herasse M, Chamberlain J, Dalkilic I, Kunkel LM, Beckmann JS (2002) Stable expression of calpain 3 from a muscle transgene in vivo: immature muscle in transgenic mice suggests a role for calpain 3 in muscle maturation. Proc Natl Acad Sci U S A 99:8874-8879.

[74]      Reverter D, Braun M, Fernandez-Catalan C, Strobl S, Sorimachi H, Bode W (2002) Flexibility analysis and structure comparison of two crystal forms of calcium-free human m-calpain. Biol Chem 383:1415-1422.

[73]      Welm AL, Timchenko NA, Ono Y, Sorimachi H, Radomska HS, Tenen DG, Lekstrom-Himes J, Darlington GJ (2002) C/EBPa is required for proteolytic cleavage of cyclin A by calpain 3 in myeloid precursor cells. J Biol Chem 277:33848-33856.

[72]      Ilian MA, Morton JD, Bekhit AE, Roberts N, Palmer B, Sorimachi H, Bickerstaffe R (2001) Effect of preslaughter feed withdrawal period on longissimus tenderness and the expression of calpains in the ovine. Journal of agricultural and food chemistry 49:1990-1998.

[71]      Bang ML, Mudry RE, McElhinny AS, Trombitas K, Geach AJ, Yamasaki R, Sorimachi H, Granzier H, Gregorio CC, Labeit S (2001) Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. J Cell Biol 153:413-427.

[70]      Tompa P, Emori Y, Sorimachi H, Suzuki K, Friedrich P (2001) Domain III of calpain is a Ca²⁺-regulated phospholipid-binding domain. Biochem Biophys Res Commun 280:1333-1339.

[69]      Futai E, Kubo T, Sorimachi H, Suzuki K, Maeda T (2001) Molecular cloning of PalBH, a mammalian homologue of the Aspergillus atypical calpain PalB. Biochim Biophys Acta 1517:316-319.

[68]      Hata S, Sorimachi H, Nakagawa K, Maeda T, Abe K, Suzuki K (2001) Domain II of m-calpain is a Ca²⁺-dependent cysteine protease. FEBS Lett 501:111-114.

[67]      Centner T, Yano Jecfa, Kimura E, McElhinny AS, Pelin K, Witt CC, Bang ML, Trombitas K, Granzier H, Gregorio CC, Sorimachi H, Labeit S (2001) Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J Mol Biol 306:717-726.

[66]      Reverter D, Strobl S, Fernandez-Catalan C, Sorimachi H, Suzuki K, Bode W (2001) Structural basis for possible calcium-induced activation mechanisms of calpains. Biol Chem 382:753-766.

[65]      Takahashi N, Sasagawa N, Usuki F, Kino Y, Kawahara H, Sorimachi H, Maeda T, Suzuki K, Ishiura S (2001) Coexpression of the CUG-binding protein reduces DM protein kinase expression in COS cells. J Biochem 130:581-587.

[64]      Nakagawa K, Masumoto H, Sorimachi H, Suzuki K (2001) Dissociation of m-calpain subunits occurs after autolysis of the N-terminus of the catalytic subunit, and is not required for activation. J Biochem 130:605-611.

[63]      Umeda T, Kouchi Z, Kawahara H, Tomioka S, Sasagawa N, Maeda T, Sorimachi H, Ishiura S, Suzuki K (2001) Limited proteolysis of filamin is catalyzed by caspase-3 in U937 and Jurkat cells. J Biochem 130:535-542.

[62]      Hata S, Nishi K, Kawamoto T, Lee HJ, Kawahara H, Maeda T, Shintani Y, Sorimachi H, Suzuki K (2001) Both the conserved and the unique gene structure of stomach-specific calpains reveal processes of calpain gene evolution. J Mol Evol 53:191-203.

[61]      Kitagaki H, Tomioka S, Yoshizawa T, Sorimachi H, Saido TC, Ishiura S, Suzuki K (2000) Autolysis of calpain large subunit inducing irreversible dissociation of stoichiometric heterodimer of calpain. Biosci Biotechnol Biochem 64:689-695.

[60]      Richard I, Roudaut C, Marchand S, Baghdiguian S, Herasse M, Stockholm D, Ono Y, Suel L, Bourg N, Sorimachi H, Lefranc G, Fardeau M, Sebille A, Beckmann JS (2000) Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IkBa/nuclear factor kB pathway perturbation in mice. J Cell Biol 151:1583-1590.

[59]      Hata S, Sato T, Sorimachi H, Ishiura S, Suzuki K (2000) A simple purification and fluorescent assay method of the poliovirus 3C protease searching for specific inhibitors. J Virol Methods 84:117-126.

[58]      Masumoto H, Nakagawa K, Irie S, Sorimachi H, Suzuki K, Bourenkov GP, Bartunik H, Fernandez-Catalan C, Bode W, Strobl S (2000) Crystallization and preliminary X-ray analysis of recombinant full-length human m-calpain. Acta crystallographica Section D, Biological crystallography 56:73-75.

[57]      Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, Irie A, Sorimachi H, Bourenkow G, Bartunik H, Suzuki K, Bode W (2000) The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. Proc Natl Acad Sci U S A 97:588-592.

[56]      Koike H, Kouchi Z, Kinouchi T, Maeda T, Sorimachi H, Saido TC, Maruyama K, Okuyama A, Suzuki K, Ishiura S (2000) Metabolism of amyloid precursor protein in COS cells transfected with a beta-secretase candidate. Cytotechnology 33:213-219.

[55]      Tagawa K, Taya C, Hayashi Y, Nakagawa M, Ono Y, Fukuda R, Karasuyama H, Toyama-Sorimachi N, Katsui Y, Hata S, Ishiura S, Nonaka I, Seyama Y, Arahata K, Yonekawa H, Sorimachi H, Suzuki K (2000) Myopathy phenotype of transgenic mice expressing active site-mutated inactive p94 skeletal muscle-specific calpain, the gene product responsible for limb girdle muscular dystrophy type 2A. Hum Mol Genet 9:1393-1402.

[54]      Futai E, Sorimachi H, Jeong SY, Kitamoto K, Ishiura S, Suzuki K (1999) Aspergillus oryzae palBory encodes a calpain-like protease: homology to Emericella nidulans PalB and conservation of functional regions. Journal of bioscience and bioengineering 88:438-440.

[53]      Suo S, Koike H, Sorimachi H, Ishiura S, Suzuki K (1999) Association and dissociation of the calcium-binding domains of calpain by Ca²⁺. Biochem Biophys Res Commun 257:63-66.

[52]      Watanabe T, Sasagawa N, Usuki F, Koike H, Saitoh N, Sorimachi H, Maruyama K, Nakase H, Takagi A, Ishiura S, Suzuki K (1999) Overexpression of myotonic dystrophy protein kinase in C2C12 myogenic culture involved in the expression of ferritin heavy chain and interleukin-1a mRNAs. J Neurol Sci 167:26-33.

[51]      Lee HJ, Tomioka S, Kinbara K, Masumoto H, Jeong SY, Sorimachi H, Ishiura S, Suzuki K (1999) Characterization of a human digestive tract-specific calpain, nCL-4, expressed in the baculovirus system. Arch Biochem Biophys 362:22-31.

[50]      Futai E, Maeda T, Sorimachi H, Kitamoto K, Ishiura S, Suzuki K (1999) The protease activity of a calpain-like cysteine protease in Saccharomyces cerevisiae is required for alkaline adaptation and sporulation. Mol Gen Genet 260:559-568.

[49]      Kouchi Z, Sorimachi H, Suzuki K, Ishiura S (1999) Proteasome inhibitors induce the association of Alzheimer's amyloid precursor protein with Hsc73. Biochem Biophys Res Commun 254:804-810.

[48]      Koike H, Seki H, Kouchi Z, Ito M, Kinouchi T, Tomioka S, Sorimachi H, Saido TC, Maruyama K, Suzuki K, Ishiura S (1999) Thimet oligopeptidase cleaves the full-length Alzheimer amyloid precursor protein at a beta-secretase cleavage site in COS cells. J Biochem 126:235-242.

[47]      Herasse M, Ono Y, Fougerousse F, Kimura E, Stockholm D, Beley C, Montarras D, Pinset C, Sorimachi H, Suzuki K, Beckmann JS, Richard I (1999) Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events. Mol Cell Biol 19:4047-4055.

[46]      Koike H, Tomioka S, Sorimachi H, Saido TC, Maruyama K, Okuyama A, Fujisawa-Sehara A, Ohno S, Suzuki K, Ishiura S (1999) Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein. Biochem J 343:371-375.

[45]      Saitoh N, Usuki F, Sasagawa N, Koike H, Sorimachi H, Yabe I, Ishiura S, Suzuki K (1998) Myotonin protein kinase (MtPK) affects the chloride permeability of C2C12 myogenic cells. Biomedical Research 19:191-198.

[44]      Koike H, Saitoh N, Sasagawa N, Watanabe T, Shimokawa M, Sorimachi H, Arahata K, Ishiura S, Suzuki K (1998) Identification and purification of myotonin protein kinase (MtPK) from rat skeletal muscle sarcoplasmic reticulum. Biomedical Research 19:93-99.

[43]      Kouchi Z, Kinouchi T, Sorimachi H, Ishiura S, Suzuki K (1998) The deletion of the C-terminal tail and addition of an endoplasmic reticulum targeting signal to Alzheimer's amyloid precursor protein change its localization, secretion, and intracellular proteolysis. Eur J Biochem 258:291-300.

[42]      Lee HJ, Sorimachi H, Jeong SY, Ishiura S, Suzuki K (1998) Molecular cloning and characterization of a novel tissue-specific calpain predominantly expressed in the digestive tract. Biol Chem 379:175-183.

[41]      Ono Y, Shimada H, Sorimachi H, Richard I, Saido TC, Beckmann JS, Ishiura S, Suzuki K (1998) Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J Biol Chem 273:17073-17078.

[40]      Masumoto H, Yoshizawa T, Sorimachi H, Nishino T, Ishiura S, Suzuki K (1998) Overexpression, purification, and characterization of human m-calpain and its active site mutant, m-C105S-calpain, using a baculovirus expression system. J Biochem 124:957-961.

[39]      Kinbara K, Ishiura S, Tomioka S, Sorimachi H, Jeong SY, Amano S, Kawasaki H, Kolmerer B, Kimura S, Labeit S, Suzuki K (1998) Purification of native p94, a muscle-specific calpain, and characterization of its autolysis. Biochem J 335:589-596.

[38]      Gregorio CC, Trombitas K, Centner T, Kolmerer B, Stier G, Kunke K, Suzuki K, Obermayr F, Herrmann B, Granzier H, Sorimachi H, Labeit S (1998) The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J Cell Biol 143:1013-1027.

[37]      Shimokawa M, Ishiura S, Kameda N, Yamamoto M, Sasagawa N, Saitoh N, Sorimachi H, Ueda H, Ohno S, Suzuki K, Kobayashi T (1997) Novel isoform of myotonin protein kinase: gene product of myotonic dystrophy is localized in the sarcoplasmic reticulum of skeletal muscle. Am J Pathol 150:1285-1295.

[36]      Sorimachi H, Freiburg A, Kolmerer B, Ishiura S, Stier G, Gregorio CC, Labeit D, Linke WA, Suzuki K, Labeit S (1997) Tissue-specific expression and alpha-actinin binding properties of the Z-disc titin: implications for the nature of vertebrate Z-discs. J Mol Biol 270:688-695.

[35]      Usuki F, Ishiura S, Saitoh N, Sasagawa N, Sorimachi H, Kuzume H, Maruyama K, Terao T, Suzuki K (1997) Expanded CTG repeats in myotonin protein kinase suppresses myogenic differentiation. Neuroreport 8:3749-3753.

[34]      Kinbara K, Sorimachi H, Ishiura S, Suzuki K (1997) Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs. Arch Biochem Biophys 342:99-107.

[33]      Ono Y, Kinouchi T, Sorimachi H, Ishiura S, Suzuki K (1997) Deletion of an endosomal/lysosomal targeting signal promotes the secretion of Alzheimer's disease amyloid precursor protein (APP). J Biochem 121:585-590.

[32]      Jeong SY, Sorimachi H, Lee HJ, Ishiura S, Suzuki K (1997) Molecular cloning and characterization of cDNAs for the m-type large subunit and the small subunit of chicken calpain. Comp Biochem Physiol B Biochem Mol Biol 118:539-547.

[31]      Sorimachi H, Forsberg NE, Lee HJ, Joeng SY, Richard I, Beckmann JS, Ishiura S, Suzuki K (1996) Highly conserved structure in the promoter region of the gene for muscle-specific calpain, p94. Biol Chem 377:859-864.

[30]      Yazaki M, Tagawa K, Maruyama K, Sorimachi H, Tsuchiya T, Ishiura S, Suzuki K (1996) Mutation of potential N-linked glycosylation sites in the Alzheimer's disease amyloid precursor protein (APP). Neurosci Lett 221:57-60.

[29]      Sasagawa N, Saitoh N, Shimokawa M, Sorimachi H, Maruyama K, Arahata K, Isiura S, Suzuki K (1996) Effect of artificial (CTG) repeat expansion on the expression of myotonin protein kinase (MtPK) in COS-1 cells. Biochim Biophys Acta 1315:112-116.

[28]      Saitoh N, Sasagawa N, Koike H, Shimokawa M, Sorimachi H, Ishiura S, Suzuki K (1996) Immunocytochemical localization of a full-length myotonin protein kinase in rat L6 myoblasts. Neurosci Lett 218:214-216.

[27]      Sorimachi H, Amano S, Ishiura S, Suzuki K (1996) Primary sequences of rat m-calpain large and small subunits are, respectively, moderately and highly similar to those of human. Biochim Biophys Acta 1309:37-41.

[26]      Suzuki K, Sorimachi H, Ishiura S, Ohno S (1995) Two family members of calpain: ubiquitous and tissue-specific calpains. Expression of Tissue ProteInases and Regulation of ProteIn Degradation as related to Meat Quality.

[25]      Kinouchi T, Ono Y, Sorimachi H, Ishiura S, Suzuki K (1995) Arachidonate metabolites affect the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein. Biochem Biophys Res Commun 209:841-849.

[24]      Sorimachi H, Tsukahara T, Okada-Ban M, Sugita H, Ishiura S, Suzuki K (1995) Identification of a third ubiquitous calpain species--chicken muscle expresses four distinct calpains. Biochim Biophys Acta 1261:381-393.

[23]      Sorimachi H, Kinbara K, Kimura S, Takahashi M, Ishiura S, Sasagawa N, Sorimachi N, Shimada H, Tagawa K, Maruyama K, Suzuki K (1995) Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem 270:31158-31162.

[22]      Yoshizawa T, Sorimachi H, Tomioka S, Ishiura S, Suzuki K (1995) A catalytic subunit of calpain possesses full proteolytic activity. FEBS Lett 358:101-103.

[21]      Yoshizawa T, Sorimachi H, Tomioka S, Ishiura S, Suzuki K (1995) Calpain dissociates into subunits in the presence of calcium ions. Biochem Biophys Res Commun 208:376-383.

[20]      Toyama-Sorimachi N, Sorimachi H, Tobita Y, Kitamura F, Yagita H, Suzuki K, Miyasaka M (1995) A novel ligand for CD44 is serglycin, a hematopoietic cell lineage-specific proteoglycan. Possible involvement in lymphoid cell adherence and activation. J Biol Chem 270:7437-7444.

[19]      Kinouchi T, Sorimachi H, Maruyama K, Mizuno K, Ohno S, Ishiura S, Suzuki K (1995) Conventional protein kinase C (PKC)-a and novel PKC-e, but not -d, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 fibroblasts. FEBS Lett 364:203-206.

[18]      Usuki F, Ishiura S, Sasagawa N, Sorimachi H, Suzuki K, Shimizu T, Terao T (1995) Up-regulation of dystrophin mRNA by exposure to dibutyryl cAMP in the C2C12 muscle cell line. Biochem Biophys Res Commun 210:654-659.

[17]      Sakamoto K, Sorimachi H, Kinbara K, Tezuka M, Amano S, Yoshizawa T, Sugita H, Ishiura S, Suzuki K (1994) Quantification of calpain-related molecules by specific PCR amplification and its application to human muscular dystrophy. Biomedical Research 15:337-346.

[16]      Sasagawa N, Sorimachi H, Maruyama K, Arahata K, Ishiura S, Suzuki K (1994) Expression of a novel human myotonin protein kinase (MtPK) cDNA clone which encodes a protein with a thymopoietin-like domain in COS cells. FEBS Lett 351:22-26.

[15]      Saido TC, Nagao S, Shiramine M, Tsukaguchi M, Yoshizawa T, Sorimachi H, Ito H, Tsuchiya T, Kawashima S, Suzuki K (1994) Distinct kinetics of subunit autolysis in mammalian m-calpain activation. FEBS Lett 346:263-267.

[14]      Kinbara K, Kitagaki H, Kinouchi T, Okano M, Sorimachi H, Ishiura S, Suzuki K (1994) Processing and secretion of Alzheimer's disease amyloid precursor protein. Tohoku J Exp Med 174:209-216.

[13]      Tagawa K, Yazaki M, Kinouchi T, Maruyama K, Sorimachi H, Tsuchiya T, Suzuki K, Ishiura S (1993) Amyloid precursor protein is found in lysosomes. Gerontology 39 Suppl 1:24-29.

[12]      Sorimachi H, Toyama-Sorimachi N, Saido TC, Kawasaki H, Sugita H, Miyasaka M, Arahata K, Ishiura S, Suzuki K (1993) Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J Biol Chem 268:10593-10605.

[11]      Sorimachi H, Ishiura S, Suzuki K (1993) A novel tissue-specific calpain species expressed predominantly in the stomach comprises two alternative splicing products with and without Ca²⁺-binding domain. J Biol Chem 268:19476-19482.

[10]      Saido TC, Nagao S, Shiramine M, Tsukaguchi M, Sorimachi H, Murofushi H, Tsuchiya T, Ito H, Suzuki K (1992) Autolytic transition of m-calpain upon activation as resolved by antibodies distinguishing between the pre- and post-autolysis forms. J Biochem 111:81-86.

[9]        Sorimachi H, Kawasaki H, Tsukahara T, Ishiura S, Emori Y, Sugita H, Suzuki K (1991) Sequence comparison among subunits of multicatalytic proteinase. Biomed Biochim Acta 50:459-464.

[8]        Sorimachi H, Emori Y, Kawasaki H, Suzuki K, Inoue Y (1990) Molecular cloning and characterization of cDNAs coding for apopolysialoglycoproteins in cherry salmon (Oncorhynchus masou) eggs. J Biochem 107:61-67.

[7]        Sorimachi H, Emori Y, Kawasaki H, Suzuki K, Inoue Y (1990) Organization and primary sequence of multiple genes coding for the apopolysialoglycoproteins of rainbow trout. J Mol Biol 211:35-48.

[6]        Sorimachi H, Tsukahara T, Kawasaki H, Ishiura S, Emori Y, Sugita H, Suzuki K (1990) Molecular cloning of cDNAs for two subunits of rat multicatalytic proteinase. Existence of N-terminal conserved and C-terminal diverged sequences among subunits. Eur J Biochem 193:775-781.

[5]        Emori Y, Homma Y, Sorimachi H, Kawasaki H, Nakanishi O, Suzuki K, Takenawa T (1989) A second type of rat phosphoinositide-specific phospholipase C containing a src-related sequence not essential for phosphoinositide-hydrolyzing activity. J Biol Chem 264:21885-21890.

[4]        Sorimachi H, Imajoh-Ohmi S, Emori Y, Kawasaki H, Ohno S, Minami Y, Suzuki K (1989) Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. J Biol Chem 264:20106-20111.

[3]        Homma Y, Takenawa T, Emori Y, Sorimachi H, Suzuki K (1989) Tissue- and cell type-specific expression of mRNAs for four types of inositol phospholipid-specific phospholipase C. Biochem Biophys Res Commun 164:406-412.

[2]        Sorimachi H, Emori Y, Kawasaki H, Kitajima K, Inoue S, Suzuki K, Inoue Y (1988) Molecular cloning and characterization of cDNAs coding for apo-polysialoglycoprotein of rainbow trout eggs. Multiple mRNA species transcribed from multiple genes contain diverged numbers of exact 39-base (13-amino acid) repeats. J Biol Chem 263:17678-17684.

[1]        Kitajima K, Sorimachi H, Inoue S, Inoue Y (1988) Comparative structures of the apopolysialoglycoproteins from unfertilized and fertilized eggs of salmonid fishes. Biochemistry 27:7141-7145.

Review papers in English

[56] Ono Y, Saido TC, Sorimachi H (2016) Calpain research for drug discovery: challenges and potential. Nat Rev Drug Discov 15:854-876.

[55] Ono Y, Ojima K, Shinkai-Ouchi F, Hata S, Sorimachi H (2015) An eccentric calpain, CAPN3/p94/calpain-3. Biochimie 122:169-187.

[54] Ono Y, Sorimachi H (2015) Amino acid sequence alignment of vertebrate CAPN3/calpain-3/p94. Data in Brief 5:366-367.

[53] Anagli J, Wang KKW, Ono Y, Sorimachi H (2013) Chapter 12: Calpains in Health and Disease. in: ”Proteases: Structure and Function”, (Wien: Springer-Verlag; Brix K, Stöcker W, eds), pp 395-431.

[52]      Sorimachi H (2013) Calpain. in ”Encyclopedia of Biological Chemistry 2nd Edition”, (Elsevier, Oxford; eds., M.D. Lane and W.J. Lennarz), vol. 3, pp353-361.

[51]      Sorimachi H, Mamitsuka H, Ono Y (2012) Understanding the substrate specificity of conventional calpains. Biol Chem 393:853-871 [pdf].

[49]      Sorimachi, H., Hata, S., and Ono, Y. (2012) Chapter 476. Other calpains. in “Handbook of Proteolytic enzymes, 3rd Edition”, (Elsevier Academic Press, Oxford, UK; RawlIngs, N. D. and Salvesen, G. eds.), pp 2027-2038.

[48]      Sorimachi, H., Ono, Y., and Hata, S. (2012) Chapter 474. Gastrointestinal calpain. in “Handbook of Proteolytic enzymes, 3rd Edition”, (Elsevier Academic Press, Oxford, UK; RawlIngs, N. D. and Salvesen, G. eds.), pp2018-2022.

[47]      Sorimachi, H., Hata, S., and Ono, Y. (2012) Chapter 473. Muscle calpain. in “Handbook of Proteolytic enzymes, 3rd Edition”, (Elsevier Academic Press, Oxford, UK; RawlIngs, N. D. and Salvesen, G. eds.), pp 2011-2017.

[46]      Sorimachi, H., Hata, S., and Ono, Y. (2012) Chapter 472. m-calpain. in “Handbook of Proteolytic enzymes, 3rd Edition”, (Elsevier Academic Press, Oxford, UK; RawlIngs, N. D. and Salvesen, G. eds.), pp 2007-2011.

[45]      Sorimachi, H., Hata, S., and Ono, Y. (2012) Chapter 471. mu-calpain. in “Handbook of Proteolytic enzymes, 3rd Edition”, (Elsevier Academic Press, Oxford, UK; RawlIngs, N. D. and Salvesen, G. eds.), pp 1995-2007.

[44]      Ono, Y., and Sorimachi, H. (2011) Calpains - an elaborate proteolytic system. Biochim Biophys Acta - Proteins and Proteomics, 1824, 224-236 (Free Funded Access).

[43]      Sorimachi, H., Hata, S., and Ono, Y. (2011) Calpain chronicle - an enzyme family under multidisciplinary characterization. Proc. Jpn. Acad. Ser. B, 87, 287-327 (Open Access).

[42]      Sorimachi, H., Hata, S., and Ono, Y. (2011) Impact of genetic insights into calpain biology. J. Biochem., 150, 23-37 (Open Access).

[41]      Fardeau, M., Beckmann, J.S., Sorimachi, H., and Urtizberea, J. A. (2010) Une contribution á l'histoire de la découverte des calpaïnopathies. (in French) Les Cahiers de Myologie, 2, 5-10.

[40]      Sorimachi H, Hata S, Ono Y (2010) Expanding members and roles of the calpain superfamily and their genetically modified animals. Exp Anim 59:549-566 (Open Access).

[39]      Sorimachi H (2004) m-Calpain. In: Handbook of Proteolytic Enzymes, 2nd Edition (Barrett AJ, Rawlings ND, Woessner JF, eds), pp 1211-1213. Oxford, UK: Academic Press.

[38]      Sorimachi H (2004) μ-Calpain. In: Handbook of Proteolytic Enzymes, 2nd Edition (Barrett AJ, Rawlings ND, Woessner JF, eds), pp 1206-1211. Oxford, UK: Academic Press.

[37]      Sorimachi H (2004) Muscle calpain p94. In: Handbook of Proteolytic Enzymes, 2nd Edition (Barrett AJ, Rawlings ND, Woessner JF, eds), pp 1213-1217. Oxford, UK: Academic Press.

[36]      Sorimachi H (2004) Other calpain. In: Handbook of Proteolytic Enzymes, 2nd Edition (Barrett AJ, Rawlings ND, Woessner JF, eds), pp 1217-1225. Oxford, UK: Academic Press.

[35]      Sorimachi H, Ono Y (2004) Calpain. In: Encyclopedia of Biological Chemistry (Lennarz WJ, Lane MD, eds), pp 300-306. Oxford, UK: Elsevier.

[34]      Suzuki K, Hata S, Kawabata Y, Sorimachi H (2004) Structure, activation, and biology of calpain. Diabetes 53 Suppl 1:S12-18.

[33]      Sorimachi H, Beckmann JS (2002) Defects of non-lysosomal proteolysis: Calpain3 deficiency. In: Structural and Molecular Basis of Skeletal Muscle Diseases (Karpati G, ed), pp 148-153. Basel: ISN Neuropath. Press.

[32]      Reverter D, Sorimachi H, Bode W (2001) The structure of calcium-free human m-calpain: implications for calcium activation and function. Trends Cardiovasc Med 11:222-229.

[31]      Sorimachi H, Suzuki K (2001) The structure of calpain. J Biochem 129:653-664.

[30]      Ono Y, Hata S, Sorimachi H, Suzuki K (2000) Calcium and muscle disease: Pathophysiology of calpains and limb-girdle muscular dystrophy type 2A (LGMD2A). In: Calcium: The Molecular Basis of Calcium Action in Biology and Medicine (Pochet R, Donato R, Haiech J, Heizmann C, Gerke V, eds), pp 443-464. Netherlands: Kluwer Academic Publishers.

[29]      Sorimachi H, Minami N, Ono Y, Suzuki K, Nonaka I (2000) Limb-girdle muscular dystrophy with calpain 3 (p94) gene mutations (calpainopathy). Neuroscience News 3:20-27.

[28]      Sorimachi H, Ono Y, Suzuki K (2000) Molecular analysis of p94 and its application to diagnosis of limb girdle muscular dystrophy type 2A. Methods Mol Biol 144:75-84.

[27]      Sorimachi H, Ono Y, Suzuki K (2000) Skeletal muscle-specific calpain, p94, and connectin/titin: their physiological functions and relationship to limb-girdle muscular dystrophy type 2A. Adv Exp Med Biol 481:383-395; discussion 395-387.

[26]     Ono Y, Sorimachi H, Suzuki K (1999) Calpains: structure and function of the calpain super family. In: Proteases: New Perspectives (Turk V, ed), pp 159-174. Basel, Switzerland: Birkhäuser Verlag.

[25]      Ono Y, Sorimachi H, Suzuki K (1999) The calpain superfamily. In: Calpain (Wang KKW, Yuen P-W, eds), pp 1-23. Ann Arbor: Taylor & Francis.

[24]      Kolmerer B, Witt CC, Freiburg A, Millevoi S, Stier G, Sorimachi H, Pelin K, Carrier L, Schwartz K, Labeit D, Gregorio CC, Linke WA, Labeit S (1999) The titin cDNA sequence and partial genomic sequences: insights into the molecular genetics, cell biology and physiology of the titin filament system. Rev Physiol Biochem Pharmacol 138:19-55.

[23]      Gregorio CC, Granzier H, Sorimachi H, Labeit S (1999) Muscle assembly: a titanic achievement? Curr Opin Cell Biol 11:18-25.

[22]      Ono Y, Sorimachi H, Suzuki K (1999) New aspect of the research on limb-girdle muscular dystrophy 2A: a molecular biologic and biochemical approach to pathology. Trends Cardiovasc Med 9:114-118.

[21]      Sorimachi H, Suzuki K (1998) m-calpain. In: Handbook of Proteolytic enzymes (Barrett AJ, RawlIngs ND, Woessner JF, eds), pp 649-654: Academic Press.

[19]      Sorimachi H, Suzuki K (1998) muscle calpain, p94. In: Handbook of Proteolytic enzymes (Barrett AJ, RawlIngs ND, Woessner JF, eds), pp 654-656: Academic Press.

[18]      Ono Y, Sorimachi H, Suzuki K (1998) Structure and physiology of calpain, an enigmatic protease. Biochem Biophys Res Commun 245:289-294.

[17]      Suzuki K, Sorimachi H (1998) A novel aspect of calpain activation. FEBS Lett 433:1-4.

[16]      Kinbara K, Sorimachi H, Ishiura S, Suzuki K (1998) Skeletal muscle-specific calpain, p94: structure and physiological function. Biochem Pharmacol 56:415-420.

[15]      Sorimachi H, Kinbara K, Shimada H, Suzuki K (1997) Interaction of a skeletal muscle-specific calpain, p94, with connectin. In: Medical Aspects of Proteases and Protease Inhibitors (Katunuma N, Kido H, Fritz H, Travis J, eds), pp 34-42. Tokyo: IOS Press.

[14]      Kinouchi T, Sorimachi H, Ishiura S, Suzuki K (1997) Regulation of proteolysis of Alzheimer's disease amyloid precursor protein by intracellular signal transduction pathways. In: Proteolysis In Cell Functions (Hopsu-Havu VK, JärvInen M, Kirschke H, eds), pp 513-519. BerlIn: IOS Press.

[13]      Ishiura S, Mabuchi Y, Urakami-Manaka Y, Isobe K, Tagawa K, Maruyama K, Sorimachi H, Suzuki K (1997) Proteases involved in the processing of the Alzheimer's disease amyloid precursor protein. In: Proteolysis In Cell Functions (Hopsu-Havu VK, JärvInen M, Kirschke H, eds), pp 507-512. BerlIn: IOS Press.

[12]      Kinbara K, Sorimachi H, Ishiura S, Suzuki K (1997) A skeletal muscle-specific calpain, p94, exists in myofibrils bound to connectin/titin. In: Proteolysis In Cell Functions (Hopsu-Havu VK, JärvInen M, Kirschke H, eds), pp 68-75. BerlIn: IOS Press.

[11]      Sorimachi H, Ishiura S, Suzuki K (1997) Structure and physiological function of calpains. Biochem J 328:721-732.

[10]      Sorimachi H, Kimura S, Kinbara K, Kazama J, Takahashi M, Yajima H, Ishiura S, Sasagawa N, Nonaka I, Sugita H, Maruyama K, Suzuki K (1996) Structure and physiological functions of ubiquitous and tissue-specific calpain species. Muscle-specific calpain, p94, interacts with connectin/titin. Adv Biophys 33:101-122.

[10]      Sorimachi H, Suzuki K (1998) μ-calpain. In: Handbook of Proteolytic enzymes (Barrett AJ, RawlIngs ND, Woessner JF, eds), pp 643-649: Academic Press.

[9]        Sorimachi H, Yoshizawa T, Suzuki K (1995) Molecular diversity and structure-function relationship of calpain. In: Advance in Biochemistry and Molecular Biology: ProceedIngs of the 11th FAOBMB Symposium on Biopolymers and Bioproducts.

[8]        Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S (1995) Calpain: novel family members, activation, and physiologic function. Biol Chem Hoppe Seyler 376:523-529.

[7]        Sorimachi H, Saido TC, Suzuki K (1994) New era of calpain research. Discovery of tissue-specific calpains. FEBS Lett 343:1-5.

[6]        Saido TC, Sorimachi H, Suzuki K (1994) Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J 8:814-822.

[5]        Sorimachi H, Suzuki K (1993) A novel calpain species, n-calpain, active at nM levels of calcium? In: Biological Functions of Proteases and Inhibitors (Katunuma N, Suzuki K, Travis J, Fritz H, eds), pp 35-46. Tokyo: Japan Scientific Societies Press.

[4]        Sorimachi H, Sorimachi N, Ishiura S, Suzuki K (1993) Identification and localization of a novel muscle-specific calpain, p94. In: Proteolysis and Protein Turnover (Bond JS, Barrett AJ, eds), pp 45-49. London: Portland Press Ltd.

[3]        Sorimachi H, Suzuki K (1992) Sequence comparison among muscle-specific calpain, p94, and calpain subunits. Biochim Biophys Acta 1160:55-62.

[2]        Suzuki K, Sorimachi H, Hata A, Ohno S, Emori Y, Kawasaki H, Saido T, Ohmi-Imajoh S, Akita Y (1990) Calcium dependent protease: A novel molecular species, regulation of gene expression, and activation at the cell membrane. In: Neurotoxicity of excitatory amino acids (Guidotti A, ed), pp 79-93. New York: Raven Press.

[1]        Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K (1990) A novel member of the calcium-dependent cysteine protease family. Biol Chem Hoppe Seyler 371 Suppl:171-176.

Review papers in Japanese

[49]      秦勝志, 小野弥子 (2018) カルパインファミリーは個性派揃い. 医学のあゆみ 267:1003-1008.

[48]     反町洋之, 小野弥子 (2016) カルパインは阻害すればよいのか？ 生化学 88:704-722.

[47]      反町洋之 (2016) 「カルパイン」. 生化学事典 (朝倉書店; 田中啓二、石浦章一、水島昇、谷口直之、遠藤玉夫、竹縄忠臣、伊藤俊樹、花岡文雄、塩見春彦編):in press.

[46]      反町洋之 (2015) カルパイン. 生体の科学 66:500-501.[pdf]

[45]      川井尚臣, 足立克仁, 反町洋之 (2015) 骨格筋症候群（上）－Ⅰ筋ジストロフィーおよび膜イオンチャネル異常症－肢帯型筋ジストロフィー－常染色体劣性型LGMD－LGMD2A（calpain 3異常症）. In: 別冊 日本臨床 新領域別症候群シリーズ, pp 105-110.

[44]      反町洋之 (2012) 『細胞が自分を食べるオートファジーの謎』水島昇／著 Book Review. 実験医学 30:523.[pdf]

[43]      反町洋之 (2012) 脳－分子・遺伝子・生理－石浦章一 他著 書評. 生化学 84:149.[pdf]

[42]      村田茂雄, 反町洋之 (2011) 細胞内分解系によるリノベーションの分子機構に迫る. 実験医学 29:1850-1854.

[41]      反町洋之, 秦勝志, 小野弥子 (2011) カルパインの組織機能論. 実験医学 29:1882-1890.[pdf]

[40]      反町洋之, 秦勝志, 小野弥子 (2011) 第1節・第4項「カルパイン」. モデル動物利用マニュアル< 生物機能モデルと新しいリソース・リサーチツール >(株式会社LIC; 小幡裕一、城石俊彦、芹川忠夫、田中啓二、米川博通編):pp.232-248.[pdf]

[39]      小野弥子, 反町洋之 (2011) 骨格筋特異的カルパイン-3の活性制御因子は細胞内Na⁺～例外か多様性か. 化学と生物 49:229-231.[pdf]

[38]      反町洋之, 小野弥子 (2011) 肢帯型筋ジストロフィーの発症機構. 生体の科学 62:95-99.[pdf]

[37]      秦勝志, 反町洋之 (2011) 胃粘膜防御に果たすカルパインの役割. 日本臨床 69:1116-1122.[pdf]

[36]      反町洋之 (2010) カルパインの機能不全と疾患. Medical Science Digest 36:706-710.[pdf]

[35]      反町洋之 (2010) 「エステラーゼ」, 「STAT」, 「エラスターゼ」, 「塩基性タンパク質」, 「カゼイン」, 「カテプシン」, 「キモシン」, 「キモトリプシノーゲン」, 「キモトリプシン」, 「グリセルアルデヒド-3-リン酸デヒドロゲナーゼ」, 「グリセロール-3-リン酸デヒドロゲナーゼ」, 「ギャップ結合タンパク質」, 「コラーゲン」, 「コラゲナーゼ」, 「ズブチリシン」, 「ゼラチン」, 「組織解離（マセレーション）酵素」, 「組織プラスミノーゲン活性化因子」, 「タンパク質代謝」, 「タンパク質多型」, 「タンパク質分解」, 「トロンビン」, 「ヌクレオヒストン」, 「ヌクレオプロタミン」, 「ヒストン」, 「非ヒストンクロマチンタンパク質」, 「プロテアーゼ」, 「プロテアーゼ阻害剤」, 「プロテイナーゼ」, 「プロテイナーゼK」, 「ボーマン・バークインヒビター」, 「マトリックスメタロプロテアーゼ」, 「融合タンパク質」, 「誘導適合仮説」, 「レニン 」生物学辞典 (東京化学同人; 石川統、黒岩常祥、塩見正衞、松本忠夫、守隆夫、八杉貞雄、山本正幸 編), pp134, 134, 152, 157, 223, 233-234, 297, 297-298, 298, 352, 353, 462, 466, 466, 696, 742, 785, 786, 840-841, 841, 842, 953, 987, 987, 1072, 1084, 1147, 1147, 1147, 1147-1148, 1215, 1236, 1290, 1295-1296, 1366.

[34]      尾嶋孝一, 反町洋之 (2008) カルパイン3異常症（カルパイノパチー）. Clinical Neurosci 26:154-155.[pdf]

[33]      小野弥子, 反町洋之 (2008) カルパインの生理機能とその不全による病態「カルパイノパチー」. 実験医学 26:306-315.[pdf]

[32]      反町洋之 (2008) 「今話題の重要なプロテオリシス」概論. 実験医学 26:294-299.[pdf]

[31]      秦勝志, 反町洋之 (2007) 「モジュレータープロテアーゼ」カルパインと細胞内膜系との新しい展開. 生化学 79:46-50.[pdf]

[30]      尾嶋孝一, 反町洋之, 木村澄子 (2005) 「筋弾性タンパク質の国際シンポジウム」報告記. 生体の科学 56:157-159.

[29]      小野弥子, 反町洋之 (2005) 神経細胞死の分子機構とCa²⁺依存性プロテアーゼカルパイン. 医学のあゆみ 215:811-817.[pdf]

[28]      小野弥子, 反町洋之 (2004) カルパインの機能制御と筋ジストロフィー. 実験医学 22:198-204.

[27]      小野弥子, 川畑順子, 反町洋之 (2004) 骨格筋特異的カルパインp94/カルパイン3と肢帯型筋ジストロフィー. ゲノム医学 4:27-34.

[26]      反町洋之, 川畑順子 (2003) カルパインと病態―構造活性相関からの考察―. 薬理学会誌 122:21-29.

[25]      鈴木紘一, 秦勝志, 反町洋之 (2002) カルパインファミリーメンバーの機能と疾患. Mol Med 39:10月17日.

[24]      反町洋之 (2002) 蛋白質「分解」酵素の「異常」による筋ジストロフィー－カルパイノパチー－. 臨床検査 46:555-560.

[23]      反町洋之 (2001) 筋ジストロフィー症とカルパイン. 蛋白質核酸酵素 46:1772-1780.

[22]      反町洋之 (2001) 骨格筋特異的カルパインの分子機能. 生体の科学 52:280-286.

[21]      秦勝志, 反町洋之, 鈴木紘一 (2001) カルパインスーパーファミリーの構造と機能. 生化学 73:1129-1140.

[20]      反町洋之 (2001) ゲノムプロジェクトによるカルパインスーパーファミリーの同定―分子構造と昨日の多様性，その疾病への応用をめざして―. "農業および園芸," 76:883-890.

[19]      反町洋之 (2000) カルパインおよびそのホモログの構造と機能. 生化学 72:1297-1315.

[18]      反町洋之, 小野弥子, 鈴木紘一 (2000) 肢帯型筋ジストロフィー. 神経進歩 44:189-203.

[17]      反町洋之, 小野弥子, 鈴木紘一 (2000) 筋ジストロフィー症. 「タンパク質分解 -分子機構と細胞機能-」（鈴木紘一・木南英紀・田中啓二、編） シュプリンガー・フェアラーク東京、東京:pp.157-164.

[16]      小野弥子, 反町洋之, 鈴木紘一 (2000) カルパイン-カルパスタチン系. 「タンパク質分解 -分子機構と細胞機能-」（鈴木紘一・木南英紀・田中啓二、編） シュプリンガー・フェアラーク東京、東京:pp.59-70.

[15]      反町洋之, 中川和博 (2000) カルシウムと分解シグナル. 「神経難病の分子機構」（石浦章一、編） シュプリンガー・フェアラーク東京、東京:pp.94-103.

[14]      反町洋之, 鈴木紘一 (1998) Ca²⁺結合タンパク質としてのカルパイン. 蛋白質核酸酵素 43:1666-1674.

[13]      反町洋之, 鈴木紘一 (1997) 酵母Two-Hybrid系を用いたタンパク質間相互作用の解析. 蛋白質核酸酵素 42:2433-2440.

[12]      田川一彦, 反町洋之, 脊山洋右, 石浦章一, 鈴木紘一 (1997) カルパインスーパーファミリーとカルパインに相互作用するタンパク質. 蛋白質核酸酵素 42:2165-2174.

[11]      ウィリアム・R・クラーク（著）,反町洋之（訳）,反町典子（訳）(1997) 「免疫の反逆」, 三田出版, 東京

[10]        反町洋之 (1996) 筋ジストロフィーに帰ってきたカルパイン. バイオインダストリー 53:1057-1058.

[9]        反町洋之, 鈴木紘一 (1996) カルパイン制御のシャペロニン機能. 医学のあゆみ 178:211-215.

[8]        嶋田弘子, 反町洋之, 鈴木紘一 (1996) Long PCRを用いたsite-directed mutagenesis. 実験医学 14:2673-2676.

[7] 　石浦章一, 笹川昇, 斎藤直人, 小池恒, 渡辺知司, 下川雅丈, 臼杵扶佐子, 丸山敬, 反町洋之, 鈴木紘一 (1996) 筋緊張性ジストロフィーとミオトニンキナーゼ. 神経化学 35:204-205.

[6]        石浦章一, 笹川昇, 反町洋之, 鈴木紘一 (1995) CTGリピートを非翻訳領域にもつ筋緊張性ジストロフィー. 実験医学 13:77-79.

[5]        反町洋之, 鈴木紘一 (1995) カルパインスーパーファミリーの分子多様性と生理機能. 実験医学 13:1045-1052.

[4]       石浦章一, 笹川昇, 斎藤直人, 小池恒, 反町洋之, 鈴木紘一, 下川雅丈, 臼杵扶佐子, 中瀬浩史, 鎌倉恵子, 丸山敬, 荒畑喜一 (1995) Myotonin protein kinase. 臨床神経学 35:1482-1483.

[3]        鈴木紘一, 反町洋之, 伴真伊, 石浦章一 (1994) 普遍的および組織特異的カルパイン. 運動生化学 6:50-56.

[2]        反町洋之, 笹川昇, 丸山敬, 荒畑喜一, 石浦章一, 鈴木紘一 (1994) Myotonic dystrophyとCTG-リピート. 臨床神経学 34:1230-1232.

[1]        反町洋之 (1993) カルパイン研究の新しい局面. 生化学 65:1170-1174.