C. Buhot

发表

CD4+ T-cell clones specific for wild-type factor VIII: a molecular mechanism responsible for a higher incidence of inhibitor formation in mild/moderate hemophilia A.

J. Vermylen, B. Maillère, K. Peerlinck, 2003, Blood.

Peptide-Binding Specificity Molecule , Defines a New Supertype of HLA-DP 4 , the Most Frequent HLA II

H. Zarour, A. Ménez, B. Maillère, 2002 .

Development and preliminary clinical evaluation of a peptide immunotherapy vaccine for cat allergy.

M. Worm, A. Kay, B. Maillère, 2011, The Journal of allergy and clinical immunology.

Emerging principles for the design of promiscuous HLA‐DR‐restricted peptides: an example from the major bee venom allergen

A. Ménez, B. Maillère, C. Texier, 2002, European journal of immunology.

Immunotherapeutic potential of the immunodominant T‐cell epitope of lipocalin allergen Bos d 2 and its analogues

B. Maillère, A. Kauppinen, A. Närvänen, 2008, Immunology.

The immunodominant epitope of lipocalin allergen Bos d 2 is suboptimal for human T cells.

B. Maillère, A. Närvänen, R. Mäntyjärvi, 2003, European journal of immunology.

HLA-DP4, the Most Frequent HLA II Molecule, Defines a New Supertype of Peptide-Binding Specificity1

Alain Sanson, H. Zarour, A. Ménez, 2002, The Journal of Immunology.

Alteration of the tertiary structure of the major bee venom allergen Api m 1 by multiple mutations is concomitant with low IgE reactivity

M. Gelb, A. Ménez, B. Maillère, 2004, Protein science : a publication of the Protein Society.

Bee venom phospholipase A2 as a membrane-binding vector for cell surface display or internalization of soluble proteins.

A. Chenal, D. Gillet, C. Almunia, 2016, Toxicon : official journal of the International Society on Toxinology.

The immunodominant epitope of lipocalin allergen Bos d 2 is suboptimal for human T cells

B. Maillère, R. Mäntyjärvi, T. Kinnunen, 2003 .