R. Adams and J. , Preclinical and clinical evaluation of proteasome inhibitor PS-341 for the treatment of cancer, Current Opinion in Chemical Biology, vol.6, issue.4
DOI : 10.1016/S1367-5931(02)00343-5

J. Adams, The proteasome: structure, function, and role in the cell, Cancer Treatment Reviews, vol.29, pp.3-9, 2003.
DOI : 10.1016/S0305-7372(03)00081-1

J. B. Almond and G. M. Cohen, The proteasome: a novel target for cancer chemotherapy, Leukemia, vol.16, issue.4, 2002.
DOI : 10.1038/sj.leu.2402417

L. A. Sklar, J. Baumler, E. Gogol, and D. Skowyra, ATP hydrolysis-dependant disassembly of the 26S proteasome is part of the catalytic cycle, Cell, vol.121, pp.553-65, 2005.

J. E. Gairin, A new generation of MELAN-A/MART- 1 peptides that fulfill both increased immunogenicity and high resistance to biodegradation : implication for molecular anti-melanoma immunotherapy, J. Immunol, vol.167, pp.5852-5861, 2001.

J. C. Bourdon, K. Fernandes, F. Murray-zmijewski, G. Liu, A. Diot et al., p53 isoforms can regulate p53 transcriptional activity, p53 isoforms can regulate p53 transcriptional activity, pp.2122-2137, 2005.
DOI : 10.1101/gad.1339905

URL : http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221884

B. Boes, H. Hengel, T. Ruppert, U. H. Multhaup, U. H. Koszinowski et al., Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes, Journal of Experimental Medicine, vol.179, issue.3, pp.901-909, 1994.
DOI : 10.1084/jem.179.3.901

S. Bose, P. Brooks, G. G. Mason, and A. J. Rivett, Gamma- Interferon decreases the level of 26 S proteasomes and changes the pattern of phosphorylation, Biochem J, vol.353, pp.291-297, 2001.

S. Bose, F. L. Stratford, K. I. Broadfoot, G. G. Mason, and A. J. Rivett, Phosphorylation of 20S alpha subunit C8 (?7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by g-interferon Biochem, J, vol.378, pp.177-84, 2004.

A. Ciechanover, The ubiquitin-proteasome pathway: on protein death and cell life, The EMBO Journal, vol.17, issue.24, pp.7151-7160, 1998.
DOI : 10.1093/emboj/17.24.7151

O. Coux, K. Tanaka, and A. L. Goldberg, Structure and Functions of the 20S and 26S Proteasomes, Annual Review of Biochemistry, vol.65, issue.1
DOI : 10.1146/annurev.bi.65.070196.004101

Y. Feng, D. L. Longo, and D. K. Ferris, Polo-like kinase interacts with proteasomes and regulates their activity

G. Fenteany, R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey et al., Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin, Science, vol.31, issue.4, pp.726-731, 1995.
DOI : 10.1021/bi00119a004

M. Gaczynska, K. L. Rock, and A. L. Goldberg, ??-Interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes, Nature, vol.365, issue.6443, pp.264-267, 1993.
DOI : 10.1038/365264a0

A. L. Golberg and K. L. Rock, Not just research tools, proteasome inhibitors offer therapeutic promise

M. Groll, L. Ditzel, J. Lowe, D. Stock, M. Bochtler et al., Structure of 20S proteasome from yeast at 2.4?? resolution, Nature, vol.386, issue.6624, pp.463-471, 1997.
DOI : 10.1038/386463a0

M. Groll and R. Huber, Substrate access and processing by the 20S proteasome core particle, The International Journal of Biochemistry & Cell Biology, vol.35, issue.5, pp.606-616, 2003.
DOI : 10.1016/S1357-2725(02)00390-4

R. Horiguchi, M. Yoshikuni, M. Tokumoto, Y. Nagahama, and T. Tokumoto, Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes. Cellular Signaling, pp.205-215, 2005.

C. D. Hu, Y. Chinenov, and T. K. Kerppola, Visualization of Interactions among bZIP and Rel Family Proteins in Living Cells Using Bimolecular Fluorescence Complementation, Molecular Cell, vol.9, issue.4, 2002.
DOI : 10.1016/S1097-2765(02)00496-3

A. F. Kisselev and A. L. Goldberg, Proteasome inhibitors: from research tools to drug candidates, Chemistry & Biology, vol.8, issue.8, pp.739-758, 2001.
DOI : 10.1016/S1074-5521(01)00056-4

P. Kloetzel, Antigen processing by the proteasome, Nat. Rev

A. Kölher, P. Cascio, D. S. Leggett, K. M. Woo, A. L. Goldberg et al., The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release, Mol. Cell, vol.7, pp.1143-1152, 2001.

Z. Kostova and D. H. Wolf, NEW EMBO MEMBER'S REVIEW: For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection, The EMBO Journal, vol.22, issue.10, pp.2309-2317, 2003.
DOI : 10.1093/emboj/cdg227

Y. A. Lam, T. G. Lawson, M. Velayutham, J. L. Zweier, and C. M. Pickart, A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal, Nature, vol.416, issue.6882, pp.763-767, 2002.
DOI : 10.1038/416763a

G. Melino, X. Lu, M. Gasco, T. Crook, and R. A. Knight, Functional regulation of p73 and p63: development and cancer, Trends in Biochemical Sciences, vol.28, issue.12, pp.663-6670, 2003.
DOI : 10.1016/j.tibs.2003.10.004

A. Belisle and J. N. Pelletier, Detection of protein-protein interactions by protein fragment complementation strategies, Methods Enzymol, vol.328, pp.208-230, 2000.

D. Sohn, G. Totzke, F. Essmann, K. Schulze-osthoff, B. Levkau et al., The Proteasome Is Required for Rapid Initiation of Death Receptor-Induced Apoptosis, Molecular and Cellular Biology, vol.26, issue.5
DOI : 10.1128/MCB.26.5.1967-1978.2006

R. Velthoven, J. C. Cerottini, T. Boon, J. E. Gairin, and B. J. Van-den-eynde, Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells, Immunity, vol.12, pp.107-117, 2000.

R. Z. Orlowski, The role of the ubiquitin-proteasome pathway in apoptosis, Cell Death and Differentiation, vol.6, issue.4, 1999.
DOI : 10.1038/sj.cdd.4400505

M. Rechsteiner and C. P. Hill, Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors, Trends in Cell Biology, vol.15, issue.1, pp.27-33, 2005.
DOI : 10.1016/j.tcb.2004.11.003

K. L. Rock and A. L. Goldberg, DEGRADATION OF CELL PROTEINS AND THE GENERATION OF MHC CLASS I-PRESENTED PEPTIDES, Annual Review of Immunology, vol.17, issue.1, pp.739-779, 1999.
DOI : 10.1146/annurev.immunol.17.1.739

H. Sawada, Assembly of the 26S proteasome is regulated by phosphorylation of the p45, 2001.

O. Schiltz, G. Warnier, V. Russo, S. Morel, F. Lévy et al., The Production of a New MAGE-3 Peptide Presented to Cytolytic T Lymphocytes by HLA-B40 Requires the Immunoproteasome, The Journal of Experimental Medicine, vol.1402, issue.4, pp.391-399, 2002.
DOI : 10.1016/S1074-7613(01)00203-5

A. J. Sijts, S. Standera, R. E. Toes, T. Ruppert, N. J. Beekman et al., MHC Class I Antigen Processing of an Adenovirus CTL Epitope Is Linked to the Levels of Immunoproteasomes in Infected Cells, The Journal of Immunology, vol.164, issue.9, pp.4500-4506, 2000.
DOI : 10.4049/jimmunol.164.9.4500

M. Unno, T. Mizushima, Y. Morimoto, Y. Tomisugi, K. Tanaka et al., The Structure of the Mammalian 20S Proteasome at 2.75 ?? Resolution, Structure, vol.10, issue.5, pp.609-627, 2002.
DOI : 10.1016/S0969-2126(02)00748-7

V. Ustrell, L. Hoffman, G. Pratt, and M. Rechsteiner, PA200, a nuclear proteasome activator involved in DNA repair, The EMBO Journal, vol.21, issue.13
DOI : 10.1093/emboj/cdf333

B. J. Van-den-eynde, Differential processing of class-I-restricted epitopes by the standard proteasome and the immunoproteasome, Current Opinion in Immunology, vol.13, issue.2, pp.147-153, 2001.
DOI : 10.1016/S0952-7915(00)00197-7

R. Verma, L. Aravind, R. Oania, W. H. Mcdonald, I. J. Yates et al., Role of Rpn11 Metalloprotease in Deubiquitination and Degradation by the 26S Proteasome, Science, vol.298, issue.5593, pp.611-615, 2002.
DOI : 10.1126/science.1075898

D. Vosges, P. Zwickl, and W. Baumeister, The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis, Annual Review of Biochemistry, vol.68, issue.1, pp.1015-1068, 1999.
DOI : 10.1146/annurev.biochem.68.1.1015

T. Yoodvidhya, E. Girbal, R. M. Willemot, and P. Monsan, Mechanism of enzyme stabilization, Ann. N.Y. Acad. Sci, vol.501, pp.59-62, 1987.

E. Girbal, R. Binot, and P. Monsan, Production, purification, properties and kinetic studies of free and immobilized polyphosphate: glucose-6-phosphotransferase from Mycobacterium phlei, Enzyme and Microbial Technology, vol.11, issue.8, pp.518-527, 1989.
DOI : 10.1016/0141-0229(89)90034-3

C. Vincent, G. Serre, J. Basile, H. Lestra, E. Girbal et al., Subclass distribution of IgG antibodies to the rat oesophagus stratum corneum (so-called anti-keratin antibodies) in rheumatoid arthritis, Clinical & Experimental Immunology, vol.23, issue.1, pp.83-89, 1990.
DOI : 10.1111/j.1365-2249.1990.tb05295.x

M. Simon, E. Girbal, M. Sebbag, V. Gomès-daudrix, C. Vincent et al., Molecular characterization of the rat and human antigens recognized by the so-called "antikeratin" autoantibodies specific for rheumatoid arthritis, EOS -Journal of Immunol. and Immunopharmacol, vol.13, pp.127-128, 1993.

E. Girbal, M. Sebbag, V. Gomès-daudrix, M. Simon, C. Vincent et al., Characterisation of the rat oesophagus epithelium antigens defined by the so-called 'antikeratin antibodies', specific for rheumatoid arthritis., Annals of the Rheumatic Diseases, vol.52, issue.10, pp.749-757, 1993.
DOI : 10.1136/ard.52.10.749

B. Abbal, G. Fournié, and . Serre, Immunoblotting detection of the so-called "antikeratin antibodies": a new assay for the diagnosis of rheumatoid arthritis, Ann. Rheum. Dis, vol.53, pp.735-742, 1994.

D. Sommé, G. Schmitt, and . Serre, Monoclonal antibodies to human epidermal filaggrin, some not recognizing profilaggrin, J. Invest. Dermatol, vol.105, pp.432-437, 1995.

. Serre, Evidence that filaggrin is a component of cornified cell envelopes in human plantar epidermis, Biochem. J, vol.317, pp.173-177, 1996.

. Serre, Normal human epidermal keratinocytes express in vitro-specific molecular forms of (pro)filaggrin recognized by rheumatoid arthritis-associated antifilaggrin autoantibodies

B. Fournié, G. Mazières, and . Serre, Immunoblotting detection of autoantibodies to human epidermis filaggrin: a new diagnostic test for rheumatoid arthritis, J. Rheumatol, vol.25, pp.838-846, 1998.

T. Simon, C. Senshu, C. Masson-bessière, M. Jolivet, G. Jolivet et al., The epitopes targeted by the rheumatoid arthritis-associated antifilaggrin autoantibodies are posttranslationally generated on various sites of (pro)filaggrin by deimination of arginine residues

C. Masson-bessière, M. Sebbag, J. Durieux, L. Nogueira, C. Vincent et al., In the rheumatoid pannus, anti-filaggrin autoantibodies are produced by local plasma cells and constitute a higher proportion of IgG than in synovial fluid and serum, Clinical and Experimental Immunology, vol.24, issue.3, pp.544-552, 2000.
DOI : 10.1073/pnas.93.1.221

C. Masson-bessière, M. Sebbag, E. Girbal-neuhauser, L. Nogueira, C. Vincent et al., The Major Synovial Targets of the Rheumatoid Arthritis-Specific Antifilaggrin Autoantibodies Are Deiminated Forms of the ??- and ??-Chains of Fibrin, The Journal of Immunology, vol.166, issue.6, pp.4177-4184, 2001.
DOI : 10.4049/jimmunol.166.6.4177

M. Sebbag, E. Girbal, V. Gomès, M. Simon, C. Vincent et al., Nouveaux antigènes de différenciation de l'épithélium malpighien cornifié d'oesophage de rat, définis par les autoanticorps anti-Stratum Corneum, spécifiques de la Polyarthrite Rhumatoïde, Congrès Annuel de Recherche Dermatologique, 1992.

E. Girbal, M. Sebbag, V. Gomès, F. Croute, and G. Serre, Expression de la (pro)filaggrine dans les épithéliums malpighiens cornifiés non épidermiques : nouvelles formes moléculaires définies dans l'oesophage de rat par des auto-anticorps humains, Congrès Annuel de Recherche Dermatologique, 1992.

E. Girbal, M. Montézin, F. Croute, M. Sebbag, M. Simon et al., Formes moléculaires des (pro)filaggrines dans des cultures de kératinocytes humains réalisés en conditions différenciantes, Congrès Annuel de Recherche Dermatologique, 1993.

E. Girbal, M. Montézin, F. Croute, M. Simon, M. Sebbag et al., Expression de l'antigène défini par les autoanticorps dits "antikératine, spécifiques de la Polyarthrite Rhumatoïde, par des kératinocytes humains en culture. 4ème Journée de l'Association pour la Recherche sur la Polyarthrite, 1993.

M. Simon, M. Sebbag, E. Girbal, C. Vincent, L. Boissier et al., Les autoanticorps anti-Stratum Corneum, spécifiques de la polyarthrite rhumatoïde, sont dirigés contre la filaggrine épidermique humaine et contre un variant acide de cette protéine

E. Girbal, M. Sebbag, V. Gomès-daudrix, M. Simon, C. Vincent et al., Caractérisation des antigènes de l'épithélium d'oesophage de rat définis par les autoanticorps anti-Stratum Corneum dits "antikératines" spécifiques de la polyarthrite rhumatoïde, 1993.

M. Sebbag, M. Simon, M. Bessières, C. Vincent, C. Girbal et al., Les facteurs anti-périnucléaires, auto-anticorps spécifiques de la polyarthrite rhumatoïde, sont dirigés contre des protéines des cellules de l'épithélium jugal apparentées à la (pro)filaggrine épidermique humaine, Congrès Annuel de Recherche Dermatologique, 1994.

J. Durieux, E. Girbal-neuhauser, M. Simon, V. Mils, C. Vincent et al., Epitopes reconnus par les auto-anticorps anti-filaggrine, spécifiques de la polyarthrite rhumatoïde, 6ème Journée de l'Association pour la Recherche sur la Polyarthrite, 1995.

M. Simon, J. Durieux, V. Mils, E. Girbal-neuhauser, M. Arnaud et al., Cartographie épitopique de 29 anticorps monoclonaux spécifiques de la (pro)filaggrine humaine, Congrès Annuel de Recherche Dermatologique, 1996.

E. Girbal-neuhauser, J. Durieux, L. Sailler, G. Salama, C. Masson-bessière et al., Les épitopes reconnus par les autoanticorps antifilaggrine, spécifiques de la polyarthrite rhumatoïde, sont générés par des modifications post-trductionnelles, 1996.

J. Durieux, C. Vincent, M. Sebbag, E. Girbal-neuhauser, and G. Serre, Identification de deux épitopes majeurs reconnus par les auto-anticorps anti-filaggrine, spécifiques de la polyarthrite rhumatoïde

B. Xu, E. Girbal-neuhauser, B. Monsarrat, and J. Gairin, Ajoene: a novel inhibitor of 20S human proteasome. VIII ème colloque " De la recherche à la découverte, 2003.

M. Sebbag, M. Simon, J. Durieux, E. Girbal-neuhauser, C. Vincent et al., Des anticorps « antikératines

G. Serre, Antikeratin antibodies (AKA) and perinuclear factor (APF) are the same autoantibodies directed to filaggrin, Rheumatology News International, vol.23, issue.6, 1995.

S. Mireille, Identification des antigènes de différenciation malpighienne définis par les autoanticorps anti-Stratum Corneum

. Masson-bessière-christine, Les autoanticorps antifilaggrine dans la polyarthrite rhumatoïde : relation avec les facteurs antipérinucléaires, synthèse articulaire et antigènes-cibles du pannus synovial, Toulouse III (Physiopathologie Humaine), 9 novembre, 1999.

S. Claverol, Le protéasome 20S humain : étude des relations structure-fonction par spectrométrie de masse et approches protéomiques, Biochimie, pp.12-2003

X. Bo, Le protéasome 20S humain, une nouvelle cible en thérapie anticancéreuse : effet de l'ajoëne, molécule naturelle anti-tumorale, et impact de modifications posttraductionnelles sur son activité catalytique, pp.12-2003

E. Rothmonie, Etude du rôle de l'immuno-protéasome dans le développement du mélanome. Doctorat de l'Université Paul Sabatier, Toulouse III, en cours depuis octobre, 2004.

R. Isabelle, Etude de la spécificité des auto-anticorps naturels humains de classe G anti-cytokératines épidermiques

C. Christine, Expression in vitro d'antigènes tardifs de différenciation des kératinocytes définis par des auto-anticorps humains spécifiques de la polyarthrite rhumatoïde, 1992.

. Masson-bessière-christine, Les auto-anticorps anti-Stratum Corneum et les facteurs antipérinucléaires , tous deux marqueurs spécifiques de la Polyarthrite Rhumatoïde, sont une seule et même entité sérologique, pp.28-1993

M. Martine, Etude du métabolisme des (pro)filaggrines dans des cultures de kératinocytes humains, 1993.

C. Thomas, Caractérisation de modifications post-traductionnelles sur le protéasome 20S humain. DEA de Biologie-Santé-Biotechnologie, 2001.

B. Christophe, Conception et validation de substrats fluorescents du protéasome

S. Cindy, Le protéasome, une nouvelle cible d'interêt pharmacologique : étude comparative du protéasome 20S de différentes lignées tumorales humaines. DEA de Biologie-Santé-Biotechnologie, 2004.

M. Diplômes-d-'etudes-supérieures-d-'université and . Caroline, Mise au point d'un protocole de purification et caractérisation structurale et fonctionnelle du protéasome 26S humain. DESU de l, 2003.

A. Sandrine, Etude des modifications post-traductionnelles du protéasome 20S. DESU de l, 2004.

E. Rothmonie, Etude de la modification par phosphorylation du protéasome 20S d'érythrocytes humains, 2004.

M. Professionnel and M. Houssaini-moulay-soufyan, Mise au point d'outils moléculaires et cellulaires pour mesurer l'activité des protéasomes, Master Biochimie -Ingénierie Biochimique

S. Ingénieur and B. Aurélie, Développement de tests spécifiques pour le dosage des activités catalytiques du protéasome et de l'immunoprotéasome

. Serre, The cytokeratin filament-aggregating protein filaggrin is the target of the so-called "antikeratin antibodies", autoantibodies specific for rheumatoid arthritis, J. Clin. Invest, vol.92, pp.1387-1393, 1993.

T. Simon, C. Senshu, C. Masson-bessière, M. Jolivet, G. Jolivet et al., The epitopes targeted by the rheumatoid arthritis-associated antifilaggrin autoantibodies are posttranslationally generated on various sites of (pro)filaggrin by deimination of arginine residues, J. Immunol, vol.162, pp.585-94, 1999.

C. Masson-bessière, M. Sebbag, E. Girbal-neuhauser, L. Nogueira, C. Vincent et al., The Major Synovial Targets of the Rheumatoid Arthritis-Specific Antifilaggrin Autoantibodies Are Deiminated Forms of the ??- and ??-Chains of Fibrin, The Journal of Immunology, vol.166, issue.6
DOI : 10.4049/jimmunol.166.6.4177

S. Claverol, O. Burlet-schiltz, E. Girbal-neuhauser, J. E. Gairin, and B. Monsarrat, Mapping and Structural Dissection of Human 20 S Proteasome Using Proteomic Approaches, Molecular & Cellular Proteomics, vol.1, issue.8, pp.567-578, 2002.
DOI : 10.1074/mcp.M200030-MCP200

X. Bo, B. Monsarrat, J. E. Gairin, and E. Girbal-neuhauser, Effect of Ajoene, a natural antitumor small molecule, on human 20S proteasome activity in vitro and in human leukemic HL-60 cells, Fundam. Clin. Pharmacol, vol.18, pp.171-180, 2004.