E. Palmieri

Discrimination Motifs Determine Self-Nonself Lacking Conventional MHC Binding Anchor Differing by a Single Methyl Group and How H13 Histocompatibility Peptides

N. Shastri, S. Almo, D. Roopenian, 2001 .

A simplified procedure for the preparation of MHC/peptide tetramers: chemical biotinylation of an unpaired cysteine engineered at the C-terminus of MHC-I.

S. Honda, S. Nathenson, A. Kalergis, 2000, Journal of immunological methods.

Predominant occupation of the class I MHC molecule H-2Kwm7 with a single self-peptide suggests a mechanism for its diabetes-protective effect.

J. Shabanowitz, D. Hunt, V. Malashkevich, 2010, International immunology.

Structure-guided development of a high-affinity human Programmed Cell Death-1: Implications for tumor immunotherapy

S. Almo, C. Guha, S. Nathenson, 2017, EBioMedicine.

An in vitro study of the dynamic features of the major histocompatibility complex class I complex relevant to its role as a versatile peptide-receptive molecule.

R. Angeletti, N. Papadopoulos, S. Nathenson, 1997, Proceedings of the National Academy of Sciences of the United States of America.

Efficient T cell activation requires an optimal dwell-time of interaction between the TCR and the pMHC complex

Alexis M. Kalergis, Immanuel F. Luescher, S. Nathenson, 2001, Nature Immunology.

T cell receptor binding kinetics required for T cell activation depend on the density of cognate ligand on the antigen-presenting cell.

Daniel Coombs, Byron Goldstein, B. Goldstein, 2005, Proceedings of the National Academy of Sciences of the United States of America.

How H13 Histocompatibility Peptides Differing by a Single Methyl Group and Lacking Conventional MHC Binding Anchor Motifs Determine Self-Nonself Discrimination1

H. Grey, N. Shastri, S. Almo, 2002, The Journal of Immunology.

Discrimination Motifs Determine Self-Nonself Lacking Conventional MHC Binding Anchor Differing by a Single Methyl Group and How H13 Histocompatibility Peptides

H. Grey, N. Shastri, S. Almo, 2001 .

Hybrid association between human apolipoproteins A-I and A-II in aqueous solution and in phospholipid recombinants.

J. Swaney, E. Palmieri, 1984, Biochimica et biophysica acta.