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Human Immunology|February 22, 2020
Cytometry-based analysis of HLA-G functions according to ILT2 expressionA Jacquier, C Dumont, E D Carosella, et al.
Human Immunology|January 4, 2001
HLA-G truncated isoforms can substitute for HLA-G1 in fetal survivalC Menier, B Riteau, J Dausset, et al.
Proceedings of the National Academy of Sciences of the United States of America|October 23, 1997
Direct evidence to support the role of HLA-G in protecting the fetus from maternal uterine natural killer cytolysisN Rouas-Freiss, R M Gonçalves, C Menier, et al.
Tissue Antigens|April 21, 2007
Quantification and identification of soluble HLA-G isoformsV Rebmann, J LeMaoult, N Rouas-Freiss, et al.
Human Immunology|January 4, 2001
HLA-G expression in trophoblast cells is independent of embryonic developmentM Rabreau, N Rouas-Freiss, M Landi, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 13, 1997
The alpha1 domain of HLA-G1 and HLA-G2 inhibits cytotoxicity induced by natural killer cells: is HLA-G the public ligand for natural killer cell inhibitory receptors?N Rouas-Freiss, R E Marchal, M Kirszenbaum, et al.
Journal of Immunology (Baltimore, Md. : 1950)|April 6, 2001
HLA-G2, -G3, and -G4 isoforms expressed as nonmature cell surface glycoproteins inhibit NK and antigen-specific CTL cytolysisB Riteau, N Rouas-Freiss, C Menier, et al.
Journal of Immunology (Baltimore, Md. : 1950)|February 1, 1993
Influence of protein-quaternary structure on antigen processingN Rouas, S Christophe, F Housseau, et al.
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