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Volumn 434, Issue 2, 2011, Pages 181-188

Beyond the endoplasmic reticulum: Atypical GRP78 in cell viability, signalling and therapeutic targeting

Author keywords

Cell surface; Cytosol; Endoplasmic reticulum; Glucose regulated protein of 78 kDA (GRP78); Mitochondrion; Nucleus

Indexed keywords

GLUCOSE REGULATED PROTEIN 78; OLIGOPEPTIDE; PACLITAXEL; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN PEP42; UNCLASSIFIED DRUG;

EID: 79951537603     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101569     Document Type: Review
Times cited : (427)

References (69)
  • 1
    • 0023890443 scopus 로고
    • Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: Structure, conservation, and regulation
    • Ting, J. and Lee, A. S. (1988) Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7, 275-286
    • (1988) DNA , vol.7 , pp. 275-286
    • Ting, J.1    Lee, A.S.2
  • 2
    • 0035423875 scopus 로고    scopus 로고
    • The glucose-regulated proteins: Stress induction and clinical applications
    • Lee, A. S. (2001) The glucose-regulated proteins: stress induction and clinical applications. Trends Biochem. Sci. 26, 504-510
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 504-510
    • Lee, A.S.1
  • 3
    • 34248571826 scopus 로고    scopus 로고
    • GRP78 induction in cancer: Therapeutic and prognostic implications
    • Lee, A. S. (2007) GRP78 induction in cancer: therapeutic and prognostic implications. Cancer Res. 67, 3496-3499
    • (2007) Cancer Res. , vol.67 , pp. 3496-3499
    • Lee, A.S.1
  • 4
    • 77952061607 scopus 로고    scopus 로고
    • Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP
    • Zhang, Y., Liu, R., Ni, M., Gill, P. and Lee, A. S. (2010) Cell surface relocalization of the endoplasmic reticulum chaperone and unfolded protein response regulator GRP78/BiP. J. Biol. Chem. 285, 15065-15075
    • (2010) J. Biol. Chem. , vol.285 , pp. 15065-15075
    • Zhang, Y.1    Liu, R.2    Ni, M.3    Gill, P.4    Lee, A.S.5
  • 6
    • 68949202516 scopus 로고    scopus 로고
    • Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders
    • Wang, M., Wey, S., Zhang, Y., Ye, R. and Lee, A. S. (2009) Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders. Antioxid. Redox. Signaling 11, 2307-2316
    • (2009) Antioxid. Redox. Signaling , vol.11 , pp. 2307-2316
    • Wang, M.1    Wey, S.2    Zhang, Y.3    Ye, R.4    Lee, A.S.5
  • 7
    • 69949170481 scopus 로고    scopus 로고
    • Regulation of PERK signaling and leukemic cell survival by a novel cytosolic isoform of the UPR regulator GRP78/BiP
    • Ni, M., Zhou, H., Wey, S., Baumeister, P. and Lee, A. S. (2009) Regulation of PERK signaling and leukemic cell survival by a novel cytosolic isoform of the UPR regulator GRP78/BiP. PLoS ONE 4, e6868
    • (2009) PLoS ONE , vol.4
    • Ni, M.1    Zhou, H.2    Wey, S.3    Baumeister, P.4    Lee, A.S.5
  • 8
    • 33646762480 scopus 로고    scopus 로고
    • Localization of GRP78 to mitochondria under the unfolded protein response
    • Sun, F. C., Wei, S., Li, C. W., Chang, Y. S., Chao, C. C. and Lai, Y. K. (2006) Localization of GRP78 to mitochondria under the unfolded protein response. Biochem. J. 396, 31-39
    • (2006) Biochem. J. , vol.396 , pp. 31-39
    • Sun, F.C.1    Wei, S.2    Li, C.W.3    Chang, Y.S.4    Chao, C.C.5    Lai, Y.K.6
  • 9
    • 77449096697 scopus 로고    scopus 로고
    • Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance
    • Ye, R., Jung, D. Y., Jun, J. Y., Li, J., Luo, S., Ko, H. J., Kim, J. K. and Lee, A. S. (2010) Grp78 heterozygosity promotes adaptive unfolded protein response and attenuates diet-induced obesity and insulin resistance. Diabetes 59, 6-16
    • (2010) Diabetes , vol.59 , pp. 6-16
    • Ye, R.1    Jung, D.Y.2    Jun, J.Y.3    Li, J.4    Luo, S.5    Ko, H.J.6    Kim, J.K.7    Lee, A.S.8
  • 10
    • 0038080911 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: Role of ATP binding site in suppression of caspase-7 activation
    • Reddy, R. K., Mao, C., Baumeister, P., Austin, R. C., Kaufman, R. J. and Lee, A. S. (2003) Endoplasmic reticulum chaperone protein GRP78 protects cells from apoptosis induced by topoisomerase inhibitors: role of ATP binding site in suppression of caspase-7 activation. J. Biol. Chem. 278, 20915-20924
    • (2003) J. Biol. Chem. , vol.278 , pp. 20915-20924
    • Reddy, R.K.1    Mao, C.2    Baumeister, P.3    Austin, R.C.4    Kaufman, R.J.5    Lee, A.S.6
  • 11
    • 70449713654 scopus 로고    scopus 로고
    • GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib
    • Kern, J., Untergasser, G., Zenzmaier, C., Sarg, B., Gastl, G., Gunsilius, E. and Steurer, M. (2009) GRP-78 secreted by tumor cells blocks the antiangiogenic activity of bortezomib. Blood 114, 3960-3967
    • (2009) Blood , vol.114 , pp. 3960-3967
    • Kern, J.1    Untergasser, G.2    Zenzmaier, C.3    Sarg, B.4    Gastl, G.5    Gunsilius, E.6    Steurer, M.7
  • 12
    • 0030948765 scopus 로고    scopus 로고
    • A lymphocyte cell surface heat shock protein homologous to the endoplasmic reticulum chaperone, immunoglobulin heavy chain binding protein BIP
    • Berger, C. L., Dong, Z., Hanlon, D., Bisaccia, E. and Edelson, R. L. (1997) A lymphocyte cell surface heat shock protein homologous to the endoplasmic reticulum chaperone, immunoglobulin heavy chain binding protein BIP. Int. J. Cancer 71, 1077-1085
    • (1997) Int. J. Cancer , vol.71 , pp. 1077-1085
    • Berger, C.L.1    Dong, Z.2    Hanlon, D.3    Bisaccia, E.4    Edelson, R.L.5
  • 14
    • 0037470247 scopus 로고    scopus 로고
    • Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function
    • Shin, B. K., Wang, H., Yim, A. M., Le Naour, F., Brichory, F., Jang, J. H., Zhao, R., Puravs, E., Tra, J., Michael, C. W. et al. (2003) Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. J. Biol. Chem. 278, 7607-7616
    • (2003) J. Biol. Chem. , vol.278 , pp. 7607-7616
    • Shin, B.K.1    Wang, H.2    Yim, A.M.3    Le Naour, F.4    Brichory, F.5    Jang, J.H.6    Zhao, R.7    Puravs, E.8    Tra, J.9    Michael, C.W.10
  • 15
  • 16
    • 35148840552 scopus 로고    scopus 로고
    • Phage display-derived human monoclonal antibodies isolated by binding to the surface of live primary breast cancer cells recognize GRP78
    • DOI 10.1158/0008-5472.CAN-06-4686
    • Jakobsen, C. G., Rasmussen, N., Laenkholm, A. V. and Ditzel, H. J. (2007) Phage display derived human monoclonal antibodies isolated by binding to the surface of live primary breast cancer cells recognize GRP78. Cancer Res. 67, 9507-9517 (Pubitemid 47535941)
    • (2007) Cancer Research , vol.67 , Issue.19 , pp. 9507-9517
    • Jakobsen, C.G.1    Rasmussen, N.2    Laenkholm, A.-V.3    Ditzel, H.J.4
  • 18
    • 2442680458 scopus 로고    scopus 로고
    • 2M*-induced signalling
    • DOI 10.1016/j.cellsig.2004.01.003, PII S0898656804000142
    • Misra, U. K., Gonzalez-Gronow, M., Gawdi, G., Wang, F. and Pizzo, S. V. (2004) A novel receptor function for the heat shock protein Grp78: silencing of Grp78 gene expression attenuates α2M*-induced signalling. Cell. Signalling 16, 929-938 (Pubitemid 38659527)
    • (2004) Cellular Signalling , vol.16 , Issue.8 , pp. 929-938
    • Misra, U.K.1    Gonzalez-Gronow, M.2    Gawdi, G.3    Wang, F.4    Pizzo, S.V.5
  • 19
    • 22544456920 scopus 로고    scopus 로고
    • 2-macroglobulin to its cell surface receptor GRP78 in 1-LN prostate cancer cells regulates PAK-2-dependent activation of LIMK
    • 2-macroglobulin to its cell surface receptor GRP78 in 1-LN prostate cancer cells regulates PAK-2-dependent activation of LIMK. J. Biol. Chem. 280, 26278-26286
    • (2005) J. Biol. Chem. , vol.280 , pp. 26278-26286
    • Misra, U.K.1    Deedwania, R.2    Pizzo, S.V.3
  • 20
    • 33744962234 scopus 로고    scopus 로고
    • Activation and cross-talk between Akt, NF-κB, and unfolded protein response signaling in 1-LN prostate cancer cells consequent to ligation of cell surface-associated GRP78
    • Misra, U. K., Deedwania, R. and Pizzo, S. V. (2006) Activation and cross-talk between Akt, NF-κB, and unfolded protein response signaling in 1-LN prostate cancer cells consequent to ligation of cell surface-associated GRP78. J. Biol. Chem. 281, 13694-13707
    • (2006) J. Biol. Chem. , vol.281 , pp. 13694-13707
    • Misra, U.K.1    Deedwania, R.2    Pizzo, S.V.3
  • 21
    • 33845780561 scopus 로고    scopus 로고
    • Prostate cancer cell proliferation in vitro is modulated by antibodies against glucose-regulated protein 78 isolated from patient serum
    • Gonzalez-Gronow, M., Cuchacovich, M., Llanos, C., Urzua, C., Gawdi, G. and Pizzo, S. V. (2006) Prostate cancer cell proliferation in vitro is modulated by antibodies against glucose-regulated protein 78 isolated from patient serum. Cancer Res. 66, 11424-11431
    • (2006) Cancer Res. , vol.66 , pp. 11424-11431
    • Gonzalez-Gronow, M.1    Cuchacovich, M.2    Llanos, C.3    Urzua, C.4    Gawdi, G.5    Pizzo, S.V.6
  • 22
    • 77956500946 scopus 로고    scopus 로고
    • Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores
    • Al-Hashimi, A. A., Caldwell, J., Gonzalez-Gronow, M., Pizzo, S. V., Aboumrad, D., Pozza, L., Al-Bayati, H., Weitz, J. I., Stafford, A., Chan, H. et al. (2010) Binding of anti-GRP78 autoantibodies to cell surface GRP78 increases tissue factor procoagulant activity via the release of calcium from endoplasmic reticulum stores. J. Biol. Chem. 285, 28912-28923
    • (2010) J. Biol. Chem. , vol.285 , pp. 28912-28923
    • Al-Hashimi, A.A.1    Caldwell, J.2    Gonzalez-Gronow, M.3    Pizzo, S.V.4    Aboumrad, D.5    Pozza, L.6    Al-Bayati, H.7    Weitz, J.I.8    Stafford, A.9    Chan, H.10
  • 23
    • 37849035474 scopus 로고    scopus 로고
    • GRP78 and Cripto form a complex at the cell surface and collaborate to inhibit transforming growth factor β signaling and enhance cell growth
    • Shani, G., Fischer, W. H., Justice, N. J., Kelber, J. A., Vale, W. and Gray, P. C. (2008) GRP78 and Cripto form a complex at the cell surface and collaborate to inhibit transforming growth factor β signaling and enhance cell growth. Mol. Cell. Biol. 28, 666-677
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 666-677
    • Shani, G.1    Fischer, W.H.2    Justice, N.J.3    Kelber, J.A.4    Vale, W.5    Gray, P.C.6
  • 24
    • 67649256065 scopus 로고    scopus 로고
    • Blockade of Cripto binding to cell surface GRP78 inhibits oncogenic Cripto signaling via MAPK/PI3K and Smad2/3 pathways
    • Kelber, J. A., Panopoulos, A. D., Shani, G., Booker, E. C., Belmonte, J. C., Vale, W. W. and Gray, P. C. (2009) Blockade of Cripto binding to cell surface GRP78 inhibits oncogenic Cripto signaling via MAPK/PI3K and Smad2/3 pathways. Oncogene 28, 2324-2336
    • (2009) Oncogene , vol.28 , pp. 2324-2336
    • Kelber, J.A.1    Panopoulos, A.D.2    Shani, G.3    Booker, E.C.4    Belmonte, J.C.5    Vale, W.W.6    Gray, P.C.7
  • 26
    • 4544255170 scopus 로고    scopus 로고
    • Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands
    • DOI 10.1016/j.ccr.2004.08.018, PII S1535610804002405
    • Arap, M. A., Lahdenranta, J., Mintz, P. J., Hajitou, A., Sarkis, A. S., Arap, W. and Pasqualini, R. (2004) Cell surface expression of the stress response chaperone GRP78 enables tumor targeting by circulating ligands. Cancer Cell 6, 275-284 (Pubitemid 39222040)
    • (2004) Cancer Cell , vol.6 , Issue.3 , pp. 275-284
    • Arap, M.A.1    Lahdenranta, J.2    Mintz, P.J.3    Hajitou, A.4    Sarkis, A.S.5    Arap, W.6    Pasqualini, R.7
  • 28
    • 2542576198 scopus 로고    scopus 로고
    • Lipoptosis: Tumor-specific cell death by antibody-induced intracellular lipid accumulation
    • DOI 10.1158/0008-5472.CAN-03-3149
    • Pohle, T., Brandlein, S., Ruoff, N., Muller-Hermelink, H. K. and Vollmers, H. P. (2004) Lipoptosis: tumor-specific cell death by antibody-induced intracellular lipid accumulation. Cancer Res. 64, 3900-3906 (Pubitemid 38697302)
    • (2004) Cancer Research , vol.64 , Issue.11 , pp. 3900-3906
    • Pohle, T.1    Brandlein, S.2    Ruoff, N.3    Muller-Hermelink, H.K.4    Vollmers, H.P.5
  • 29
    • 66849083879 scopus 로고    scopus 로고
    • Ligation of cancer cell surface GRP78 with antibodies directed against its COOH-terminal domain up-regulates p53 activity and promotes apoptosis
    • Misra, U. K., Mowery, Y., Kaczowka, S. and Pizzo, S. V. (2009) Ligation of cancer cell surface GRP78 with antibodies directed against its COOH-terminal domain up-regulates p53 activity and promotes apoptosis. Mol. Cancer Ther. 8, 1350-1362
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 1350-1362
    • Misra, U.K.1    Mowery, Y.2    Kaczowka, S.3    Pizzo, S.V.4
  • 30
    • 77949273353 scopus 로고    scopus 로고
    • Modulation of the unfolded protein response in prostate cancer cells by antibody-directed against the carboxyl-terminal domain of GRP78
    • Misra, U. K. and Pizzo, S. V. (2010) Modulation of the unfolded protein response in prostate cancer cells by antibody-directed against the carboxyl-terminal domain of GRP78. Apoptosis 15, 173-182
    • (2010) Apoptosis , vol.15 , pp. 173-182
    • Misra, U.K.1    Pizzo, S.V.2
  • 31
    • 76749104619 scopus 로고    scopus 로고
    • Inhibition of NF-κB1 and NF-κB2 activation in prostate cancer cells treated with antibody against the carboxyl terminal domain of GRP78: Effect of p53 upregulation
    • Misra, U. K., Kaczowka, S. and Pizzo, S. V. (2010) Inhibition of NF-κB1 and NF-κB2 activation in prostate cancer cells treated with antibody against the carboxyl terminal domain of GRP78: Effect of p53 upregulation. Biochem. Biophys. Res. Commun. 392, 538-542
    • (2010) Biochem. Biophys. Res. Commun. , vol.392 , pp. 538-542
    • Misra, U.K.1    Kaczowka, S.2    Pizzo, S.V.3
  • 32
    • 85046915739 scopus 로고    scopus 로고
    • Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while promoting caspase activation in human prostate cancer cells
    • Misra, U. K. and Pizzo, A. V. (2010) Ligation of cell surface GRP78 with antibody directed against the COOH-terminal domain of GRP78 suppresses Ras/MAPK and PI 3-kinase/AKT signaling while promoting caspase activation in human prostate cancer cells. Cancer Biol. Ther. 9, 1-11
    • (2010) Cancer Biol. Ther. , vol.9 , pp. 1-11
    • Misra, U.K.1    Pizzo, A.V.2
  • 33
    • 67650632688 scopus 로고    scopus 로고
    • The tumor suppressor Par-4 activates an extrinsic pathway for apoptosis
    • Burikhanov, R., Zhao, Y., Goswami, A., Qiu, S., Schwarze, S. R. and Rangnekar, V. M. (2009) The tumor suppressor Par-4 activates an extrinsic pathway for apoptosis. Cell 138, 377-388
    • (2009) Cell , vol.138 , pp. 377-388
    • Burikhanov, R.1    Zhao, Y.2    Goswami, A.3    Qiu, S.4    Schwarze, S.R.5    Rangnekar, V.M.6
  • 34
    • 77954533130 scopus 로고    scopus 로고
    • Cancer-selective apoptotic effects of extracellular and intracellular Par-4
    • Shrestha-Bhattarai, T. and Rangnekar, V. M. (2010) Cancer-selective apoptotic effects of extracellular and intracellular Par-4. Oncogene 29, 3873-3880
    • (2010) Oncogene , vol.29 , pp. 3873-3880
    • Shrestha-Bhattarai, T.1    Rangnekar, V.M.2
  • 35
    • 75749123054 scopus 로고    scopus 로고
    • Targeting plasma membrane GRP78 for cancer growth inhibition
    • Schwarze, S. and Rangnekar, V. M. (2010) Targeting plasma membrane GRP78 for cancer growth inhibition. Cancer Biol. Ther. 9, 153-155
    • (2010) Cancer Biol. Ther. , vol.9 , pp. 153-155
    • Schwarze, S.1    Rangnekar, V.M.2
  • 36
    • 77952087611 scopus 로고    scopus 로고
    • The Par-4-GRP78 TRAIL, more twists and turns
    • Lee, A. S. (2009) The Par-4-GRP78 TRAIL, more twists and turns. Cancer Biol. Ther. 8, 2103-2105
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 2103-2105
    • Lee, A.S.1
  • 40
    • 0034900520 scopus 로고    scopus 로고
    • Major histocompatibility class one molecule associates with glucose regulated protein (GRP) 78 on the cell surface
    • Triantafilou, M., Fradelizi, D. and Triantafilou, K. (2001) Major histocompatibility class one molecule associates with glucose regulated protein (GRP) 78 on the cell surface. Hum. Immunol. 62, 764-770
    • (2001) Hum. Immunol. , vol.62 , pp. 764-770
    • Triantafilou, M.1    Fradelizi, D.2    Triantafilou, K.3
  • 41
    • 44949176516 scopus 로고    scopus 로고
    • Identification of proteins associating with glycosylphosphatidylinositol- anchored T-cadherin on the surface of vascular endothelial cells: Role for Grp78/BiP in T-cadherin-dependent cell survival
    • Philippova, M., Ivanov, D., Joshi, M. B., Kyriakakis, E., Rupp, K., Afonyushkin, T., Bochkov, V., Erne, P. and Resink, T. J. (2008) Identification of proteins associating with glycosylphosphatidylinositol-anchored T-cadherin on the surface of vascular endothelial cells: role for Grp78/BiP in T-cadherin-dependent cell survival. Mol. Cell. Biol. 28, 4004-4017
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4004-4017
    • Philippova, M.1    Ivanov, D.2    Joshi, M.B.3    Kyriakakis, E.4    Rupp, K.5    Afonyushkin, T.6    Bochkov, V.7    Erne, P.8    Resink, T.J.9
  • 42
    • 67650456845 scopus 로고    scopus 로고
    • Plasminogen Kringle 5 induces apoptosis of brain microvessel endothelial cells: Sensitization by radiation and requirement for GRP78 and LRP1
    • McFarland, B. C., Stewart, Jr, J., Hamza, A., Nordal, R., Davidson, D. J., Henkin, J. and Gladson, C. L. (2009) Plasminogen Kringle 5 induces apoptosis of brain microvessel endothelial cells: sensitization by radiation and requirement for GRP78 and LRP1. Cancer Res. 69, 5537-5545
    • (2009) Cancer Res. , vol.69 , pp. 5537-5545
    • McFarland, B.C.1    Stewart Jr., J.2    Hamza, A.3    Nordal, R.4    Davidson, D.J.5    Henkin, J.6    Gladson, C.L.7
  • 45
    • 38649085349 scopus 로고    scopus 로고
    • Therapeutic angiogenesis of mouse hind limb ischemia by novel peptide activating GRP78 receptor on endothelial cells
    • Hardy, B., Battler, A., Weiss, C., Kudasi, O. and Raiter, A. (2008) Therapeutic angiogenesis of mouse hind limb ischemia by novel peptide activating GRP78 receptor on endothelial cells. Biochem. Pharmacol. 75, 891-899
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 891-899
    • Hardy, B.1    Battler, A.2    Weiss, C.3    Kudasi, O.4    Raiter, A.5
  • 46
    • 76049112584 scopus 로고    scopus 로고
    • Activation of GRP78 on endothelial cell membranes by an ADAM15-derived peptide Induces angiogenesis
    • Raiter, A., Weiss, C., Bechor, Z., Ben-Dor, I., Battler, A., Kaplan, B. and Hardy, B. (2010) Activation of GRP78 on endothelial cell membranes by an ADAM15-derived peptide Induces angiogenesis. J. Vasc. Res. 47, 399-411
    • (2010) J. Vasc. Res. , vol.47 , pp. 399-411
    • Raiter, A.1    Weiss, C.2    Bechor, Z.3    Ben-Dor, I.4    Battler, A.5    Kaplan, B.6    Hardy, B.7
  • 47
    • 0036139925 scopus 로고    scopus 로고
    • GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization
    • DOI 10.1128/JVI.76.2.633-643.2002
    • Triantafilou, K., Fradelizi, D., Wilson, K. and Triantafilou, M. (2002) GRP78, a coreceptor for coxsackievirus A9, interacts with major histocompatibility complex class I molecules which mediate virus internalization. J. Virol. 76, 633-643 (Pubitemid 34033362)
    • (2002) Journal of Virology , vol.76 , Issue.2 , pp. 633-643
    • Triantafilou, K.1    Fradelizi, D.2    Wilson, K.3    Triantafilou, M.4
  • 48
    • 2442457815 scopus 로고    scopus 로고
    • Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2
    • Jindadamrongwech, S., Thepparit, C. and Smith, D. R. (2004) Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch. Virol. 149, 915-927
    • (2004) Arch. Virol. , vol.149 , pp. 915-927
    • Jindadamrongwech, S.1    Thepparit, C.2    Smith, D.R.3
  • 49
    • 70450206641 scopus 로고    scopus 로고
    • Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface
    • Honda, T., Horie, M., Daito, T., Ikuta, K. and Tomonaga, K. (2009) Molecular chaperone BiP interacts with Borna disease virus glycoprotein at the cell surface. J. Virol. 83, 12622-12625
    • (2009) J. Virol. , vol.83 , pp. 12622-12625
    • Honda, T.1    Horie, M.2    Daito, T.3    Ikuta, K.4    Tomonaga, K.5
  • 50
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S. and Pelham, H. R. (1987) A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 51
    • 0031558806 scopus 로고    scopus 로고
    • KDEL receptor expression is not coordinatedly up-regulated with ER stress-induced reticuloplasmin expression in HeLa cells
    • Llewellyn, D. H., Roderick, H. L. and Rose, S. (1997) KDEL receptor expression is not coordinatedly up-regulated with ER stress-induced reticuloplasmin expression in HeLa cells. Biochem. Biophys. Res. Commun. 240, 36-40
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 36-40
    • Llewellyn, D.H.1    Roderick, H.L.2    Rose, S.3
  • 53
    • 44349167189 scopus 로고    scopus 로고
    • Hypoxic inhibition of nonsense-mediated RNA decay regulates gene expression and the integrated stress response
    • Gardner, L. B. (2008) Hypoxic inhibition of nonsense-mediated RNA decay regulates gene expression and the integrated stress response. Mol. Cell. Biol. 28, 3729-3741
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3729-3741
    • Gardner, L.B.1
  • 55
    • 33746370728 scopus 로고    scopus 로고
    • The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins
    • Hegde, N. R., Chevalier, M. S., Wisner, T. W., Denton, M. C., Shire, K., Frappier, L. and Johnson, D. C. (2006) The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins. J. Biol. Chem. 281, 20910-20919
    • (2006) J. Biol. Chem. , vol.281 , pp. 20910-20919
    • Hegde, N.R.1    Chevalier, M.S.2    Wisner, T.W.3    Denton, M.C.4    Shire, K.5    Frappier, L.6    Johnson, D.C.7
  • 56
    • 37349040367 scopus 로고    scopus 로고
    • Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly
    • Buchkovich, N. J., Maguire, T. G., Yu, Y., Paton, A. W., Paton, J. C. and Alwine, J. C. (2008) Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly. J. Virol. 82, 31-39
    • (2008) J. Virol. , vol.82 , pp. 31-39
    • Buchkovich, N.J.1    Maguire, T.G.2    Yu, Y.3    Paton, A.W.4    Paton, J.C.5    Alwine, J.C.6
  • 57
    • 70350647319 scopus 로고    scopus 로고
    • The endoplasmic reticulum chaperone BiP/GRP78 is important in the structure and function of the human cytomegalovirus assembly compartment
    • Buchkovich, N. J., Maguire, T. G., Paton, A. W., Paton, J. C. and Alwine, J. C. (2009) The endoplasmic reticulum chaperone BiP/GRP78 is important in the structure and function of the human cytomegalovirus assembly compartment. J. Virol. 83, 11421-11428
    • (2009) J. Virol. , vol.83 , pp. 11421-11428
    • Buchkovich, N.J.1    Maguire, T.G.2    Paton, A.W.3    Paton, J.C.4    Alwine, J.C.5
  • 58
    • 21644471445 scopus 로고    scopus 로고
    • The involvement of copper transporter in lead-induced oxidative stress in astroglia
    • Qian, Y., Zheng, Y., Ramos, K. S. and Tiffany-Castiglioni, E. (2005) The involvement of copper transporter in lead-induced oxidative stress in astroglia. Neurochem. Res. 30, 429-438
    • (2005) Neurochem. Res. , vol.30 , pp. 429-438
    • Qian, Y.1    Zheng, Y.2    Ramos, K.S.3    Tiffany-Castiglioni, E.4
  • 60
    • 0035879050 scopus 로고    scopus 로고
    • Identification and characterization of molecular interactions between glucose-regulated proteins (GRPs) mortalin/GRP75/peptide-binding protein 74 (PBP74) and GRP94
    • Takano, S., Wadhwa, R., Mitsui, Y. and Kaul, S. C. (2001) Identification and characterization of molecular interactions between glucose-regulated proteins (GRPs) mortalin/GRP75/peptide-binding protein 74 (PBP74) and GRP94. Biochem. J. 357, 393-398
    • (2001) Biochem. J. , vol.357 , pp. 393-398
    • Takano, S.1    Wadhwa, R.2    Mitsui, Y.3    Kaul, S.C.4
  • 61
    • 79251600505 scopus 로고    scopus 로고
    • 2+ handling and function of mitochondria in astrocytes after ischemia-like stress
    • doi:10.1016/j.mito.2010.10.007
    • 2+ handling and function of mitochondria in astrocytes after ischemia-like stress. Mitochondrion, doi:10.1016/j.mito.2010.10.007
    • (2010) Mitochondrion
    • Ouyang, Y.B.1    Xu, L.J.2    Emery, J.F.3    Lee, A.S.4    Giffard, R.G.5
  • 63
    • 0034660877 scopus 로고    scopus 로고
    • Histone H3 and heat shock protein GRP78 are selectively cross-linked to DNA by photoactivated gilvocarcin V in human fibroblasts
    • Matsumoto, A. and Hanawalt, P. C. (2000) Histone H3 and heat shock protein GRP78 are selectively cross-linked to DNA by photoactivated gilvocarcin V in human fibroblasts. Cancer Res. 60, 3921-3926
    • (2000) Cancer Res. , vol.60 , pp. 3921-3926
    • Matsumoto, A.1    Hanawalt, P.C.2
  • 64
    • 26644437215 scopus 로고    scopus 로고
    • Identification of mammalian proteins cross-linked to DNA by ionizing radiation
    • Barker, S., Weinfeld, M., Zheng, J., Li, L. and Murray, D. (2005) Identification of mammalian proteins cross-linked to DNA by ionizing radiation. J. Biol. Chem. 280, 33826-33838
    • (2005) J. Biol. Chem. , vol.280 , pp. 33826-33838
    • Barker, S.1    Weinfeld, M.2    Zheng, J.3    Li, L.4    Murray, D.5
  • 66
    • 16244400102 scopus 로고    scopus 로고
    • Decreased cell survival and DNA repair capacity after UVC irradiation in association with down-regulation of GRP78/BiP in human RSa cells
    • Zhai, L., Kita, K., Wano, C., Wu, Y., Sugaya, S. and Suzuki, N. (2005) Decreased cell survival and DNA repair capacity after UVC irradiation in association with down-regulation of GRP78/BiP in human RSa cells. Exp. Cell Res. 305, 244-252
    • (2005) Exp. Cell Res. , vol.305 , pp. 244-252
    • Zhai, L.1    Kita, K.2    Wano, C.3    Wu, Y.4    Sugaya, S.5    Suzuki, N.6
  • 67
    • 0026689538 scopus 로고
    • Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase
    • Takemoto, H., Yoshimori, T., Yamamoto, A., Miyata, Y., Yahara, I., Inoue, K. and Tashiro, Y. (1992) Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase. Arch. Biochem. Biophys. 296, 129-136
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 129-136
    • Takemoto, H.1    Yoshimori, T.2    Yamamoto, A.3    Miyata, Y.4    Yahara, I.5    Inoue, K.6    Tashiro, Y.7


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