메뉴 건너뛰기




Volumn 2, Issue 5, 2007, Pages 565-576

Comprehensive survey of p94/calpain 3 substances by comparative proteomics - Possible regulation of protein synthesis by p94

Author keywords

Calpain; Fodrin; iTRAQ; Proteolysis; Substrate

Indexed keywords

CALPAIN 3; DNA 26S; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 2; FILAMIN A; FODRIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE (NADP)(PHOSPHORYLATING); INITIATION FACTOR 3; KARYOPHERIN; KARYOPHERIN 7; LIPOCORTIN 1; LIPOCORTIN 2; SYNEXIN; THIOREDOXIN; TRIOSEPHOSPHATE ISOMERASE; UNCLASSIFIED DRUG; VIMENTIN;

EID: 34249657818     PISSN: 18606768     EISSN: None     Source Type: Journal    
DOI: 10.1002/biot.200700018     Document Type: Article
Times cited : (29)

References (47)
  • 3
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi, H., Ishiura, S., Suzuki, K., Structure and physiological function of calpains. Biochem. J. 1997, 328, 721-732.
    • (1997) Biochem. J , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 4
    • 0035008875 scopus 로고    scopus 로고
    • Disruption of the mouse mu-calpain gene reveals an essential role in platelet function
    • Azam, M., Andrabi, S. S., Sahr, K. E., Kamath, L. et al., Disruption of the mouse mu-calpain gene reveals an essential role in platelet function. Mol. Cell. Biol. 2001, 21, 2213-2220.
    • (2001) Mol. Cell. Biol , vol.21 , pp. 2213-2220
    • Azam, M.1    Andrabi, S.S.2    Sahr, K.E.3    Kamath, L.4
  • 5
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur, J. S., Elce, J. S., Hegadorn, C., Williams, K. et al., Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol. Cell Biol. 2000, 20, 4474-4481.
    • (2000) Mol. Cell Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4
  • 6
    • 33644558362 scopus 로고    scopus 로고
    • m-Calpain is required foi preimplantation embryonic development in mice
    • DOI:10.1186/1471-213X-6-3
    • Dutt, P., Croall, D. E., Arthur, S. C., De Veyra, T. et al., m-Calpain is required foi preimplantation embryonic development in mice. BMC Dev. Biol. 2006, 6, DOI:10.1186/1471-213X-6-3.
    • (2006) BMC Dev. Biol , vol.6
    • Dutt, P.1    Croall, D.E.2    Arthur, S.C.3    De Veyra, T.4
  • 7
    • 0033788531 scopus 로고    scopus 로고
    • The calpain small subunit gene is essential: Its inactivation results in embryonic lethality
    • Zimmerman, U. J., Boring, L., Pak, J. H., Mukerjee, N. et al., The calpain small subunit gene is essential: its inactivation results in embryonic lethality. IUBMB Life 2000, 50, 63-68.
    • (2000) IUBMB Life , vol.50 , pp. 63-68
    • Zimmerman, U.J.1    Boring, L.2    Pak, J.H.3    Mukerjee, N.4
  • 8
    • 0036798005 scopus 로고    scopus 로고
    • Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology
    • Spencer, M. J., Mellgren, R. L., Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology. Hum. Mol. Genet. 2002, 11, 2645-2655.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 2645-2655
    • Spencer, M.J.1    Mellgren, R.L.2
  • 9
    • 0037206901 scopus 로고    scopus 로고
    • Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans
    • Syntichaki, P., Xu, K., Driscoll, M., Tavernarakis, N., Specific aspartyl and calpain proteases are required for neurodegeneration in C. elegans. Nature 2002, 419, 939-944.
    • (2002) Nature , vol.419 , pp. 939-944
    • Syntichaki, P.1    Xu, K.2    Driscoll, M.3    Tavernarakis, N.4
  • 10
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: Evidence from calpastatin mutant mice
    • Takano, J., Tomioka, M., Tsubuki, S., Higuchi, M. et al., Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J. Biol. Chem. 2005, 280, 16175-16184.
    • (2005) J. Biol. Chem , vol.280 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3    Higuchi, M.4
  • 11
    • 16244401481 scopus 로고    scopus 로고
    • Spatial resolution of calpain-catalyzed proteolysis in focal cerebral ischemia
    • Kambe, A., Yokota, M., Saido, T. C., Satokata, I. et al., Spatial resolution of calpain-catalyzed proteolysis in focal cerebral ischemia. Brain Res. 2005, 1040, 36-43.
    • (2005) Brain Res , vol.1040 , pp. 36-43
    • Kambe, A.1    Yokota, M.2    Saido, T.C.3    Satokata, I.4
  • 12
    • 17644393902 scopus 로고    scopus 로고
    • Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors
    • Higuchi, M., Tomioka, M., Takano, J., Shirotani, K. et al., Distinct mechanistic roles of calpain and caspase activation in neurodegeneration as revealed in mice overexpressing their specific inhibitors. J. Biol. Chem. 2005, 280, 15229-15237.
    • (2005) J. Biol. Chem , vol.280 , pp. 15229-15237
    • Higuchi, M.1    Tomioka, M.2    Takano, J.3    Shirotani, K.4
  • 13
    • 4544297614 scopus 로고    scopus 로고
    • Role of proteases in the pathophysiology of cardiac disease
    • Singh, R. B., Dandekar, S. P., Elimban, V., Gupta, S. K. et al.. Role of proteases in the pathophysiology of cardiac disease. Mol. Cell. Biochem. 2004, 263, 241-256.
    • (2004) Mol. Cell. Biochem , vol.263 , pp. 241-256
    • Singh, R.B.1    Dandekar, S.P.2    Elimban, V.3    Gupta, S.K.4
  • 14
    • 33646081999 scopus 로고    scopus 로고
    • Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans
    • Artal-Sanz, M., Samara, C., Syntichaki, P., Tavernarakis, N., Lysosomal biogenesis and function is critical for necrotic cell death in Caenorhabditis elegans. J. Cell Biol. 2006, 173, 231-239.
    • (2006) J. Cell Biol , vol.173 , pp. 231-239
    • Artal-Sanz, M.1    Samara, C.2    Syntichaki, P.3    Tavernarakis, N.4
  • 15
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: A therapeutic strategy targeting multiple disease states
    • Carragher, N. O., Calpain inhibition: a therapeutic strategy targeting multiple disease states. Curr. Pharm. Des. 2006, 12, 615-638.
    • (2006) Curr. Pharm. Des , vol.12 , pp. 615-638
    • Carragher, N.O.1
  • 16
    • 26644447992 scopus 로고    scopus 로고
    • Chlortetracycline and demeclocycline inhibit calpains and protect mouse neurons against glutamate toxicity and cerebral ischemia
    • Jiang, S. X., Lertvorachon, J., Hou, S. T., Konishi, Y. et al., Chlortetracycline and demeclocycline inhibit calpains and protect mouse neurons against glutamate toxicity and cerebral ischemia. J. Biol. Chem. 2005, 280, 33811-33818.
    • (2005) J. Biol. Chem , vol.280 , pp. 33811-33818
    • Jiang, S.X.1    Lertvorachon, J.2    Hou, S.T.3    Konishi, Y.4
  • 17
    • 0032479445 scopus 로고    scopus 로고
    • Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A
    • Ono, Y., Shimada, H., Sorimachi, H., Richard, I. et al., Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J. Biol. Chem. 1998, 273, 17073-17078.
    • (1998) J. Biol. Chem , vol.273 , pp. 17073-17078
    • Ono, Y.1    Shimada, H.2    Sorimachi, H.3    Richard, I.4
  • 18
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard, I., Broux, O., Allamand, V., Fougerousse, F. et al., Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 1995, 81, 27-40.
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3    Fougerousse, F.4
  • 19
    • 33746129198 scopus 로고    scopus 로고
    • Calpain 3: A key regulator of the sarcomere?
    • Duguez, S., Bartoli, M., Richard, I., Calpain 3: a key regulator of the sarcomere? FEBS J. 2006, 273, 3427-3436.
    • (2006) FEBS J , vol.273 , pp. 3427-3436
    • Duguez, S.1    Bartoli, M.2    Richard, I.3
  • 20
    • 33846372980 scopus 로고    scopus 로고
    • Molecular and cellular basis of calpainopathy (limb girdle muscular dystrophy type 2A)
    • Kramerova, I., Beckmann, J. S., Spencer, M. J., Molecular and cellular basis of calpainopathy (limb girdle muscular dystrophy type 2A). Biochim. Biophys. Acta 2007, 1772, 128-144.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 128-144
    • Kramerova, I.1    Beckmann, J.S.2    Spencer, M.J.3
  • 21
    • 33751012118 scopus 로고    scopus 로고
    • Regulation of the M-cadherin-beta-catenin complex by calpain 3 during terminal stages of myogenic differentiation
    • Kramerova, I., Kudryashova, E., Wu, B., Spencer, M. J., Regulation of the M-cadherin-beta-catenin complex by calpain 3 during terminal stages of myogenic differentiation. Mol. Cell. Biol. 2006, 26, 8437-8447.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 8437-8447
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3    Spencer, M.J.4
  • 22
    • 0346366816 scopus 로고    scopus 로고
    • Newly identified exons encoding novel variants of p94/calpain 3 are expressed ubiquitously and overlap the alpha-glucosidase C gene
    • Kawabata, Y., Hata, S., Ono, Y., Ito, Y. et al., Newly identified exons encoding novel variants of p94/calpain 3 are expressed ubiquitously and overlap the alpha-glucosidase C gene. FEBS Lett. 2003, 555, 623-630.
    • (2003) FEBS Lett , vol.555 , pp. 623-630
    • Kawabata, Y.1    Hata, S.2    Ono, Y.3    Ito, Y.4
  • 23
    • 0242721312 scopus 로고    scopus 로고
    • Characterization of a new p94-like calpain form in human lymphocytes
    • De Tullio, R., Stifanese, R., Salamino, F., Pontremoli, S. et al., Characterization of a new p94-like calpain form in human lymphocytes. Biochem. J. 2003, 375, 689-696.
    • (2003) Biochem. J , vol.375 , pp. 689-696
    • De Tullio, R.1    Stifanese, R.2    Salamino, F.3    Pontremoli, S.4
  • 24
    • 0346556240 scopus 로고    scopus 로고
    • Calpain 3 is expressed in astrocytes of rat and Microcebus brain
    • Konig, N., Raynaud, F., Feane, H., Durand, M. et al., Calpain 3 is expressed in astrocytes of rat and Microcebus brain. J. Chem. Neuroanat. 2003, 25, 129-136.
    • (2003) J. Chem. Neuroanat , vol.25 , pp. 129-136
    • Konig, N.1    Raynaud, F.2    Feane, H.3    Durand, M.4
  • 25
    • 18144445733 scopus 로고    scopus 로고
    • Purification of native p94, a muscle-specific calpain, and characterization of its autolysis
    • Kinbara, K., Ishiura, S., Tomioka, S., Sorimachi, H. et al.. Purification of native p94, a muscle-specific calpain, and characterization of its autolysis. Biochem. J. 1998, 335, 589-596.
    • (1998) Biochem. J , vol.335 , pp. 589-596
    • Kinbara, K.1    Ishiura, S.2    Tomioka, S.3    Sorimachi, H.4
  • 26
    • 0027276561 scopus 로고
    • Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle
    • Sorimachi, H., Toyama-Sorimachi, N., Saido, T. C., Kawasaki, H. et al., Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J. Biol. Chem. 1993, 268, 10593-10605.
    • (1993) J. Biol. Chem , vol.268 , pp. 10593-10605
    • Sorimachi, H.1    Toyama-Sorimachi, N.2    Saido, T.C.3    Kawasaki, H.4
  • 27
    • 33745817771 scopus 로고    scopus 로고
    • Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system
    • Ono, Y., Torii, F., Ojima, K., Doi, N. et al.. Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system. J. Biol. Chem. 2006, 281, 18519-18531.
    • (2006) J. Biol. Chem , vol.281 , pp. 18519-18531
    • Ono, Y.1    Torii, F.2    Ojima, K.3    Doi, N.4
  • 28
    • 1242326458 scopus 로고    scopus 로고
    • Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3
    • Ono, Y., Kakinuma, K., Torii, F., Irie, A. et al., Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3. J. Biol. Chem. 2004, 279, 2761-2771.
    • (2004) J. Biol. Chem , vol.279 , pp. 2761-2771
    • Ono, Y.1    Kakinuma, K.2    Torii, F.3    Irie, A.4
  • 29
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al.. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 30
    • 24944440037 scopus 로고    scopus 로고
    • Quantitative proteomic analysis using isobaric protein tags enables rapid comparison of changes in transcript and protein levels in transformed cells
    • Unwin, R. D., Pierce, A., Watson, R. B., Sternberg, D. W. et al., Quantitative proteomic analysis using isobaric protein tags enables rapid comparison of changes in transcript and protein levels in transformed cells. Mol. Cell. Proteomics 2005, 4, 924-935.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 924-935
    • Unwin, R.D.1    Pierce, A.2    Watson, R.B.3    Sternberg, D.W.4
  • 31
    • 29144469393 scopus 로고    scopus 로고
    • Comparative study of [Three] LC-MALDI workflows for the analysis of complex proteomic samples
    • Hattan, S. J., Marchese, J., Khainovski, N., Martin, S. et al., Comparative study of [Three] LC-MALDI workflows for the analysis of complex proteomic samples. J. Proteome Res. 2005, 4, 1931-1941.
    • (2005) J. Proteome Res , vol.4 , pp. 1931-1941
    • Hattan, S.J.1    Marchese, J.2    Khainovski, N.3    Martin, S.4
  • 32
    • 34247341829 scopus 로고    scopus 로고
    • Proteomic discovery of metalloproteinase substrates in the cellular context by iTRAQ0 labeling reveals a diverse MMP-2 substrate degradome
    • in press
    • Dean, R A., Overall, C. M., Proteomic discovery of metalloproteinase substrates in the cellular context by iTRAQ0 labeling reveals a diverse MMP-2 substrate degradome. Mol. Cell. Proteomics 2007, 6, in press.
    • (2007) Mol. Cell. Proteomics , vol.6
    • Dean, R.A.1    Overall, C.M.2
  • 33
    • 0027365768 scopus 로고
    • Spatial resolution of fodrin proteolysis in postischemic brain
    • Saido, T. C., Yokota, M., Nagao, S., Yamaura, I. et al., Spatial resolution of fodrin proteolysis in postischemic brain. J. Biol. Chem. 1993, 268, 25239-25243.
    • (1993) J. Biol. Chem , vol.268 , pp. 25239-25243
    • Saido, T.C.1    Yokota, M.2    Nagao, S.3    Yamaura, I.4
  • 34
    • 17444383113 scopus 로고    scopus 로고
    • Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry
    • DeSouza, L., Diehl, G., Rodrigues, M. J., Guo, J. et al., Search for cancer markers from endometrial tissues using differentially labeled tags iTRAQ and cICAT with multidimensional liquid chromatography and tandem mass spectrometry. J. Proteome Res. 2005, 4, 377-386.
    • (2005) J. Proteome Res , vol.4 , pp. 377-386
    • DeSouza, L.1    Diehl, G.2    Rodrigues, M.J.3    Guo, J.4
  • 35
    • 33744926266 scopus 로고    scopus 로고
    • Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells
    • Unwin, R. D., Smith, D. L., Blinco, D., Wilson, C. L. et al., Quantitative proteomics reveals posttranslational control as a regulatory factor in primary hematopoietic stem cells. Blood 2006, 107, 4687-4694.
    • (2006) Blood , vol.107 , pp. 4687-4694
    • Unwin, R.D.1    Smith, D.L.2    Blinco, D.3    Wilson, C.L.4
  • 36
    • 0030667730 scopus 로고    scopus 로고
    • Identification of endogenous substrates for Drosophila calpain from a salt-extracted fraction of Drosophila ovaries
    • Amano, S., Kawasaki, H., Ishiura, S., Kawashima, S. et al., Identification of endogenous substrates for Drosophila calpain from a salt-extracted fraction of Drosophila ovaries. J. Biochem. 1997, 122, 865-871.
    • (1997) J. Biochem , vol.122 , pp. 865-871
    • Amano, S.1    Kawasaki, H.2    Ishiura, S.3    Kawashima, S.4
  • 38
    • 0025184841 scopus 로고
    • Human endothelial actin-binding protein (ABP-280, nonmuscle nlamin): A molecular leaf spring
    • Gorlin, J. B., Yamin, R., Egan, S., Stewart, M. et al., Human endothelial actin-binding protein (ABP-280, nonmuscle nlamin): a molecular leaf spring. J. Cell Biol. 1990, 222, 1089-1105.
    • (1990) J. Cell Biol , vol.222 , pp. 1089-1105
    • Gorlin, J.B.1    Yamin, R.2    Egan, S.3    Stewart, M.4
  • 39
    • 0024583598 scopus 로고
    • Enhancement of calcium sensitivity of lipocortin I in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography
    • Ando, Y., Imamura, S., Hong, Y. M., Owada, M. K. et al., Enhancement of calcium sensitivity of lipocortin I in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography. J. Biol. Chem. 1989, 264, 6948-6955.
    • (1989) J. Biol. Chem , vol.264 , pp. 6948-6955
    • Ando, Y.1    Imamura, S.2    Hong, Y.M.3    Owada, M.K.4
  • 40
    • 0344629442 scopus 로고    scopus 로고
    • Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components
    • Taveau,M., Bourg, N., Sillon, G., Roudaut, C. et al., Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol. Cell. Biol. 2003, 23, 9127-9135.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 9127-9135
    • Taveau, M.1    Bourg, N.2    Sillon, G.3    Roudaut, C.4
  • 41
    • 33845230658 scopus 로고    scopus 로고
    • Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice
    • Cohen, N., Kudryashova, E., Kramerova, I., Anderson, L. V. et al., Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Proteomics 2006, 6, 6075-6084.
    • (2006) Proteomics , vol.6 , pp. 6075-6084
    • Cohen, N.1    Kudryashova, E.2    Kramerova, I.3    Anderson, L.V.4
  • 42
    • 33745618209 scopus 로고    scopus 로고
    • Biochemical background of the VO2 on-kinetics in skeletal muscles
    • Korzeniewski, B., Zoladz, J. A., Biochemical background of the VO2 on-kinetics in skeletal muscles. J. Physiol Sci. 2006, 56, 1-12.
    • (2006) J. Physiol Sci , vol.56 , pp. 1-12
    • Korzeniewski, B.1    Zoladz, J.A.2
  • 43
    • 27144493736 scopus 로고    scopus 로고
    • Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway
    • Hayashi, M., Fukuzawa, T., Sorimachi, H., Maeda, T., Constitutive activation of the pH-responsive Rim101 pathway in yeast mutants defective in late steps of the MVB/ESCRT pathway. Mol. Cell. Biol. 2005, 25, 9478-9490.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 9478-9490
    • Hayashi, M.1    Fukuzawa, T.2    Sorimachi, H.3    Maeda, T.4
  • 44
    • 9444284398 scopus 로고    scopus 로고
    • Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans
    • Xu, W., Smith, F. J., Jr., Subaran, R., MitcheE, A. P., Multivesicular body-ESCRT components function in pH response regulation in Saccharomyces cerevisiae and Candida albicans. Mol. Biol. Cell 2004, 15, 5528-5537.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5528-5537
    • Xu, W.1    Smith Jr., F.J.2    Subaran, R.3    MitcheE, A.P.4
  • 45
    • 26444610334 scopus 로고    scopus 로고
    • Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin-proteasome pathway
    • Kramerova, I., Kudryashova, E., Venkatiaman, G., Spencer, M. J., Calpain 3 participates in sarcomere remodeling by acting upstream of the ubiquitin-proteasome pathway. Hum. Mol. Genet. 2005, 14, 2125-2134.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 2125-2134
    • Kramerova, I.1    Kudryashova, E.2    Venkatiaman, G.3    Spencer, M.J.4
  • 46
    • 33846821908 scopus 로고    scopus 로고
    • Proteomic discovery of protease substrates
    • DOI:10.1016/ j.cbpa.2006.11.037
    • Schilling, O., Overall, C. M., Proteomic discovery of protease substrates. Curr. Opin. Chem. Biol. 2006, DOI:10.1016/ j.cbpa.2006.11.037.
    • (2006) Curr. Opin. Chem. Biol
    • Schilling, O.1    Overall, C.M.2
  • 47
    • 0024477632 scopus 로고
    • Proteolysis of N-ethyl-maleimide-modified aldolase loaded into erythrocyte ghosts: Prevention by inhibitors of calpain
    • Hopgood, M. F., Knowles, S. E., Ballard, F. J., Proteolysis of N-ethyl-maleimide-modified aldolase loaded into erythrocyte ghosts: prevention by inhibitors of calpain. Biochem. J. 1989, 259, 237-242.
    • (1989) Biochem. J , vol.259 , pp. 237-242
    • Hopgood, M.F.1    Knowles, S.E.2    Ballard, F.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.