메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

Nuclear Legumain Activity in Colorectal Cancer

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN L; HISTONE H3; LEGUMAIN;

EID: 84872241498     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0052980     Document Type: Article
Times cited : (71)

References (58)
  • 2
    • 0027191298 scopus 로고
    • The Two Cysteine Endopeptidases of Legume Seeds: Purification and Characterization by Use of Specific Fluorometric Assays
    • Kembhavi AA, Buttle DJ, Knight CG, Barrett AJ, (1993) The Two Cysteine Endopeptidases of Legume Seeds: Purification and Characterization by Use of Specific Fluorometric Assays. Arch Biochem Biophys 303: 208-213.
    • (1993) Arch Biochem Biophys , vol.303 , pp. 208-213
    • Kembhavi, A.A.1    Buttle, D.J.2    Knight, C.G.3    Barrett, A.J.4
  • 3
    • 0027688051 scopus 로고
    • Molecular Characterization of a Vacuolar Processing Enzyme Related to a Putative Cysteine Proteinase of Schistosoma mansoni
    • Hara-Nishimura I, Takeuchi Y, Nishimura M, (1993) Molecular Characterization of a Vacuolar Processing Enzyme Related to a Putative Cysteine Proteinase of Schistosoma mansoni. Plant Cell 5: 1651-1659.
    • (1993) Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 4
    • 0030992979 scopus 로고    scopus 로고
    • Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase
    • Chen JM, Dando PM, Rawlings ND, Brown MA, Young NE, et al. (1997) Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase. J Biol Chem 272: 8090-8098.
    • (1997) J Biol Chem , vol.272 , pp. 8090-8098
    • Chen, J.M.1    Dando, P.M.2    Rawlings, N.D.3    Brown, M.A.4    Young, N.E.5
  • 5
    • 84855998523 scopus 로고    scopus 로고
    • Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile
    • Dall E, Brandstetter H, (2012) Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile. Acta Crystallogr F 68: 24-31.
    • (2012) Acta Crystallogr F , vol.68 , pp. 24-31
    • Dall, E.1    Brandstetter, H.2
  • 6
    • 0141755165 scopus 로고    scopus 로고
    • Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo
    • Li DN, Matthews SP, Antoniou AN, Mazzeo D, Watts C, (2003) Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo. J Biol Chem 278: 38980-38990.
    • (2003) J Biol Chem , vol.278 , pp. 38980-38990
    • Li, D.N.1    Matthews, S.P.2    Antoniou, A.N.3    Mazzeo, D.4    Watts, C.5
  • 7
    • 0036929283 scopus 로고    scopus 로고
    • Processing and activation of lysosomal proteinases
    • Ishidoh K, Kominami E, (2002) Processing and activation of lysosomal proteinases. Biol Chem 383: 1827-1831.
    • (2002) Biol Chem , vol.383 , pp. 1827-1831
    • Ishidoh, K.1    Kominami, E.2
  • 8
    • 33744915019 scopus 로고    scopus 로고
    • Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification
    • Cheng T, Hitomi K, van Vlijmen-Willems IM, de Jongh GJ, Yamamoto K, et al. (2006) Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification. J Biol Chem 281: 15893-15899.
    • (2006) J Biol Chem , vol.281 , pp. 15893-15899
    • Cheng, T.1    Hitomi, K.2    van Vlijmen-Willems, I.M.3    de Jongh, G.J.4    Yamamoto, K.5
  • 9
    • 0033516575 scopus 로고    scopus 로고
    • Inhibition of Mammalian Legumain by Some Cystatins Is Due to a Novel Second Reactive Site
    • Alvarez-Fernandez M, Barrett AJ, Gerhartz B, Dando PM, Ni J, et al. (1999) Inhibition of Mammalian Legumain by Some Cystatins Is Due to a Novel Second Reactive Site. J Biol Chem 274: 19195-19203.
    • (1999) J Biol Chem , vol.274 , pp. 19195-19203
    • Alvarez-Fernandez, M.1    Barrett, A.J.2    Gerhartz, B.3    Dando, P.M.4    Ni, J.5
  • 10
    • 0038243036 scopus 로고    scopus 로고
    • Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy
    • Liu C, Sun C, Huang H, Janda K, Edgington T, (2003) Overexpression of legumain in tumors is significant for invasion/metastasis and a candidate enzymatic target for prodrug therapy. Cancer Res 63: 2957-2964.
    • (2003) Cancer Res , vol.63 , pp. 2957-2964
    • Liu, C.1    Sun, C.2    Huang, H.3    Janda, K.4    Edgington, T.5
  • 11
    • 16844367758 scopus 로고    scopus 로고
    • Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer
    • Murthy RV, Arbman G, Gao J, Roodman GD, Sun XF, (2005) Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer. Clin Cancer Res 11: 2293-2299.
    • (2005) Clin Cancer Res , vol.11 , pp. 2293-2299
    • Murthy, R.V.1    Arbman, G.2    Gao, J.3    Roodman, G.D.4    Sun, X.F.5
  • 13
    • 76949097013 scopus 로고    scopus 로고
    • Cystatin E/M suppresses legumain activity and invasion of human melanoma
    • Briggs J, Haugen M, Johansen H, Riker A, Abrahamson M, et al. (2010) Cystatin E/M suppresses legumain activity and invasion of human melanoma. BMC Cancer 10: 17.
    • (2010) BMC Cancer , vol.10 , pp. 17
    • Briggs, J.1    Haugen, M.2    Johansen, H.3    Riker, A.4    Abrahamson, M.5
  • 14
    • 0041876230 scopus 로고    scopus 로고
    • Biosynthetic Processing of Cathepsins and Lysosomal Degradation Are Abolished in Asparaginyl Endopeptidase-deficient Mice
    • Shirahama-Noda K, Yamamoto A, Sugihara K, Hashimoto N, Asano M, et al. (2003) Biosynthetic Processing of Cathepsins and Lysosomal Degradation Are Abolished in Asparaginyl Endopeptidase-deficient Mice. J Biol Chem 278: 33194-33199.
    • (2003) J Biol Chem , vol.278 , pp. 33194-33199
    • Shirahama-Noda, K.1    Yamamoto, A.2    Sugihara, K.3    Hashimoto, N.4    Asano, M.5
  • 15
    • 58849134849 scopus 로고    scopus 로고
    • Mice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome
    • Chan C-B, Abe M, Hashimoto N, Hao C, Williams IR, et al. (2009) Mice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome. Proc Natl Acad Sci U S A 106: 468-473.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 468-473
    • Chan, C.-B.1    Abe, M.2    Hashimoto, N.3    Hao, C.4    Williams, I.R.5
  • 16
    • 79955673020 scopus 로고    scopus 로고
    • Asparagine endopeptidase is required for normal kidney physiology and homeostasis
    • Miller G, Matthews SP, Reinheckel T, Fleming S, Watts C, (2011) Asparagine endopeptidase is required for normal kidney physiology and homeostasis. FASEB J 25: 1606-1617.
    • (2011) FASEB J , vol.25 , pp. 1606-1617
    • Miller, G.1    Matthews, S.P.2    Reinheckel, T.3    Fleming, S.4    Watts, C.5
  • 17
    • 84860419784 scopus 로고    scopus 로고
    • Nucleoplasmic calcium regulates cell proliferation through legumain
    • Andrade V, Guerra M, Jardim C, Melo F, Silva W, et al. (2011) Nucleoplasmic calcium regulates cell proliferation through legumain. J Hepatol 55: 626-635.
    • (2011) J Hepatol , vol.55 , pp. 626-635
    • Andrade, V.1    Guerra, M.2    Jardim, C.3    Melo, F.4    Silva, W.5
  • 18
    • 0034937132 scopus 로고    scopus 로고
    • Activation of progelatinase A by mammalian legumain, a recently discovered cysteine proteinase
    • Chen JM, Fortunato M, Stevens RA, Barrett AJ, (2001) Activation of progelatinase A by mammalian legumain, a recently discovered cysteine proteinase. Biol Chem 382: 777-783.
    • (2001) Biol Chem , vol.382 , pp. 777-783
    • Chen, J.M.1    Fortunato, M.2    Stevens, R.A.3    Barrett, A.J.4
  • 19
    • 84855427940 scopus 로고    scopus 로고
    • Targeting Cell Surface Alpha(v)beta(3) Integrin Increases Therapeutic Efficacies of a Legumain Protease-Activated Auristatin Prodrug
    • Liu Y, Bajjuri KM, Liu C, Sinha SC, (2011) Targeting Cell Surface Alpha(v)beta(3) Integrin Increases Therapeutic Efficacies of a Legumain Protease-Activated Auristatin Prodrug. Mol Pharmaceut 9: 168-175.
    • (2011) Mol Pharmaceut , vol.9 , pp. 168-175
    • Liu, Y.1    Bajjuri, K.M.2    Liu, C.3    Sinha, S.C.4
  • 20
    • 82255191976 scopus 로고    scopus 로고
    • Synthetic enzyme inhibitor: a novel targeting ligand for nanotherapeutic drug delivery inhibiting tumor growth without systemic toxicity
    • Liao D, Liu Z, Wrasidlo W, Chen T, Luo Y, et al. (2011) Synthetic enzyme inhibitor: a novel targeting ligand for nanotherapeutic drug delivery inhibiting tumor growth without systemic toxicity. Nanomed: Nanotechnol 7: 665-673.
    • (2011) Nanomed: Nanotechnol , vol.7 , pp. 665-673
    • Liao, D.1    Liu, Z.2    Wrasidlo, W.3    Chen, T.4    Luo, Y.5
  • 21
    • 80052391876 scopus 로고    scopus 로고
    • Autophagic activity measured in whole rat hepatocytes as the accumulation of a novel BHMT fragment (p10), generated in amphisomes by the asparaginyl proteinase, legumain
    • Øverbye A, Sætre F, Hagen LK, Johansen HT, Seglen PO, (2011) Autophagic activity measured in whole rat hepatocytes as the accumulation of a novel BHMT fragment (p10), generated in amphisomes by the asparaginyl proteinase, legumain. Autophagy 7: 1011-1027.
    • (2011) Autophagy , vol.7 , pp. 1011-1027
    • Øverbye, A.1    Sætre, F.2    Hagen, L.K.3    Johansen, H.T.4    Seglen, P.O.5
  • 22
    • 0032542285 scopus 로고    scopus 로고
    • An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation
    • Manoury B, Hewitt EW, Morrice N, Dando PM, Barrett AJ, et al. (1998) An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. Nature 396: 695-699.
    • (1998) Nature , vol.396 , pp. 695-699
    • Manoury, B.1    Hewitt, E.W.2    Morrice, N.3    Dando, P.M.4    Barrett, A.J.5
  • 23
    • 70449477746 scopus 로고    scopus 로고
    • Critical Role for Asparagine Endopeptidase in Endocytic Toll-like Receptor Signaling in Dendritic Cells
    • Sepulveda FE, Maschalidi S, Colisson R, Heslop L, Ghirelli C, et al. (2009) Critical Role for Asparagine Endopeptidase in Endocytic Toll-like Receptor Signaling in Dendritic Cells. Immunity 31: 737-748.
    • (2009) Immunity , vol.31 , pp. 737-748
    • Sepulveda, F.E.1    Maschalidi, S.2    Colisson, R.3    Heslop, L.4    Ghirelli, C.5
  • 24
    • 0017064628 scopus 로고
    • Human Colonic Adenocarcinoma Cells. I. Establishment and Description of a New Line
    • Tom BH, Rutzky LP, Jakstys MM, Oyasu R, Kaye CI, et al. (1976) Human Colonic Adenocarcinoma Cells. I. Establishment and Description of a New Line. In Vitro 12: 180-191.
    • (1976) In Vitro , vol.12 , pp. 180-191
    • Tom, B.H.1    Rutzky, L.P.2    Jakstys, M.M.3    Oyasu, R.4    Kaye, C.I.5
  • 25
    • 0027979552 scopus 로고
    • Differential expression of sucrase-isomaltase in clones isolated from early and late passages of the cell line Caco-2: evidence for glucose-dependent negative regulation
    • Chantret I, Rodolosse A, Barbat A, Dussaulx E, Brot-Laroche E, et al. (1994) Differential expression of sucrase-isomaltase in clones isolated from early and late passages of the cell line Caco-2: evidence for glucose-dependent negative regulation. Journal of Cell Science 107: 213-225.
    • (1994) Journal of Cell Science , vol.107 , pp. 213-225
    • Chantret, I.1    Rodolosse, A.2    Barbat, A.3    Dussaulx, E.4    Brot-Laroche, E.5
  • 26
    • 2942574538 scopus 로고    scopus 로고
    • Twelve colorectal cancer cell lines exhibit highly variable growth and metastatic capacities in an orthotopic model in nude mice
    • Flatmark K, Maelandsmo GM, Martinsen M, Rasmussen H, Fodstad O, (2004) Twelve colorectal cancer cell lines exhibit highly variable growth and metastatic capacities in an orthotopic model in nude mice. Eur J Cancer 40: 1593-1598.
    • (2004) Eur J Cancer , vol.40 , pp. 1593-1598
    • Flatmark, K.1    Maelandsmo, G.M.2    Martinsen, M.3    Rasmussen, H.4    Fodstad, O.5
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix K, Lemansky P, Herzog V, (1996) Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137: 1963-1974.
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 29
    • 0033543510 scopus 로고    scopus 로고
    • Colorimetric and fluorimetric microplate assays for legumain and a staining reaction for detection of the enzyme after electrophoresis
    • Johansen HT, Knight CG, Barrett AJ, (1999) Colorimetric and fluorimetric microplate assays for legumain and a staining reaction for detection of the enzyme after electrophoresis. Anal Biochem 273: 278-283.
    • (1999) Anal Biochem , vol.273 , pp. 278-283
    • Johansen, H.T.1    Knight, C.G.2    Barrett, A.J.3
  • 32
    • 2542579391 scopus 로고    scopus 로고
    • Evidence that unrestricted legumain activity is involved in disturbed epidermal cornification in cystatin M/E deficient mice
    • Zeeuwen PL, van Vlijmen-Willems IM, Olthuis D, Johansen HT, Hitomi K, et al. (2004) Evidence that unrestricted legumain activity is involved in disturbed epidermal cornification in cystatin M/E deficient mice. Hum Mol Genet 13: 1069-1079.
    • (2004) Hum Mol Genet , vol.13 , pp. 1069-1079
    • Zeeuwen, P.L.1    van Vlijmen-Willems, I.M.2    Olthuis, D.3    Johansen, H.T.4    Hitomi, K.5
  • 33
    • 77957854397 scopus 로고    scopus 로고
    • The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea
    • fj.10-155879
    • Zeeuwen PLJM, van Vlijmen-Willems IMJJ, Cheng T, Rodijk-Olthuis D, Hitomi K, et al. (2010) The cystatin M/E-cathepsin L balance is essential for tissue homeostasis in epidermis, hair follicles, and cornea. FASEB J pp. fj.10-155879.
    • (2010) FASEB J
    • Zeeuwen, P.L.J.M.1    van Vlijmen-Willems, I.M.J.J.2    Cheng, T.3    Rodijk-Olthuis, D.4    Hitomi, K.5
  • 34
    • 0043025195 scopus 로고    scopus 로고
    • Nuclear localization of the metastasis-related protein S100A4 correlates with tumour stage in colorectal cancer
    • Flatmark K, Pedersen KB, Nesland JM, Rasmussen H, Aamodt G, et al. (2003) Nuclear localization of the metastasis-related protein S100A4 correlates with tumour stage in colorectal cancer. J Pathol 200: 589-595.
    • (2003) J Pathol , vol.200 , pp. 589-595
    • Flatmark, K.1    Pedersen, K.B.2    Nesland, J.M.3    Rasmussen, H.4    Aamodt, G.5
  • 35
    • 0036538799 scopus 로고    scopus 로고
    • Legumain from bovine kidney: its purification, molecular cloning, immunohistochemical localization and degradation of annexin II and vitamin D-binding protein
    • Yamane T, Takeuchi K, Yamamoto Y, Li YH, Fujiwara M, et al. (2002) Legumain from bovine kidney: its purification, molecular cloning, immunohistochemical localization and degradation of annexin II and vitamin D-binding protein. Biochim Biophys Acta 1596: 108-120.
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 108-120
    • Yamane, T.1    Takeuchi, K.2    Yamamoto, Y.3    Li, Y.H.4    Fujiwara, M.5
  • 36
    • 0034528474 scopus 로고    scopus 로고
    • Activation of human prolegumain by cleavage at a C-terminal asparagine residue
    • Chen JM, Fortunato M, Barrett AJ, (2000) Activation of human prolegumain by cleavage at a C-terminal asparagine residue. Biochem J 352 Pt 2: 327-334.
    • (2000) Biochem J , vol.352 , Issue.Pt 2 , pp. 327-334
    • Chen, J.M.1    Fortunato, M.2    Barrett, A.J.3
  • 37
    • 66149088069 scopus 로고    scopus 로고
    • Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer
    • Sullivan S, Tosetto M, Kevans D, Coss A, Wang L, et al. (2009) Localization of nuclear cathepsin L and its association with disease progression and poor outcome in colorectal cancer. Int J Cancer 125: 54-61.
    • (2009) Int J Cancer , vol.125 , pp. 54-61
    • Sullivan, S.1    Tosetto, M.2    Kevans, D.3    Coss, A.4    Wang, L.5
  • 38
    • 53549094681 scopus 로고    scopus 로고
    • Cathepsin L Proteolytically Processes Histone H3 During Mouse Embryonic Stem Cell Differentiation
    • Duncan EM, Muratore-Schroeder TL, Cook RG, Garcia BA, Shabanowitz J, et al. (2008) Cathepsin L Proteolytically Processes Histone H3 During Mouse Embryonic Stem Cell Differentiation. Cell 135: 284-294.
    • (2008) Cell , vol.135 , pp. 284-294
    • Duncan, E.M.1    Muratore-Schroeder, T.L.2    Cook, R.G.3    Garcia, B.A.4    Shabanowitz, J.5
  • 39
    • 10044296973 scopus 로고    scopus 로고
    • Cysteine cathepsins in human cancer
    • Jedeszko C, Sloane BF, (2005) Cysteine cathepsins in human cancer. Biol Chem 385: 1017-1027.
    • (2005) Biol Chem , vol.385 , pp. 1017-1027
    • Jedeszko, C.1    Sloane, B.F.2
  • 40
    • 3242749959 scopus 로고    scopus 로고
    • Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages
    • Lecaille F, Muno D, Kominami E, Ishidoh K, (2005) Proteinases participating in the processing and activation of prolegumain in primary cultured rat macrophages. Biol Chem 385: 511-516.
    • (2005) Biol Chem , vol.385 , pp. 511-516
    • Lecaille, F.1    Muno, D.2    Kominami, E.3    Ishidoh, K.4
  • 41
    • 0030890648 scopus 로고    scopus 로고
    • Cystatin E is a Novel Human Cysteine Proteinase Inhibitor with Structural Resemblance to Family 2 Cystatins
    • Ni J, Abrahamson M, Zhang M, Fernandez MA, Grubb A, et al. (1997) Cystatin E is a Novel Human Cysteine Proteinase Inhibitor with Structural Resemblance to Family 2 Cystatins. J Biol Chem 272: 10853-10858.
    • (1997) J Biol Chem , vol.272 , pp. 10853-10858
    • Ni, J.1    Abrahamson, M.2    Zhang, M.3    Fernandez, M.A.4    Grubb, A.5
  • 42
    • 0031030180 scopus 로고    scopus 로고
    • Identification, Cloning, and Characterization of Cystatin M, a Novel Cysteine Proteinase Inhibitor, Down-regulated in Breast Cancer
    • Sotiropoulou G, Anisowicz A, Sager R, (1997) Identification, Cloning, and Characterization of Cystatin M, a Novel Cysteine Proteinase Inhibitor, Down-regulated in Breast Cancer. J Biol Chem 272: 903-910.
    • (1997) J Biol Chem , vol.272 , pp. 903-910
    • Sotiropoulou, G.1    Anisowicz, A.2    Sager, R.3
  • 43
    • 67349129706 scopus 로고    scopus 로고
    • The Biology of Cystatin M/E and its Cognate Target Proteases
    • Zeeuwen PL, Cheng T, Schalkwijk J, (2009) The Biology of Cystatin M/E and its Cognate Target Proteases. J Invest Dermatol 129: 1327-1338.
    • (2009) J Invest Dermatol , vol.129 , pp. 1327-1338
    • Zeeuwen, P.L.1    Cheng, T.2    Schalkwijk, J.3
  • 44
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: cellular roadmap to different functions
    • Brix K, Dunkhorst A, Mayer K, Jordans S, (2008) Cysteine cathepsins: cellular roadmap to different functions. Biochimie 90: 194-207.
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 45
    • 68849086963 scopus 로고    scopus 로고
    • A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug L-asparaginase
    • Patel N, Krishnan S, Offman MN, Krol M, Moss CX, et al. (2009) A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug L-asparaginase. J Clin Invest 119: 1964-1973.
    • (2009) J Clin Invest , vol.119 , pp. 1964-1973
    • Patel, N.1    Krishnan, S.2    Offman, M.N.3    Krol, M.4    Moss, C.X.5
  • 47
    • 67649845784 scopus 로고    scopus 로고
    • Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs
    • Kosugi S, Hasebe M, Tomita M, Yanagawa H, (2009) Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc Natl Acad Sci USA 106: 10171-10176.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10171-10176
    • Kosugi, S.1    Hasebe, M.2    Tomita, M.3    Yanagawa, H.4
  • 48
    • 71049188177 scopus 로고    scopus 로고
    • Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions
    • Jordans S, Jenko-Kokalj S, Kuhl N, Tedelind S, Sendt W, et al. (2009) Monitoring compartment-specific substrate cleavage by cathepsins B, K, L, and S at physiological pH and redox conditions. BMC Biochemistry 10: 23.
    • (2009) BMC Biochemistry , vol.10 , pp. 23
    • Jordans, S.1    Jenko-Kokalj, S.2    Kuhl, N.3    Tedelind, S.4    Sendt, W.5
  • 49
    • 76249090850 scopus 로고    scopus 로고
    • Blastocystis legumain is localized on the cell surface, and specific inhibition of its activity implicates a pro-survival role for the enzyme
    • Wu B, Yin J, Texier C, Roussel M, Tan KS, (2009) Blastocystis legumain is localized on the cell surface, and specific inhibition of its activity implicates a pro-survival role for the enzyme. J Biol Chem 285: 1790-1798.
    • (2009) J Biol Chem , vol.285 , pp. 1790-1798
    • Wu, B.1    Yin, J.2    Texier, C.3    Roussel, M.4    Tan, K.S.5
  • 50
    • 12544256390 scopus 로고    scopus 로고
    • Nuclear Translocation of Caspase-3 Is Dependent on Its Proteolytic Activation and Recognition of a Substrate-like Protein(s)
    • Kamada S, Kikkawa U, Tsujimoto Y, Hunter T, (2005) Nuclear Translocation of Caspase-3 Is Dependent on Its Proteolytic Activation and Recognition of a Substrate-like Protein(s). J Biol Chem 280: 857-860.
    • (2005) J Biol Chem , vol.280 , pp. 857-860
    • Kamada, S.1    Kikkawa, U.2    Tsujimoto, Y.3    Hunter, T.4
  • 51
    • 0033575347 scopus 로고    scopus 로고
    • Identification of a Vertebrate Sister-Chromatid Separation Inhibitor Involved in Transformation and Tumorigenesis
    • Zou H, McGarry TJ, Bernal T, Kirschner MW, (1999) Identification of a Vertebrate Sister-Chromatid Separation Inhibitor Involved in Transformation and Tumorigenesis. Science 285: 418-422.
    • (1999) Science , vol.285 , pp. 418-422
    • Zou, H.1    McGarry, T.J.2    Bernal, T.3    Kirschner, M.W.4
  • 52
    • 1942470581 scopus 로고    scopus 로고
    • A Cathepsin L Isoform that Is Devoid of a Signal Peptide Localizes to the Nucleus in S Phase and Processes the CDP/Cux Transcription Factor
    • Goulet B, Baruch A, Moon N-S, Poirier M, Sansregret LL, et al. (2004) A Cathepsin L Isoform that Is Devoid of a Signal Peptide Localizes to the Nucleus in S Phase and Processes the CDP/Cux Transcription Factor. Mol Cell 14: 207-219.
    • (2004) Mol Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.-S.3    Poirier, M.4    Sansregret, L.L.5
  • 53
    • 34548689404 scopus 로고    scopus 로고
    • Increased Expression and Activity of Nuclear Cathepsin L in Cancer Cells Suggests a Novel Mechanism of Cell Transformation
    • Goulet B, Sansregret L, Leduy L, Bogyo M, Weber E, et al. (2007) Increased Expression and Activity of Nuclear Cathepsin L in Cancer Cells Suggests a Novel Mechanism of Cell Transformation. Mol Cancer Res 5: 899-907.
    • (2007) Mol Cancer Res , vol.5 , pp. 899-907
    • Goulet, B.1    Sansregret, L.2    Leduy, L.3    Bogyo, M.4    Weber, E.5
  • 55
    • 84868196191 scopus 로고    scopus 로고
    • Intra- and extracellular regulation of activity and processing of legumain by cystatin E/M
    • Smith R, Johansen HT, Nilsen H, Haugen MH, Pettersen SJ, et al. (2012) Intra- and extracellular regulation of activity and processing of legumain by cystatin E/M. Biochimie 94 (12):: 2590-2599.
    • (2012) Biochimie , vol.94 , Issue.12 , pp. 2590-2599
    • Smith, R.1    Johansen, H.T.2    Nilsen, H.3    Haugen, M.H.4    Pettersen, S.J.5
  • 56
    • 21044432199 scopus 로고    scopus 로고
    • Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice
    • Maehr R, Hang HC, Mintern JD, Kim YM, Cuvillier A, et al. (2005) Asparagine endopeptidase is not essential for class II MHC antigen presentation but is required for processing of cathepsin L in mice. J Immunol 174: 7066-7074.
    • (2005) J Immunol , vol.174 , pp. 7066-7074
    • Maehr, R.1    Hang, H.C.2    Mintern, J.D.3    Kim, Y.M.4    Cuvillier, A.5
  • 57
    • 40849111819 scopus 로고    scopus 로고
    • Neuroprotective Actions of PIKE-L by Inhibition of SET Proteolytic Degradation by Asparagine Endopeptidase
    • Liu Z, Jang S-W, Liu X, Cheng D, Peng J, et al. (2008) Neuroprotective Actions of PIKE-L by Inhibition of SET Proteolytic Degradation by Asparagine Endopeptidase. Mol Cell 29: 665-678.
    • (2008) Mol Cell , vol.29 , pp. 665-678
    • Liu, Z.1    Jang, S.-W.2    Liu, X.3    Cheng, D.4    Peng, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.