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Volumn 41, Issue 5, 2010, Pages 318-325

Proteases of the calpain family: Structure and functions

Author keywords

calpains; functions; proteolysis; regulation

Indexed keywords


EID: 77957374607     PISSN: 10623604     EISSN: 16083326     Source Type: Journal    
DOI: 10.1134/S1062360410050073     Document Type: Article
Times cited : (13)

References (64)
  • 1
    • 34548022009 scopus 로고
    • (Chemistry of Proteolysis), Moscow: Mir
    • Antonov, V. K., Khimiya proteoliza (Chemistry of Proteolysis), Moscow: Mir, 1983.
    • (1983) Khimiya Proteoliza
    • Antonov, V.K.1
  • 2
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the Murine Calpain SC Subunit Gene, Capn4: Calpain is Essential for Embryonic Development but Not for Cell Growth and Division
    • Arthur, J. S. C., Elce, J. S., Hegadorn, C., et al., Disruption of the Murine Calpain SC Subunit Gene, Capn4: Calpain is Essential for Embryonic Development but Not for Cell Growth and Division, Mol. Cell Biol., 2000, vol. 20, pp. 4474-4481.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 4474-4481
    • Arthur, J.S.C.1    Elce, J.S.2    Hegadorn, C.3
  • 3
    • 0035008875 scopus 로고    scopus 로고
    • Disruption of the Mouse μ-Calpain Gene Reveals an Essential Role in Platelet Function
    • Azam, M., Andarabi, S., Sahr, K., et al., Disruption of the Mouse μ-Calpain Gene Reveals an Essential Role in Platelet Function, Mol. Cell Biol., 2001, vol. 21, pp. 2213-2220.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2213-2220
    • Azam, M.1    Andarabi, S.2    Sahr, K.3
  • 4
    • 19744377715 scopus 로고    scopus 로고
    • Overexpression of Calpastatin Inhibits L8 Myoblast Fusion
    • Barnoy, S., Maki, M., and Kosower, N. S., Overexpression of Calpastatin Inhibits L8 Myoblast Fusion, Biochem. Biophys. Res. Commun., 2005, vol. 332, pp. 697-701.
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , pp. 697-701
    • Barnoy, S.1    Maki, M.2    Kosower, N.S.3
  • 6
    • 17444384218 scopus 로고    scopus 로고
    • The Expression of Calpain 1 and Calpain 2 in Spermatogenic Cells and Spermatozoa of the Mouse
    • Ben-Aharon, I., Brown, P. R., Etkovitz, N., et al., The Expression of Calpain 1 and Calpain 2 in Spermatogenic Cells and Spermatozoa of the Mouse, Reproduction, 2005, vol. 129, pp. 435-442.
    • (2005) Reproduction , vol.129 , pp. 435-442
    • Ben-Aharon, I.1    Brown, P.R.2    Etkovitz, N.3
  • 7
    • 31544441649 scopus 로고    scopus 로고
    • Understanding Muscle Architectural Adaptation: Macro- and Micro-Level Research
    • Blazevich, A. J. and Sharp, N. C., Understanding Muscle Architectural Adaptation: Macro- and Micro-Level Research, Cells Tiss. Organs, 2005, vol. 181, no. 1, pp. 1-10.
    • (2005) Cells Tiss. Organs , vol.181 , Issue.1 , pp. 1-10
    • Blazevich, A.J.1    Sharp, N.C.2
  • 10
    • 0036208170 scopus 로고    scopus 로고
    • Protein Degradation during Aging: The Lysosome-, the Calpain and the Proteasome-Dependent Cellular Proteolytic Systems
    • Chondrogianni, N., Fragoulis, E. G., and Gonos, E. S., Protein Degradation during Aging: The Lysosome-, the Calpain and the Proteasome-Dependent Cellular Proteolytic Systems, Biogerontology, 2002, vol. 3, pp. 121-123.
    • (2002) Biogerontology , vol.3 , pp. 121-123
    • Chondrogianni, N.1    Fragoulis, E.G.2    Gonos, E.S.3
  • 11
    • 0001110114 scopus 로고    scopus 로고
    • Direct Cleavage by the Calcium-Activated Protease Calpain can Lead to Inactivation of Caspases
    • Chua, B. T., Guo, K., and Li, P., Direct Cleavage by the Calcium-Activated Protease Calpain can Lead to Inactivation of Caspases, J. Biol. Chem., 2000, vol. 275, pp. 5131-5135.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5131-5135
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 12
    • 0028169864 scopus 로고
    • 2+-Dependent Proteases (Calpains) and Muscle Cell Differentiation
    • 2+-Dependent Proteases (Calpains) and Muscle Cell Differentiation, Biochim. Biophys. Acta, 1994, vol. 1223, pp. 170-178.
    • (1994) Biochim. Biophys. Acta , vol.1223 , pp. 170-178
    • Cottin, P.1    Brustis, J.J.2    Poussard, S.3
  • 13
    • 36148990505 scopus 로고    scopus 로고
    • The Calpains: Modular Designs and Functional Diversity
    • Croall, D. E. and Ersfeld, K., The Calpains: Modular Designs and Functional Diversity, Genome Biol., 2007, vol. 8, pp. 218. 1-218. 11.
    • (2007) Genome Biol. , vol.8 , pp. 1-11
    • Croall, D.E.1    Ersfeld, K.2
  • 14
    • 0017101439 scopus 로고
    • 2+-Activated Protease Possibly Involved in Myofibrillar Protein Turnover. Purification from Porcine Muscle
    • 2+-Activated Protease Possibly Involved in Myofibrillar Protein Turnover. Purification from Porcine Muscle, Biochemistry, 1976, vol. 15, pp. 2150-2158.
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3
  • 15
    • 0032722011 scopus 로고    scopus 로고
    • Diverse mRNA Expression Patterns of the Mouse Calpain Genes Capn5, Capn6, and Capn11 during Development
    • Dear, T. N. and Boehm, T., Diverse mRNA Expression Patterns of the Mouse Calpain Genes Capn5, Capn6, and Capn11 during Development, Mech. Devel., 1999, vol. 89, pp. 201-209.
    • (1999) Mech. Devel. , vol.89 , pp. 201-209
    • Dear, T.N.1    Boehm, T.2
  • 16
    • 0036067552 scopus 로고    scopus 로고
    • Estrogen Regulates a Tissue-Specific Calpain in the Anterior Pituitary
    • Duan, W. R., Ito, M., and Lee, E. J., Estrogen Regulates a Tissue-Specific Calpain in the Anterior Pituitary, Biochem. Biophys. Res. Commun., 2002, vol. 295, pp. 261-266.
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 261-266
    • Duan, W.R.1    Ito, M.2    Lee, E.J.3
  • 17
    • 33746129198 scopus 로고    scopus 로고
    • Calpain 3: a Key Regulator of the Sarcomere?
    • Duguez, S., Bartoli, M., and Richard, I., Calpain 3: a Key Regulator of the Sarcomere?, FEBS J, 2006, vol. 273, pp. 3427-3436.
    • (2006) FEBS J , vol.273 , pp. 3427-3436
    • Duguez, S.1    Bartoli, M.2    Richard, I.3
  • 18
    • 33644558362 scopus 로고    scopus 로고
    • m-Calpain Is Required for Preimplantation Embryonic Development in Mice
    • Dutt, P., Croall, D. E., and Arthur, J. S., m-Calpain Is Required for Preimplantation Embryonic Development in Mice, BMC Devel. Biol., 2006, vol. 6, p. 3.
    • (2006) BMC Devel. Biol. , vol.6 , pp. 3
    • Dutt, P.1    Croall, D.E.2    Arthur, J.S.3
  • 19
    • 0021285005 scopus 로고
    • 2+-Activated Proteinase in the Rat. Quantification by Immunoassay in the Uterus during Pregnancy and Involution, and in Other Tissues
    • 2+-Activated Proteinase in the Rat. Quantification by Immunoassay in the Uterus during Pregnancy and Involution, and in Other Tissues, Biochem. J., 1984, vol. 220, pp. 507-512.
    • (1984) Biochem. J. , vol.220 , pp. 507-512
    • Elce, J.S.1    Baenziger, J.E.2    Young, D.C.3
  • 20
    • 27544455512 scopus 로고
    • Development Initiation during Fertilization
    • Epel', D., Development Initiation during Fertilization, Ontogenez, 1992, vol. 23, pp. 213-227.
    • (1992) Ontogenez , vol.23 , pp. 213-227
    • Epel', D.1
  • 21
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the Chase: Calpain Proteases in Cell Motility
    • Glading, A., Lauffenburger, D. A., and Wells, A., Cutting to the Chase: Calpain Proteases in Cell Motility, Trends Cell Biol., 2002, vol. 12, pp. 46-54.
    • (2002) Trends Cell Biol. , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 22
    • 0025868336 scopus 로고
    • Studies of the α-Actinin/Actin Interaction in the Z-Disk by using Calpain
    • Goll, D. E., Dayton, W. R., Singh, I., et al., Studies of the α-Actinin/Actin Interaction in the Z-Disk by using Calpain, J. Biol. Chem., 1991, vol. 266, pp. 8501-8510.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3
  • 24
    • 32544454165 scopus 로고    scopus 로고
    • Expression and Immunolocalization of the Calpain-Calpastatin System during Parthenogenetic Activation and Fertilization in the Rat Egg
    • Haim, K., Ben-Aharon, I., and Shalgi, R., Expression and Immunolocalization of the Calpain-Calpastatin System during Parthenogenetic Activation and Fertilization in the Rat Egg, Reproduction, 2006, vol. 131, pp. 35-43.
    • (2006) Reproduction , vol.131 , pp. 35-43
    • Haim, K.1    Ben-Aharon, I.2    Shalgi, R.3
  • 25
    • 5644280075 scopus 로고    scopus 로고
    • Differential Compartmentalization of the Calpain/Calpastatin Network with the Endoplasmic Reticulum and Golgi Apparatus
    • Hood, J. L., Brooks, W. H., and Roszman, T. L., Differential Compartmentalization of the Calpain/Calpastatin Network with the Endoplasmic Reticulum and Golgi Apparatus, J. Biol. Chem., 2004, vol. 279, pp. 43126-43135.
    • (2004) J. Biol. Chem. , vol.279 , pp. 43126-43135
    • Hood, J.L.1    Brooks, W.H.2    Roszman, T.L.3
  • 26
    • 0026801930 scopus 로고
    • Gene Expression of Calpains and Their Specific Endogenous Inhibitor, Calpastatin, in Skeletal Muscle of Fed and Fasted Rabbits
    • Ilian, M. A. and Forsberg, N. E., Gene Expression of Calpains and Their Specific Endogenous Inhibitor, Calpastatin, in Skeletal Muscle of Fed and Fasted Rabbits, Biochem. J., 1992, vol. 287, pp. 163-171.
    • (1992) Biochem. J. , vol.287 , pp. 163-171
    • Ilian, M.A.1    Forsberg, N.E.2
  • 27
    • 0032783288 scopus 로고    scopus 로고
    • The Evolution of the Calpain Family as Reflected in Paralogous Chromosome Regions
    • Jékely, G. and Friedrich, P., The Evolution of the Calpain Family as Reflected in Paralogous Chromosome Regions, J. Mol. Evol., 1999, vol. 49, no. 2, pp. 272-281.
    • (1999) J. Mol. Evol. , vol.49 , Issue.2 , pp. 272-281
    • Jékely, G.1    Friedrich, P.2
  • 28
    • 0034507993 scopus 로고    scopus 로고
    • Proteolytic Regulation of Apoptosis
    • Kidd, V. J., Lahti, J. M., and Teitz, T., Proteolytic Regulation of Apoptosis, Cell Devel. Biol., 2000, vol. 11, pp. 191-201.
    • (2000) Cell Devel. Biol. , vol.11 , pp. 191-201
    • Kidd, V.J.1    Lahti, J.M.2    Teitz, T.3
  • 29
    • 0033393515 scopus 로고    scopus 로고
    • Intracellular Proteolysis
    • Kirschner, M., Intracellular Proteolysis, TCB, 2000, vol. 9, no. 12, pp. M42-M45.
    • (2000) Tcb , vol.9 , Issue.12
    • Kirschner, M.1
  • 30
    • 0024428624 scopus 로고
    • Calcium Dependent Cysteine Proteinase is a Precursor of a Chemotactic Factor for Neutrophils
    • Kunimatsu, M., Higashiyama, S., Sato, K., et al., Calcium Dependent Cysteine Proteinase is a Precursor of a Chemotactic Factor for Neutrophils, Biochem. Biophys. Res. Commun., 1989, vol. 164, pp. 875-882.
    • (1989) Biochem. Biophys. Res. Commun. , vol.164 , pp. 875-882
    • Kunimatsu, M.1    Higashiyama, S.2    Sato, K.3
  • 31
    • 21144454581 scopus 로고    scopus 로고
    • Mutation in the Arabidopsis thaliana DEK1 Calpain Gene Perturbs Endosperm and Embryo Development While Over-Expression Affects Organ Development Globally
    • Lid, S., Olsen, L., Nestestog, R., et al., Mutation in the Arabidopsis thaliana DEK1 Calpain Gene Perturbs Endosperm and Embryo Development While Over-Expression Affects Organ Development Globally, Planta, 2005, vol. 221, pp. 339-351.
    • (2005) Planta , vol.221 , pp. 339-351
    • Lid, S.1    Olsen, L.2    Nestestog, R.3
  • 32
    • 0034613338 scopus 로고    scopus 로고
    • Antisense RNA-Mediated Deficiency of the Calpain Protease, NCL-4, in NIH3T3 Cells is Associated with Neoplastic Transformation and Tumorigenesis
    • Liu, K., Li, L., and Cohen, S. N., Antisense RNA-Mediated Deficiency of the Calpain Protease, NCL-4, in NIH3T3 Cells is Associated with Neoplastic Transformation and Tumorigenesis, J. Biol. Chem., 2000, vol. 275, pp. 31093-31098.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31093-31098
    • Liu, K.1    Li, L.2    Cohen, S.N.3
  • 33
    • 0037067162 scopus 로고    scopus 로고
    • Participation of the Conventional Calpains in Apoptosis
    • Lu, T., Xu, Y., and Mericle, M. T., Participation of the Conventional Calpains in Apoptosis, Biochim. Biophys. Acta, 2002, vol. 1590, pp. 16-26.
    • (2002) Biochim. Biophys. Acta , vol.1590 , pp. 16-26
    • Lu, T.1    Xu, Y.2    Mericle, M.T.3
  • 34
    • 0033658427 scopus 로고    scopus 로고
    • Calcium-Activated Proteinase in Gametes of the Green See Urchin (Strongylocentrotus droebachiensis)
    • Mukhin, V. A., Nemova, N. N., Kyaivyaryainen, E. I., et al., Calcium-Activated Proteinase in Gametes of the Green See Urchin (Strongylocentrotus droebachiensis), Zhurn. Evolyuts. Biokhim. Fiziol., 2000, vol. 36, pp. 3-6.
    • (2000) Zhurn. Evolyuts. Biokhim. Fiziol. , vol.36 , pp. 3-6
    • Mukhin, V.A.1    Nemova, N.N.2    Kyaivyaryainen, E.I.3
  • 35
    • 33644824974 scopus 로고    scopus 로고
    • μ-Calpain and Calpain-3 are not Autolyzed with Exhaustive Exercise in Humans
    • Murphy, R. M., Snow, R. J., and Lamb, G. D., μ-Calpain and Calpain-3 are not Autolyzed with Exhaustive Exercise in Humans, Am. J. Physiol. Cell Physiol., 2006, vol. 290, pp. 116-122.
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290 , pp. 116-122
    • Murphy, R.M.1    Snow, R.J.2    Lamb, G.D.3
  • 36
    • 0034698878 scopus 로고    scopus 로고
    • Cross-Talk between Two Cysteine Protease Families. Activation of Caspase-12 by Calpain in Apoptosis
    • Nakagawa, T. and Yuan, J., Cross-Talk between Two Cysteine Protease Families. Activation of Caspase-12 by Calpain in Apoptosis, J. Cell Biol., 2000, vol. 150, pp. 887-894.
    • (2000) J. Cell Biol. , vol.150 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 37
    • 0026764130 scopus 로고
    • Specific Increase in Calcium-Activated Neutral Protease with Low Calcium Sensitivity (M-Calpain) in Proerythroblastic K562 Cell Line Cells Induced to Differentiation by Phorbol 12-Myristate 13-Acetate
    • Nakamura, M., Mori, M., Morishita, Y., et al., Specific Increase in Calcium-Activated Neutral Protease with Low Calcium Sensitivity (M-Calpain) in Proerythroblastic K562 Cell Line Cells Induced to Differentiation by Phorbol 12-Myristate 13-Acetate, Ex. Cell Res., 1992, vol. 200, pp. 513-522.
    • (1992) Ex. Cell Res. , vol.200 , pp. 513-522
    • Nakamura, M.1    Mori, M.2    Morishita, Y.3
  • 38
    • 0022056022 scopus 로고
    • Acid Proteinase from Rainbow Trout Eggs
    • Nemova, N. N. and Sidorov, V. S., Acid Proteinase from Rainbow Trout Eggs, Ukr. Biokhim. Zh., 1985, vol. 3, pp. 22-26.
    • (1985) Ukr. Biokhim. Zh. , vol.3 , pp. 22-26
    • Nemova, N.N.1    Sidorov, V.S.2
  • 39
    • 77957343548 scopus 로고
    • Lysosomal Proteases in Embryogenesis of Salmon Salmo salar L
    • Nemova, N. N. and Sidorov, V. S., Lysosomal Proteases in Embryogenesis of Salmon Salmo salar L., Zhurn. Evolyuts. Biokhim. Fiziol., 1984, vol. 20, pp. 576-580.
    • (1984) Zhurn. Evolyuts. Biokhim. Fiziol , vol.20 , pp. 576-580
    • Nemova, N.N.1    Sidorov, V.S.2
  • 40
    • 77957363202 scopus 로고
    • Activity of Lysosomal Proteases in Early Development of Artemia salina
    • (Biochemistry of Ectothermic and Endothermic Organisms), Petrozavodsk: KarNTs
    • Nemova, N. N. and Vysotskaya, R. U., Activity of Lysosomal Proteases in Early Development of Artemia salina, in Biokhimiya ektoi endotermnykh organizmov (Biochemistry of Ectothermic and Endothermic Organisms), Petrozavodsk: KarNTs, 1989, pp. 112-116.
    • (1989) Biokhimiya Ektoi Endotermnykh Organizmov , pp. 112-116
    • Nemova, N.N.1    Vysotskaya, R.U.2
  • 42
    • 77957333605 scopus 로고    scopus 로고
    • Nemova, N. N., Kyaivyaryainen, E. I., Krupnova, M. Yu., et al., Mechanisms of Proteolytic Regulation in Development of Aquatic Animals, Vopr. Rybolovstva, 2001, Suppl. 1, pp. 189-192.
  • 43
    • 27544468424 scopus 로고
    • Calcium-Activated Proteinase in Embryogenesis of Salmon Salmo salar L
    • Nemova, N. N., Kyaivyaryainen, E. I., Mosolov, V. V., et al., Calcium-Activated Proteinase in Embryogenesis of Salmon Salmo salar L., Zh. Evol. Biokhim. Fiziol., 1993, vol. 3, pp. 231-235.
    • (1993) Zh. Evol. Biokhim. Fiziol , vol.3 , pp. 231-235
    • Nemova, N.N.1    Kyaivyaryainen, E.I.2    Mosolov, V.V.3
  • 44
    • 77957348151 scopus 로고
    • Lysosomal Digestion of Proteins of Organs of Salmon (Salmo salar L.) Kept in Nurse Ponds in the Prespawning Period during Fasting
    • Nemova, N. N., Sidorov, V. S., and Ripatti, P. O., Lysosomal Digestion of Proteins of Organs of Salmon (Salmo salar L.) Kept in Nurse Ponds in the Prespawning Period during Fasting, Vopr. Ikhtiol., 1980, vol. 120, pp. 180-182.
    • (1980) Vopr. Ikhtiol. , vol.120 , pp. 180-182
    • Nemova, N.N.1    Sidorov, V.S.2    Ripatti, P.O.3
  • 45
    • 0344406973 scopus 로고    scopus 로고
    • Mutation in a Calpain-Like Protease Affects the Posttranslational Mannosylation of Phosphatases in Aspergillus nidulans
    • Nozawa, S. R., May, G. S., Martinez-Rossi, N. M., et al., Mutation in a Calpain-Like Protease Affects the Posttranslational Mannosylation of Phosphatases in Aspergillus nidulans, Fungal. Genet. Biol., 2003, vol. 38, pp. 220-227.
    • (2003) Fungal. Genet. Biol. , vol.38 , pp. 220-227
    • Nozawa, S.R.1    May, G.S.2    Martinez-Rossi, N.M.3
  • 48
    • 11144273211 scopus 로고    scopus 로고
    • Identification and Molecular Characterization of the Rainbow Trout Calpains (Capn1 and Capn2): Their Expression in Muscle Wasting during Starvation
    • Salem, M., Nath, J., Rexroad, C. E., et al., Identification and Molecular Characterization of the Rainbow Trout Calpains (Capn1 and Capn2): Their Expression in Muscle Wasting during Starvation, Comp. Biochem. Physiol. B. Biochem. Mol. Biol., 2005, vol. 140, pp. 63-71.
    • (2005) Comp. Biochem. Physiol. B. Biochem. Mol. Biol. , vol.140 , pp. 63-71
    • Salem, M.1    Nath, J.2    Rexroad, C.E.3
  • 49
    • 0034714442 scopus 로고    scopus 로고
    • Breakdown of Cytoskeletal Proteins during Meiosis of Starfish Oocytes and Proteolysis Induced by Calpain
    • Santella, L., Kyozuka, K., Hoving, S., et al., Breakdown of Cytoskeletal Proteins during Meiosis of Starfish Oocytes and Proteolysis Induced by Calpain, Exp. Cell Res., 2000, vol. 259, pp. 117-126.
    • (2000) Exp. Cell Res. , vol.259 , pp. 117-126
    • Santella, L.1    Kyozuka, K.2    Hoving, S.3
  • 50
    • 77957372148 scopus 로고    scopus 로고
    • An Emerging Role for Calpain in Skeletal Muscle Adaptation
    • Shewchuk, L. D., An Emerging Role for Calpain in Skeletal Muscle Adaptation, Diss. Abstr. Int., B, 2003, vol. 63, no. 12, p. 5629.
    • (2003) Diss. Abstr. Int., B , vol.63 , Issue.12 , pp. 5629
    • Shewchuk, L.D.1
  • 51
    • 0034655551 scopus 로고    scopus 로고
    • Proteolysis in Caenorhabditis elegans Sex Determination: Cleavage of TRA-2A by TRA-3
    • Sokol, S. B. and Kuwabara, P. E., Proteolysis in Caenorhabditis elegans Sex Determination: Cleavage of TRA-2A by TRA-3, Genes Devel., 2000, vol. 14, pp. 901-906.
    • (2000) Genes Devel. , vol.14 , pp. 901-906
    • Sokol, S.B.1    Kuwabara, P.E.2
  • 52
    • 0024369426 scopus 로고
    • Molecular Cloning of a Novel Mammalian Calcium-Dependent Protease Distinct from Both m- and μ-Types. Specific Expression of the mRNA in Skeletal Muscle
    • Sorimachi, H., Imajoh-Ohmi, S., Emori, Y., et al., Molecular Cloning of a Novel Mammalian Calcium-Dependent Protease Distinct from Both m- and μ-Types. Specific Expression of the mRNA in Skeletal Muscle, J. Biol. Chem., 1989, vol. 264, pp. 20106-20111.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3
  • 53
    • 0031452173 scopus 로고    scopus 로고
    • Structure and Physiological Function of Calpains
    • Sorimachi, H., Ishiura, S., and Suzuki, K., Structure and Physiological Function of Calpains, Biochem. J., 1997, vol. 328, pp. 721-732.
    • (1997) Biochem. J. , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 54
    • 12944300453 scopus 로고    scopus 로고
    • The Crystal Structure of Calcium-Free Human m-Calpain Suggests an Electrostatic Switch Mechanism for Activation by Calcium
    • Strobl, S., Fernandez-Catalan, C., Braun, M., et al., The Crystal Structure of Calcium-Free Human m-Calpain Suggests an Electrostatic Switch Mechanism for Activation by Calcium, Proc. Natl. Acad. Sci. USA, 2000, vol. 97, pp. 588-592.
    • (2000) Proc. Natl. Acad.Sci. USA , vol.97 , pp. 588-592
    • Strobl, S.1    Fernandez-Catalan, C.2    Braun, M.3
  • 55
    • 0842328803 scopus 로고    scopus 로고
    • Structure, Activation, and Biology of Calpain
    • Suzuki, K., Hata, S., and Kawabata, Y., Structure, Activation, and Biology of Calpain, Diabetes, 2004, vol. 53, Suppl. 1, pp. 12-18.
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1 , pp. 12-18
    • Suzuki, K.1    Hata, S.2    Kawabata, Y.3
  • 57
    • 33745686005 scopus 로고    scopus 로고
    • Conditional Disruption of Ubiquitous Calpains in the Mouse
    • Tan, Y., Dourdin, N., Wu, C., et al., Conditional Disruption of Ubiquitous Calpains in the Mouse, Genesis, 2006, vol. 44, pp. 297-303.
    • (2006) Genesis , vol.44 , pp. 297-303
    • Tan, Y.1    Dourdin, N.2    Wu, C.3
  • 58
    • 0037066395 scopus 로고    scopus 로고
    • The Calpain System in Human Placenta
    • Thompson, V. F., Saldaña, S., Cong, J., et al., The Calpain System in Human Placenta, Life Sci., 2002, vol. 70, pp. 2493-2508.
    • (2002) Life Sci. , vol.70 , pp. 2493-2508
    • Thompson, V.F.1    Saldaña, S.2    Cong, J.3
  • 60
    • 0029044893 scopus 로고
    • Inflammatory Cell Response to Acute Muscle Injury. Review
    • Tidball, J. G., Inflammatory Cell Response to Acute Muscle Injury. Review, Med. Sci. Sports Exerc., 1995, vol. 27, pp. 1022-1032.
    • (1995) Med. Sci. Sports Exerc. , vol.27 , pp. 1022-1032
    • Tidball, J.G.1
  • 62
    • 0024326801 scopus 로고
    • Specific Proteolysis of the C-Mos Proto-Oncogene Product by Calpain in Fertilization of Xenopus Eggs
    • Watanabe, N., van De Woude, G. F., and Ikawa, Y., Specific Proteolysis of the C-Mos Proto-Oncogene Product by Calpain in Fertilization of Xenopus Eggs, Nature, 1989, vol. 342, pp. 505-511.
    • (1989) Nature , vol.342 , pp. 505-511
    • Watanabe, N.1    van de Woude, G.F.2    Ikawa, Y.3
  • 63
    • 0033199115 scopus 로고    scopus 로고
    • Calpain Functions in a Caspase-Independent Manner to Promote Apoptosis-Like Events during Platelet Activation
    • Wolf, B. B., Goldstein, J. C., Stennicke, H. R., et al., Calpain Functions in a Caspase-Independent Manner to Promote Apoptosis-Like Events during Platelet Activation, Blood, 1999, vol. 94, pp. 1683-1692.
    • (1999) Blood , vol.94 , pp. 1683-1692
    • Wolf, B.B.1    Goldstein, J.C.2    Stennicke, H.R.3
  • 64
    • 0022402473 scopus 로고
    • Regulation of Protein Degradation in Muscle by Calcium. Evidence for Enhanced Nonlysosomal Proteolysis Associated with Elevated Cytosolic Calcium
    • Zeman, R. J., Kameyama, T., Matsumoto, K., et al., Regulation of Protein Degradation in Muscle by Calcium. Evidence for Enhanced Nonlysosomal Proteolysis Associated with Elevated Cytosolic Calcium, J. Biol. Chem., 1985, vol. 260, pp. 13619-13624.
    • (1985) J. Biol. Chem. , vol.260 , pp. 13619-13624
    • Zeman, R.J.1    Kameyama, T.2    Matsumoto, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.