Author

D. Moschidi

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Immunology· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Assay:proteomics· 3 Research Focus:cell type annotation· 2 Research Focus:clustering· 2 Approach:deep learning· 2 Research Focus:differential expression· 2 Approach:experimental assay· 2 Organism:human· 2 Approach:statistical model· 2

Frequent Co-Authors

N. G. Sgourakis· 4 shared A. C. McShan· 3 shared C. A. Devlin· 2 shared E. Procko· 2 shared J. S. Toor· 2 shared S. A. Overall· 2 shared A. S. Japp· 1 shared D. A. Fletcher· 1 shared

Activity by Year

2019-2020 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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4 shared papersImmunology

N. G. Sgourakis

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4 papers

Recent·Most cited

TAPBPR Promotes Antigen Loading on MHC-I Molecules Using a Peptide Trap

A. C. McShan, C. A. Devlin, G. I. Morozov, S. Overall, D. Moschidi, N. Akella, E. Procko, N. G. Sgourakis

This study identifies the role of TAPBPR's 16-residue loop in promoting peptide loading on MHC-I by acting as a kinetic trap, not by competing with incoming peptides.

bioRxiv · Apr 24, 2020Immunology

Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection

A. C. McShan, C. A. Devlin, S. A. Overall, J. Park, J. S. Toor, D. Moschidi, D. Flores-Solis, H. Choi, S. Tripathi, E. Procko, N. G. Sgourakis

This paper identifies molecular determinants of TAPBPR chaperone interactions with MHC-I molecules, showing that conformational dynamics and disulfide bonds influence recognition and antigen repertoire selection.

bioRxiv · Sep 24, 2019Immunology

Computational design of a protein family that adopts two well-defined and structurally divergent de novo folds

K. Y. Wei, D. Moschidi, M. J. Bick, S. Nerli, A. C. McShan, L. P. Carter, P.-S. Huang, D. A. Fletcher, N. G. Sgourakis, S. E. Boyken, D. Baker

This paper designs a protein family with two structurally divergent folds, showing that sequences can adopt distinct conformations under different conditions.

bioRxiv · Sep 4, 2019 · PreprintBiochemistry

High Throughput pMHC-I Tetramer Library Production Using Chaperone Mediated Peptide Exchange

S. A. Overall, J. S. Toor, S. Hao, M. Yarmarkovich, S. Nguyen, A. S. Japp, D. Moschidi, M. R. Betts, J. M. Maris, P. Smibert, N. G. Sgourakis

The paper introduces a method to produce pMHC-I tetramer libraries using TAPBPR chaperone-mediated peptide exchange, enabling high-throughput analysis of TCR repertoires and pMHC-I specificities.

bioRxiv · May 30, 2019Immunology