Jingjia Liu

ORCID: 0000-0002-6038-593X
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About
Contact & Profiles
Research Areas
  • Immunotherapy and Immune Responses
  • vaccines and immunoinformatics approaches
  • Monoclonal and Polyclonal Antibodies Research
  • Enzyme Structure and Function
  • T-cell and B-cell Immunology
  • Antimicrobial Peptides and Activities
  • Glycosylation and Glycoproteins Research
  • Peptidase Inhibition and Analysis
  • Protein purification and stability
  • Protein Structure and Dynamics

Bioengineering Center
2024

Stanford University
2022-2024

Nanobodies bind a target antigen with kinetic profile similar to conventional antibody, but exist as single heavy chain domain that can be readily multimerized engage via multiple interactions. Presently, most nanobodies are produced by immunizing camelids; however, platforms for animal-free production growing in popularity. Here, we describe the development of fully synthetic nanobody library based on an engineered human V

10.1073/pnas.2216612120 article EN cc-by Proceedings of the National Academy of Sciences 2023-06-05

The ability to finely control the structure of protein folds is an important prerequisite functional design. TIM barrel fold target for these efforts as it highly enriched diverse functions in nature. Although a has been designed de novo, alter curvature central beta and overall architecture remains elusive, limiting its utility Here, we report novo design with ovoid (twofold) symmetry, drawing inspiration from natural barrels curvature. We use autoregressive backbone sampling strategy...

10.34133/2022/9842315 article EN cc-by BioDesign Research 2022-01-01

Class-II major histocompatibility complexes (MHC-IIs) are central to the communications between CD4+ T cells and antigen presenting (APCs), but intrinsic structural features associated with MHC-II make it difficult develop a general targeting system high affinity specificity. Here, we introduce protein platform, Targeted Recognition of Antigen-MHC Complex Reporter for (

10.1101/2024.01.26.577489 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-01-30

Identifying highly specific T cell receptors (TCRs) or antibodies against epitopic peptides presented by class I major histocompatibility complex (MHC I) proteins remains a bottleneck in the development of targeted therapeutics. Here, we introduce recognition antigen–MHC reporter for MHC (TRACeR-I), generalizable platform targeting on polymorphic HLA-A*, HLA-B* and HLA-C* allotypes while overcoming cross-reactivity challenges TCRs. Our TRACeR–MHC co-crystal structure reveals unique antigen...

10.1038/s41587-024-02505-8 article EN cc-by-nc-nd Nature Biotechnology 2024-12-13
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