Author

A. C. McShan

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:deep learning· 2 Organism:human· 2 Assay:proteomics· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Research Focus:differential expression· 1

Frequent Co-Authors

D. Moschidi· 3 shared N. G. Sgourakis· 3 shared C. A. Devlin· 2 shared E. Procko· 2 shared D. A. Fletcher· 1 shared D. Baker· 1 shared D. Flores-Solis· 1 shared G. I. Morozov· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersImmunology

D. Moschidi

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Author profile →

3 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