dc.contributor.author | Ménoret, A. | fr_FR |
dc.contributor.author | Le Pendu, J. | fr_FR |
dc.date.accessioned | 2013-02-15T12:00:34Z | |
dc.date.available | 2013-02-15T12:00:34Z | |
dc.date.issued | 1994 | fr_FR |
dc.identifier.citation | Ménoret, A. ; Le Pendu, J., Protéines de choc thermique et antigènes tumoraux, Med Sci (Paris), 1994, Vol. 10, N° 6-7; p.665-71 | fr_FR |
dc.identifier.issn | 1958-5381 | fr_FR |
dc.identifier.uri | http://hdl.handle.net/10608/2683 | |
dc.description.abstract | Heat 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.iso | fr | fr_FR |
dc.publisher | John Libbey Eurotext, Montrouge | fr_FR |
dc.rights | Article en libre accès | fr |
dc.rights | Médecine/Sciences - Inserm - SRMS | fr |
dc.source | M/S. Médecine sciences [revue papier, ISSN : 0767-0974], 1994, Vol. 10, N° 6-7; p.665-71 | fr_FR |
dc.title | Protéines de choc thermique et antigènes tumoraux | fr |
dc.type | Article | fr_FR |
dc.identifier.doi | 10.4267/10608/2683 | |