Julia N Danon
6 Papers
Julia N Danon is an academic researcher. The author has contributed to research in topics: Major histocompatibility complex & Medicine. The author has an hindex of 1, co-authored 4 publications.
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Papers
Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes
Yi Sun,Michael C. Young,Claire H. Woodward,Julia N Danon,H. V. Truong,Sagar Gupta,Trenton J Winters,Joan Font-Burgada,George M. Burslem,Nikolaos G. Sgourakis +9 more
TL;DR: In this article , a structure-guided approach for generating conformationally stable, open MHC-I with enhanced ligand exchange kinetics spanning five HLA-A supertypes, all HLA B supertypes and oligomorphic HLAIb allotypes is presented.
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Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes
Yi Sun,Georgia F Papadaki,Christine A. Devlin,Julia N Danon,Michael C. Young,Trenton J Winters,George M. Burslem,Erik Procko,Nikolaos G. Sgourakis +8 more
TL;DR: In this article , a chicken TAPBPR ortholog was found to recognize empty MHC-I with broader allele specificity and facilitate peptide exchange by maintaining a reservoir of receptive molecules.
Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes
Yi Sun,Georgia F Papadaki,Christine A. Devlin,Julia N Danon,Michael Young,Trenton J Winters,George Burslem,Erik Procko,Nikolaos Sgourakis +8 more
TL;DR: TAPBPR facilitates antigenic peptide optimization and quality control of MHC-I, but its efficacy is restricted to a limited set of HLA allotypes due to allelic dependency on chaperones for assembly and epitope selection.
Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules
Georgia Papadaki,Omar Al Ani,Tyler J. Florio,Michael C. Young,Julia N Danon,Yi Sun,Devin Dersh,Nikolaos G. Sgourakis +7 more
TL;DR: In this paper , a fixed-backbone computational design approach for engineering synthetic molecules that combine peptide binding and TCR recognition surfaces from existing HLA allotypes is presented, which underscore a novel, structure-guided platform for developing synthetic HLA molecules with desired properties as screening probes for peptide-centric interactions with TCRs and other therapeutic modalities.
Universal open MHC-I molecules for rapid peptide loading and enhanced complex stability across HLA allotypes
Yi Sun,Michael C. Young,Claire H. Woodward,Julia N Danon,H. V. Truong,Sagar Gupta,Trenton J Winters,George M. Burslem,Nikolaos G. Sgourakis +8 more
TL;DR: In this article , a structure-guided approach for generating conformationally stable, open MHC-I molecules with enhanced ligand exchange kinetics spanning five HLAA, all HLA-B supertypes, and oligomorphic HLAIb allotypes was proposed.