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dc.contributor.authorMénoret, A.fr_FR
dc.contributor.authorLe Pendu, J.fr_FR
dc.date.accessioned2013-02-15T12:00:34Z
dc.date.available2013-02-15T12:00:34Z
dc.date.issued1994fr_FR
dc.identifier.citationMénoret, A. ; Le Pendu, J., Protéines de choc thermique et antigènes tumoraux, Med Sci (Paris), 1994, Vol. 10, N° 6-7; p.665-71fr_FR
dc.identifier.issn1958-5381fr_FR
dc.identifier.urihttp://hdl.handle.net/10608/2683
dc.description.abstractHeat shock proteins (HSP) belong to the family of chaperone molecules. They associate with peptides or misfolded proteins. Their role as peptide binders and as transporters of these peptides to MHC molecules, as well as the presence of constitutive anti-HSP immune responses, suggest an important role for these proteins in cellular immunity. In tumor cells, HSPs are often overexpressed and associated with <<abnormal>> proteins which are potentially antigenic. Immunisation against some HSPs (grp94, hsp70) purified from some tumors protects animals from a challenge with the tumor from which they were purified. This protection is dependent on the association between HSP and immunogenic peptides(s). However, the nature of these peptides is still unknown and the mechanisms of the HSP-mediated anti-tumor response are not yet fully understood.fr
dc.language.isofrfr_FR
dc.publisherJohn Libbey Eurotext, Montrougefr_FR
dc.rightsArticle en libre accèsfr
dc.rightsMédecine/Sciences - Inserm - SRMSfr
dc.sourceM/S. Médecine sciences [revue papier, ISSN : 0767-0974], 1994, Vol. 10, N° 6-7; p.665-71fr_FR
dc.titleProtéines de choc thermique et antigènes tumorauxfr
dc.typeArticlefr_FR
dc.identifier.doi10.4267/10608/2683


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