Crystal structure of a TAPBPR–MHC I complex reveals the mechanism of peptide editing in antigen presentation J Jiang, K Natarajan, LF Boyd, GI Morozov, MG Mage, DH Margulies Science 358 (6366), 1064-1068, 2017 | 121 | 2017 |
Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing GI Morozov, H Zhao, MG Mage, LF Boyd, J Jiang, MA Dolan, R Venna, ... Proceedings of the National Academy of Sciences 113 (8), E1006-E1015, 2016 | 93 | 2016 |
Mapping of functional domains in p47(phox) involved in the activation of NADPH oxidase by "peptide walking". I Morozov, O Lotan, G Joseph, Y Gorzalczany, E Pick Journal of Biological Chemistry 273 (25), 15435-44, 1998 | 53 | 1998 |
High throughput pMHC-I tetramer library production using chaperone-mediated peptide exchange SA Overall, JS Toor, S Hao, M Yarmarkovich, SM O’Rourke, GI Morozov, ... Nature communications 11 (1), 1909, 2020 | 48 | 2020 |
TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap AC McShan, CA Devlin, GI Morozov, SA Overall, D Moschidi, N Akella, ... Nature communications 12 (1), 3174, 2021 | 39 | 2021 |
TAPBPR employs a ligand-independent docking mechanism to chaperone MR1 molecules AC McShan, CA Devlin, GF Papadaki, Y Sun, AI Green, GI Morozov, ... Nature chemical biology 18 (8), 859-868, 2022 | 17 | 2022 |
Production of soluble pMHC-I molecules in mammalian cells using the molecular chaperone TAPBPR SM O’Rourke, GI Morozov, JT Roberts, AW Barb, NG Sgourakis Protein Engineering, Design and Selection 32 (12), 525-532, 2019 | 12 | 2019 |
Flavin Reductase Contributes to Pneumococcal Virulence by Protecting from Oxidative Stress and Mediating Adhesion and Elicits Protection Against Pneumococcal Challenge Scientific Reports 8 (314), 2018 | 12 | 2018 |
Illuminating the Mechanism of MHC-I Folding and Antigen Repertoire Selection Using Deep Mutational Scanning and Biophysical Studies N Sgourakis, AC McShan, CA Devlin, G Morozov, E Procko The Journal of Immunology 204 (1_Supplement), 140.21-140.21, 2020 | | 2020 |
Insights into MHC-I peptide loading obtained from the structure of a TAPBPR/MHC-I complex K Natarajan, J Jiang, LF Boyd, GI Morozov, MG Mage, DH Margulies The Journal of Immunology 198 (1_Supplement), 146.25-146.25, 2017 | | 2017 |
NIAID, NIH. J Jiang, K Natarajan, LF Boyd, GI Morozov, MG Mage, DH Margulies Acta Cryst 73, a80, 2017 | | 2017 |
TAPBPR, a Peptide Editor–interactions with MHC complexes and SAXS structural studies K Natarajan, G Morozov, J Jiang, LF Boyd, MG Mage, DH Margulies The Journal of Immunology 196 (1_Supplement), 116.5-116.5, 2016 | | 2016 |
Tapasin-related protein TAPBP-R interacts directly with peptide-free MHC-I/beta 2-microglobulin complexes and is released by high affinity peptides GI Morozov, H Zhao, MG Mage, LF Boyd, WH Hildebrand, C McMurtrey, ... MOLECULAR IMMUNOLOGY 68 (2), 149-149, 2015 | | 2015 |
Direct interaction of recombinant TAPBPR with MHC-I molecules: stabilization of peptide-free MHC-I promotes high affinity peptide loading (APP5P. 102) G Morozov, H Zhao, M Mage, L Boyd, R Venna, M Norcross, C McMurtrey, ... The Journal of Immunology 194 (1_Supplement), 183.4-183.4, 2015 | | 2015 |
Tapasin-related protein TAPBPR interacts directly with peptide-free MHC-I/β2-microgolbulin complexes (APP3P. 101) G Morozov, H Zhao, M Mage, L Boyd, P Schuck, K Natarajan, D Margulies The Journal of Immunology 192 (1_Supplement), 111.2-111.2, 2014 | | 2014 |