C. Turano, S. Coppari, F. Altieri, and A. Ferraro, Proteins of the PDI family: Unpredicted non-ER locations and functions, Journal of Cellular Physiology, vol.273, issue.2, pp.154-163, 2002.
DOI : 10.1002/jcp.10172

R. C. Khanal and I. Nemere, The ERp57/GRp58/1,25D3-MARRS Receptor: Multiple Functional Roles in Diverse Cell Systems, Current Medicinal Chemistry, vol.14, issue.10, pp.1087-1093, 2007.
DOI : 10.2174/092986707780362871

H. Coe and M. Michalak, ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase, The International Journal of Biochemistry & Cell Biology, vol.42, issue.6, pp.796-799, 2010.
DOI : 10.1016/j.biocel.2010.01.009

C. F. Bennett, J. M. Balcarek, A. Varrichio, and S. T. Crooke, Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C, Nature, vol.334, issue.6179, pp.268-270, 1988.
DOI : 10.1038/334268a0

A. S. Lee, The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12, Journal of Cellular Physiology, vol.77, issue.1, pp.119-125, 1981.
DOI : 10.1002/jcp.1041060113

D. M. Ferrari and H. D. Söling, The protein disulphide-isomerase family: unravelling a string of folds, Biochemical Journal, vol.339, issue.1, pp.1-10, 1999.
DOI : 10.1042/bj3390001

L. Silvennoinen, J. Myllyharju, M. Ruoppolo, S. Orrù, M. Caterino et al., Identification and Characterization of Structural Domains of Human ERp57: ASSOCIATION WITH CALRETICULIN REQUIRES SEVERAL DOMAINS, Journal of Biological Chemistry, vol.279, issue.14, pp.279-13607, 2004.
DOI : 10.1074/jbc.M313054200

S. J. Russell, L. W. Ruddock, K. E. Salo, J. D. Oliver, Q. P. Roebuck et al., The Primary Substrate Binding Site in the b' Domain of ERp57 Is Adapted for Endoplasmic Reticulum Lectin Association, Journal of Biological Chemistry, vol.279, issue.18, pp.279-18861, 2004.
DOI : 10.1074/jbc.M400575200

G. Kozlov, P. Maattanen, J. D. Schrag, S. Pollock, M. Cygler et al., Crystal Structure of the bb??? Domains of the Protein Disulfide Isomerase ERp57, Structure, vol.14, issue.8, pp.1331-1339, 2006.
DOI : 10.1016/j.str.2006.06.019

P. Klappa, L. W. Ruddock, N. J. Darby, and R. B. Freedman, The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins, The EMBO Journal, vol.17, issue.4, pp.927-935, 1998.
DOI : 10.1093/emboj/17.4.927

E. Gaucci, S. Chichiarelli, C. Grillo, D. Vecchio, E. Eufemi et al., The Binding of Antibiotics to ERp57/GRP58, The Journal of Antibiotics, vol.72, issue.6, pp.61-400, 2008.
DOI : 10.1038/ja.2008.56

T. P. Dick, N. Bangia, D. R. Peaper, and P. Cresswell, Disulfide Bond Isomerization and the Assembly of MHC Class I-Peptide Complexes, Immunity, vol.16, issue.1, pp.87-98, 2002.
DOI : 10.1016/S1074-7613(02)00263-7

C. Grillo, C. D-'ambrosio, A. Scaloni, M. Maceroni, S. Merluzzi et al., Cooperative activity of Ref-1/APE and ERp57 in reductive activation of transcription factors, Free Radical Biology and Medicine, vol.41, issue.7, pp.41-1113, 2006.
DOI : 10.1016/j.freeradbiomed.2006.06.016

A. Donella-deana, P. James, W. Staudenmann, L. Cesaro, O. Marin et al., Isolation from Spleen of a 57-kDa Protein Substrate of the Tyrosine Kinase Lyn. Identification as a Protein Related to Protein Disulfide-Isomerase and Localisation of the Phosphorylation Sites, European Journal of Biochemistry, vol.221, issue.1-2, pp.18-25, 1996.
DOI : 10.1016/0092-8674(94)90334-4

K. Kita, N. Okumura, T. Takao, M. Watanabe, T. Matsubara et al., Evidence for phosphorylation of rat liver glucose-regulated protein 58, FEBS Lett, vol.60, issue.580, pp.199-205, 2006.

L. Zhou, B. A. Mckenzie, E. D. Eccleston, . Jr, S. P. Srivastava et al., C]Acetaminophen to Mouse Hepatic Microsomal Proteins:?? The Specific Binding to Calreticulin and the Two Forms of the Thiol:Protein Disulfide Oxidoreductases, Chemical Research in Toxicology, vol.9, issue.7, pp.1176-1182, 1996.
DOI : 10.1021/tx960069d

J. L. Martin, N. R. Pumford, A. C. Larosa, B. M. Martin, H. M. Gonzaga et al., A metabolite of halothane covalently binds to an endoplasmic reticulum protein that is highly homologous to phosphatidylinositol-specific phospholipase C-alpha but has no activity, Biochem. Biophys. Res. Commun, pp.178-679, 1991.

T. Laragione, E. Gianazza, R. Tonelli, P. Bigini, T. Mennini et al., Regulation of redox-sensitive exofacial protein thiols in CHO cells, Biological Chemistry, vol.387, issue.10/11, pp.387-1371, 2006.
DOI : 10.1515/BC.2006.172

D. Van-der-vlies, E. H. Pap, J. A. Post, J. E. Celis, and K. W. Wirtz, Endoplasmic reticulum resident proteins of normal human dermal fibroblasts are the major targets for oxidative stress induced by hydrogen peroxide, Biochem. J, pp.366-825, 2002.

C. Grillo, C. D-'ambrosio, V. Consalvi, R. Chiaraluce, A. Scaloni et al., DNA-binding Activity of the ERp57 C-terminal Domain Is Related to a Redox-dependent Conformational Change, Journal of Biological Chemistry, vol.282, issue.14, pp.282-10299, 2007.
DOI : 10.1074/jbc.M700966200

R. B. Freedman, T. R. Hirst, and M. F. Tuite, Protein disulphide isomerase: building bridges in protein folding, Trends in Biochemical Sciences, vol.19, issue.8, pp.331-336, 1994.
DOI : 10.1016/0968-0004(94)90072-8

H. Okudo, M. Kito, T. Moriyama, T. Ogawa, and R. Urade, Transglutaminase Activity of Human ER-60, Bioscience, Biotechnology, and Biochemistry, vol.64, issue.3, pp.66-1423, 2002.
DOI : 10.1074/jbc.273.16.9857

R. Urade, M. Nasu, T. Moriyama, K. Wada, and M. Kito, Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum, J. Biol. Chem, vol.267, pp.15152-15159, 1992.

M. S. Murthy and S. V. Pande, A stress-regulated protein, GRP58, a member of thioredoxin superfamily, is a carnitine palmitoyltransferase isoenzyme, Biochemical Journal, vol.304, issue.1, pp.31-34, 1994.
DOI : 10.1042/bj3040031

J. D. Oliver, F. J. Van-der-wal, N. J. Bulleid, and S. High, Interaction of the Thiol-Dependent Reductase ERp57 with Nascent Glycoproteins, Science, vol.275, issue.5296, pp.86-88, 1997.
DOI : 10.1126/science.275.5296.86

M. Molinari and A. Helenius, Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells, Nature, vol.402, pp.90-93, 1999.

J. D. Oliver, H. L. Roderick, D. H. Llewellyn, and S. High, ERp57 Functions as a Subunit of Specific Complexes Formed with the ER Lectins Calreticulin and Calnexin, Molecular Biology of the Cell, vol.10, issue.8, pp.2573-2582, 1999.
DOI : 10.1091/mbc.10.8.2573

C. E. Jessop, S. Chakravarthi, N. Garbi, G. J. Hämmerling, S. Lovell et al., ERp57 is essential for efficient folding of glycoproteins sharing common structural domains, The EMBO Journal, vol.273, issue.1, pp.28-40, 2007.
DOI : 10.1038/sj.emboj.7601505

J. A. Lindquist, O. N. Jensen, M. Mann, and G. J. Hämmerling, ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly, The EMBO Journal, vol.17, issue.8, pp.2186-2195, 1998.
DOI : 10.1093/emboj/17.8.2186

T. P. Dick, N. Bangia, D. R. Peaper, and P. Cresswell, Disulfide Bond Isomerization and the Assembly of MHC Class I-Peptide Complexes, Immunity, vol.16, issue.1, pp.87-98, 2002.
DOI : 10.1016/S1074-7613(02)00263-7

G. Dong, P. A. Wearsch, D. R. Peaper, P. Cresswell, and K. M. Reinisch, Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer, Immunity, vol.30, issue.1, pp.21-32, 2009.
DOI : 10.1016/j.immuni.2008.10.018

Y. Zhang, G. Kozlov, C. L. Pocanschi, U. Brockmeier, B. S. Ireland et al., ERp57 Does Not Require Interactions with Calnexin and Calreticulin to Promote Assembly of Class I Histocompatibility Molecules, and It Enhances Peptide Loading Independently of Its Redox Activity, Journal of Biological Chemistry, vol.284, issue.15, pp.10160-10173, 2009.
DOI : 10.1074/jbc.M808356200

D. R. Peaper and P. Cresswell, The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading, Proc. Natl. Acad. Sci. USA 105, pp.10477-10482, 2008.
DOI : 10.1073/pnas.0805044105

N. Garbi, S. Tanaka, F. Momburg, and G. J. Hammerling, Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57, Nature Immunology, vol.33, issue.1, pp.93-102, 2006.
DOI : 10.1038/ni1288

Y. Li and P. Camacho, -dependent redox modulation of SERCA 2b by ERp57, The Journal of Cell Biology, vol.7, issue.1, pp.35-46, 2004.
DOI : 10.1074/jbc.273.11.6009
URL : https://hal.archives-ouvertes.fr/tel-00807841

M. Schelhaas, J. Malmström, L. Pelkmans, J. Haugstetter, L. Ellgaard et al., Simian Virus 40 Depends on ER Protein Folding and Quality Control Factors for Entry into Host Cells, Cell, vol.131, issue.3, pp.516-529, 2007.
DOI : 10.1016/j.cell.2007.09.038

M. Desjardins, ER-mediated phagocytosis: a new membrane for new functions, Nature Reviews Immunology, vol.3, issue.4, pp.280-291, 2003.
DOI : 10.1038/nri1053

E. M. Frickel, R. Riek, I. Jelesarov, A. Helenius, K. Wuthrich et al., TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain, Proc. Natl. Acad. Sci. USA 99, pp.1954-1959, 2002.
DOI : 10.1073/pnas.042699099

N. Hirano, F. Shibasaki, R. Sakai, T. Tanaka, J. Nishida et al., Molecular cloning of the human glucoseregulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation, Eur. J. Biochem, pp.234-336, 1995.

S. Johnson, M. Michalak, M. Opas, and P. Eggleton, The ins and outs of calreticulin: from the ER lumen to the extracellular space, Trends in Cell Biology, vol.11, issue.3, pp.122-129, 2001.
DOI : 10.1016/S0962-8924(01)01926-2

N. Afshar, B. E. Black, and B. M. Paschal, Retrotranslocation of the Chaperone Calreticulin from the Endoplasmic Reticulum Lumen to the Cytosol, Molecular and Cellular Biology, vol.25, issue.20, pp.25-8844, 2005.
DOI : 10.1128/MCB.25.20.8844-8853.2005

D. A. Ellerman and D. G. Myles, A Role for Sperm Surface Protein Disulfide Isomerase Activity in Gamete Fusion: Evidence for the Participation of ERp57, Developmental Cell, vol.10, issue.6, pp.831-837, 2006.
DOI : 10.1016/j.devcel.2006.03.011

I. Nemere, M. C. Farach-carson, B. Rohe, T. M. Sterling, A. W. Norman et al., Ribozyme knockdown functionally links a 1,25(OH)2D3 membrane binding protein (1,25D3-MARRS) and phosphate uptake in intestinal cells, Proc. Natl. Acad. Sci. USA, pp.7392-7397, 2004.
DOI : 10.1073/pnas.0402207101

B. D. Boyan, K. L. Wong, M. Fang, and Z. Schwartz, 1??,25(OH)2D3 is an autocrine regulator of extracellular matrix turnover and growth factor release via ERp60 activated matrix vesicle metalloproteinases, The Journal of Steroid Biochemistry and Molecular Biology, vol.103, issue.3-5, pp.25-467, 2007.
DOI : 10.1016/j.jsbmb.2006.11.003

J. Chen, R. Olivares-navarrete, Y. Wang, T. R. Herman, B. D. Boyan et al., Protein-disulfide Isomerase-associated 3 (Pdia3) Mediates the Membrane Response to 1,25-Dihydroxyvitamin D3 in Osteoblasts, Journal of Biological Chemistry, vol.285, issue.47, pp.285-37041, 2010.
DOI : 10.1074/jbc.M110.157115

S. Tunsophon and I. Nemere, Protein kinase C isotypes in signal transduction for the 1,25D3-MARRS receptor (ERp57/PDIA3) in steroid hormone-stimulated phosphate uptake, Steroids, vol.75, issue.4-5, pp.307-313, 2010.
DOI : 10.1016/j.steroids.2010.01.004

I. Nemere, N. Garbi, G. J. Hämmerling, and R. C. Khanal, Intestinal Cell Calcium Uptake and the Targeted Knockout of the 1,25D3-MARRS (Membrane-associated, Rapid Response Steroid-binding) Receptor/PDIA3/Erp57, Journal of Biological Chemistry, vol.285, issue.41, pp.285-31859, 2010.
DOI : 10.1074/jbc.M110.116954

C. L. Richard, M. C. Farach-carson, B. Rohe, I. Nemere, and K. A. Meckling, Involvement of 1,25D3-MARRS (membrane associated, rapid response steroid-binding), a novel vitamin D receptor, in growth inhibition of breast cancer cells, Experimental Cell Research, vol.316, issue.5, pp.316-695, 2010.
DOI : 10.1016/j.yexcr.2009.12.015

W. Wu, G. Beilhartz, Y. Roy, C. L. Richard, M. Curtin et al., Nuclear translocation of the 1,25D3-MARRS (membrane associated rapid response to steroids) receptor protein and NFkappaB in differentiating NB4 leukemia cells, Exp. Cell Res, pp.316-1101, 2010.

S. J. Mah, A. M. Ades, R. Mir, I. R. Siemens, J. R. Williamson et al., Association of solubilized angiotensin II receptors with phospholipase C-alpha in murine neuroblastoma NIE-115 cells, Mol. Pharmacol, pp.42-217, 1992.

N. Aiyar, C. F. Bennett, P. Nambi, W. Valinski, M. Angioli et al., Solubilization of rat liver vasopressin receptors as a complex with a guanine-nucleotide-binding protein and phosphoinositidespecific phospholipase C, Biochem. J, pp.261-63, 1989.

F. Altieri, B. Maras, M. Eufemi, A. Ferraro, and C. Turano, Purification of a 57kDa nuclear matrix protein associated with thiol:protein-disulfide oxidoreductase and phospholipase C activities, Biochem. Biophys. Res. Commun, pp.194-992, 1993.

S. P. Srivastava, J. A. Fuchs, and J. L. Holtzman, The reported cDNA sequence for phospholipase C alpha encodes protein disulfide isomerase, isozyme Q-2 and not phospholipase-C, Biochem. Biophys. Res. Commun, pp.193-971, 1993.

Y. Tokutomi, N. Araki, K. Kataoka, E. Yamamoto, and S. Kim-mitsuyama, Oxidation of Prx2 and phosphorylation of GRP58 by angiotensin II in human coronary smooth muscle cells identified by 2D-DIGE analysis, Biochemical and Biophysical Research Communications, vol.364, issue.4, pp.364-822, 2007.
DOI : 10.1016/j.bbrc.2007.10.095

L. Zhu, N. C. Santos, and K. H. Kim, Disulfide isomerase glucose-regulated protein 58 is required for the nuclear localization and degradation of retinoic acid receptor ??, Reproduction, vol.139, issue.4, pp.717-731, 2010.
DOI : 10.1530/REP-09-0527

M. I. Ndubuisi, G. G. Guo, V. A. Fried, J. D. Etlinger, and P. B. Sehgal, Cellular Physiology of STAT3: Where's the Cytoplasmic Monomer?, Journal of Biological Chemistry, vol.274, issue.36, pp.274-25499, 1999.
DOI : 10.1074/jbc.274.36.25499

P. B. Sehgal, G. G. Guo, M. Shah, V. Kumar, and K. Patel, Cytokine Signaling, Journal of Biological Chemistry, vol.277, issue.14, pp.277-12067, 2002.
DOI : 10.1074/jbc.M200018200

G. G. Guo, K. Patel, V. Kumar, M. Shah, V. A. Fried et al., Association of the Chaperone Glucose-Regulated Protein 58 (GRP58/ER-60/ERp57) with Stat3 in Cytosol and Plasma Membrane Complexes, Journal of Interferon & Cytokine Research, vol.22, issue.5, pp.555-563, 2002.
DOI : 10.1089/10799900252982034

M. Eufemi, S. Coppari, F. Altieri, C. Grillo, A. Ferraro et al., ERp57 is present in STAT3???DNA complexes, Biochemical and Biophysical Research Communications, vol.323, issue.4, pp.323-1306, 2004.
DOI : 10.1016/j.bbrc.2004.09.009

S. Chichiarelli, E. Gaucci, A. Ferraro, C. Grillo, F. Altieri et al., Role of ERp57 in the signaling and transcriptional activity of STAT3 in a melanoma cell line, Archives of Biochemistry and Biophysics, vol.494, issue.2, pp.494-178, 2010.
DOI : 10.1016/j.abb.2009.12.004

B. Wyse, N. Ali, and D. H. Ellison, Interaction with grp58 increases activity of the thiazide-sensitive Na-Cl cotransporter, American Journal of Physiology - Renal Physiology, vol.282, issue.3, pp.424-430, 2002.
DOI : 10.1152/ajprenal.0028.2001

T. Panaretakis, N. Joza, N. Modjtahedi, A. Tesniere, I. Vitale et al., The co-translocation of ERp57 and calreticulin determines the immunogenicity of cell death, Cell Death and Differentiation, vol.21, issue.9, pp.1499-1509, 2008.
DOI : 10.1038/cdd.2008.67

M. Obeid, ERP57 Membrane Translocation Dictates the Immunogenicity of Tumor Cell Death by Controlling the Membrane Translocation of Calreticulin, The Journal of Immunology, vol.181, issue.4, pp.2533-2543, 2008.
DOI : 10.4049/jimmunol.181.4.2533

I. Ramírez-rangel, I. Bracho-valdés, A. Vázquez-macías, J. Carretero-ortega, G. Reyes-cruz et al., Regulation of mTORC1 Complex Assembly and Signaling by GRp58/ERp57, Molecular and Cellular Biology, vol.31, issue.8, pp.31-1657, 2011.
DOI : 10.1128/MCB.00824-10

D. D. Sarbassov and D. M. Sabatini, Redox Regulation of the Nutrient-sensitive Raptor-mTOR Pathway and Complex, Journal of Biological Chemistry, vol.280, issue.47, pp.39505-39509, 2005.
DOI : 10.1074/jbc.M506096200

R. Scherz-shouval, E. Shvets, E. Fass, H. Shorer, L. Gil et al., Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4, The EMBO Journal, vol.103, issue.7, pp.1749-1760, 2007.
DOI : 10.1038/sj.emboj.7601623

H. Ohtani, H. Wakui, T. Ishino, A. Komatsuda, and A. B. Miura, An isoform of protein disulfide isomerase is expressed in the developing acrosome of spermatids during rat spermiogenesis and is transported into the nucleus of mature spermatids and epididymal spermatozoa, Histochemistry, vol.265, issue.6, pp.423-429, 1993.
DOI : 10.1007/BF00267822

S. Coppari, F. Altieri, A. Ferraro, S. Chichiarelli, M. Eufemi et al., Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells, Journal of Cellular Biochemistry, vol.273, issue.2, pp.85-325, 2002.
DOI : 10.1002/jcb.10137

E. Y. Krynetski, N. F. Krynetskaia, M. E. Bianchi, and W. Evans, A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues, Cancer Res, vol.63, pp.100-106, 2003.

N. F. Krynetskaia, M. S. Phadke, S. H. Jadhav, and E. Krynetskiy, Chromatin-associated proteins HMGB1/2 and PDIA3 trigger cellular response to chemotherapy-induced DNA damage, Molecular Cancer Therapeutics, vol.8, issue.4, pp.864-872, 2009.
DOI : 10.1158/1535-7163.MCT-08-0695

L. Cicchillitti, D. Michele, M. Urbani, A. Ferlini, C. Donat et al., Comparative Proteomic Analysis of Paclitaxel Sensitive A2780 Epithelial Ovarian Cancer Cell Line and Its Resistant Counterpart A2780TC1 by 2D-DIGE: The Role of ERp57, Journal of Proteome Research, vol.8, issue.4, pp.1902-1912, 2009.
DOI : 10.1021/pr800856b

L. Cicchillitti, A. Della-corte, D. Michele, M. Donati, M. B. Rotilio et al., Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of ??-actin, International Journal of Oncology, vol.37, issue.2, pp.445-454, 2010.
DOI : 10.3892/ijo_00000693

A. Ferraro, F. Altieri, S. Coppari, M. Eufemi, S. Chichiarelli et al., Binding of the protein disulfide isomerase isoform ERp60 to the nuclear matrix-associated regions of DNA, Journal of Cellular Biochemistry, vol.380, issue.4, pp.72-528, 1999.
DOI : 10.1002/(SICI)1097-4644(19990315)72:4<528::AID-JCB8>3.0.CO;2-V

C. Grillo, S. Coppari, C. Turano, and F. Altieri, The DNA-binding activity of protein disulfide isomerase ERp57 is associated with the a??? domain, Biochemical and Biophysical Research Communications, vol.295, issue.1, pp.295-67, 2002.
DOI : 10.1016/S0006-291X(02)00634-4

S. Chichiarelli, A. Ferraro, F. Altieri, M. Eufemi, S. Coppari et al., The stress protein ERp57/GRP58 binds specific DNA sequences in HeLa cells, Journal of Cellular Physiology, vol.273, issue.2, pp.210-343, 2007.
DOI : 10.1002/jcp.20824

J. R. Schultz-norton, W. H. Mcdonald, J. R. Yates, and A. M. Nardulli, Protein Disulfide Isomerase Serves as a Molecular Chaperone to Maintain Estrogen Receptor ?? Structure and Function, Molecular Endocrinology, vol.20, issue.9, pp.1982-1995, 2006.
DOI : 10.1210/me.2006-0006

H. Coe, J. Jung, J. Groenendyk, D. Prins, and M. Michalak, ERp57 Modulates STAT3 Signaling from the Lumen of the Endoplasmic Reticulum, Journal of Biological Chemistry, vol.285, issue.9, pp.285-6725, 2010.
DOI : 10.1074/jbc.M109.054015

P. B. Sehgal, Plasma membrane rafts and chaperones in cytokine/STAT signaling, Acta Biochim. Pol, vol.50, pp.583-594, 2003.

M. Markus and R. Benezra, Two Isoforms of Protein Disulfide Isomerase Alter the Dimerization Status of E2A Proteins by a Redox Mechanism, Journal of Biological Chemistry, vol.274, issue.2, pp.1040-1049, 1999.
DOI : 10.1074/jbc.274.2.1040

T. Ozaki, T. Yamashita, and S. Ishiguro, ERp57-associated mitochondrial ??-calpain truncates apoptosis-inducing factor, Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, vol.1783, issue.10, pp.1955-1963, 2008.
DOI : 10.1016/j.bbamcr.2008.05.011

J. I. Murray, M. L. Whitfield, N. D. Trinklein, R. M. Myers, P. O. Brown et al., Diverse and Specific Gene Expression Responses to Stresses in Cultured Human Cells, Molecular Biology of the Cell, vol.15, issue.5, pp.2361-2374, 2004.
DOI : 10.1091/mbc.E03-11-0799

B. Rohe, S. E. Safford, I. Nemere, and M. C. Farach-carson, Regulation of expression of 1,25D3-MARRS/ERp57/PDIA3 in rat IEC-6 cells by TGF?? and 1,25(OH)2D3, Steroids, vol.72, issue.2, pp.144-150, 2007.
DOI : 10.1016/j.steroids.2006.11.013

M. Corazzari, P. E. Lovat, J. L. Armstrong, G. M. Fimia, D. S. Hill et al., Targeting homeostatic mechanisms of endoplasmic reticulum stress to increase susceptibility of cancer cells to fenretinide-induced apoptosis: the role of stress proteins ERdj5 and ERp57, British Journal of Cancer, vol.80, issue.7, pp.1062-1071, 2007.
DOI : 10.1124/mol.106.024323

P. E. Lovat, M. Corazzari, J. L. Armstrong, S. Martin, V. Pagliarini et al., Increasing Melanoma Cell Death Using Inhibitors of Protein Disulfide Isomerases to Abrogate Survival Responses to Endoplasmic Reticulum Stress, Cancer Research, vol.68, issue.13, pp.5363-5369, 2008.
DOI : 10.1158/0008-5472.CAN-08-0035

C. Hetz, M. Russelakis-carneiro, S. Wälchli, S. Carboni, E. Vial-knecht et al., The Disulfide Isomerase Grp58 Is a Protective Factor against Prion Neurotoxicity, Journal of Neuroscience, vol.25, issue.11, pp.25-2793, 2005.
DOI : 10.1523/JNEUROSCI.4090-04.2005

D. Xu, R. E. Perez, M. H. Rezaiekhaligh, M. Bourdi, and W. Truog, Knockdown of ERp57 increases BiP/GRP78 induction and protects against hyperoxia and tunicamycin-induced apoptosis, AJP: Lung Cellular and Molecular Physiology, vol.297, issue.1, pp.297-341, 2009.
DOI : 10.1152/ajplung.90626.2008

A. A. Dukes, V. S. Van-laar, M. Cascio, and T. G. Hastings, Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine, Journal of Neurochemistry, vol.366, issue.1, pp.333-346, 2008.
DOI : 10.1016/j.ceb.2006.06.005

J. S. Kim-han, O. Malley, and K. L. , Cell Stress Induced by the Parkinsonian Mimetic, 6-Hydroxydopamine, is Concurrent with Oxidation of the Chaperone, ERp57, and Aggresome Formation, Antioxidants & Redox Signaling, vol.9, issue.12, pp.2255-2264, 2007.
DOI : 10.1089/ars.2007.1791

Y. O. Akazawa, Y. Saito, K. Nishio, M. Horie, T. Kinumi et al., Proteomic characterization of the striatum and midbrain treated with 6-hydroxydopamine: Alteration of 58-kDa glucose-regulated protein and C/EBP homologous protein, Free Radical Research, vol.277, issue.4, pp.44-410, 2010.
DOI : 10.1126/science.1523409