Author

Y.-J. Park

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

Biology Disciplines

Click to filter author papers

Biochemistry· 8 Immunology· 7 Microbiology· 7 Bioengineering· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 21 Research Focus:host-pathogen & immune response· 16 Organism:human· 8 Assay:structural biology· 6 Research Focus:drug response / drug discovery· 5 Organism:mouse· 5 Assay:proteomics· 5 Assay:protein structure· 4

Frequent Co-Authors

D. Veesler· 17 shared A. C. Walls· 8 shared D. Corti· 7 shared J. E. Bowen· 6 shared M. A. Tortorici· 6 shared C. Stewart· 5 shared D. Pinto· 5 shared N. P. King· 5 shared

Activity by Year

2020-2024 · peak 9/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

17 shared papersBiochemistry

D. Veesler

Mutual co-authors in cluster

Author profile →

23 papers

Recent·Most cited

Human coronavirus HKU1 recognition of the TMPRSS2 host receptor

M. McCallum, Y.-J. Park, C. Stewart, K. R. Sprouse, J. Brown, M. A. Tortorici, C. Gibson, E. Wong, M. Ieven, A. Telenti, D. Veesler

This study determines the structure of HKU1 spike RBD bound to TMPRSS2, identifies host receptor usage determinants, and shows the role of antibodies and glycan shielding in neutralization.

Cell · Aug 1, 2024Peer-reviewedBiochemistry

A broadly generalizable stabilization strategy for sarbecovirus fusion machinery vaccines

J. Lee, C. Stewart, A. Schaefer, E. M. Leaf, Y.-J. Park, D. Asarnow, J. M. Powers, C. Treichel, D. Corti, R. Baric, N. P. King, D. Veesler

This paper develops a stabilization strategy for sarbecovirus fusion machinery vaccines, showing broad reactivity and protection against SARS-CoV-2 variants.

bioRxiv · Dec 12, 2023Biochemistry

Umbrella toxin particles produced by Streptomyces block mycelial growth of competing species

Q. Zhao, S. Bertolli, Y.-J. Park, Y. Tan, K. J. Cutler, P. Srinivas, K. L. Asfahl, C. Fonseca Garcia, L. A. Gallagher, Y. Li, Y. Wang, D. Coleman-Derr, F. DiMaio, D. Zhang, S. B. Peterson, , J. D. Mougous

This study identifies umbrella toxin particles produced by Streptomyces that inhibit the growth of competing bacterial species, distinct from small molecule antibiotics.

bioRxiv · Dec 9, 2023 · PreprintMicrobiology

Multiple independent acquisitions of ACE2 usage in MERS-related coronaviruses

C.-B. Ma, C. Liu, Y.-J. Park, J. Tang, J. Chen, Q. Xiong, J. Lee, C. Stewart, D. Asarnow, J. Brown, M. A. Tortorici, X. Yang, Y.-H. Sun, Y.-M. Chen, X. Yu, , H. Yan

The paper identifies two European bat MERS-related coronaviruses that use ACE2 as their receptor, revealing a distinct binding mode and host tropism determinants.

bioRxiv · Oct 2, 2023Microbiology

Broad receptor tropism and immunogenicity of a clade 3 sarbecovirus

J. Lee, S. Zepeda, Y.-J. Park, A. L. Taylor, J. Quispe, C. Stewart, E. M. Leaf, C. Treichel, D. Corti, N. P. King, T. N. Starr, D. Veesler

This study characterizes the receptor tropism and antigenicity of a clade 3 sarbecovirus, identifying broad ACE2 usage and cross-neutralizing antibodies with implications for vaccine design.

bioRxiv · Sep 12, 2023Biochemistry

Structure and design of Langya virus glycoprotein antigens

Z. Wang, M. McCallum, L. Yan, W. Sharkey, Y.-J. Park, H. V. Dang, M. Amaya, A. Person, C. C. Broder, D. J. Veesler

The paper determines the structure of Langya virus glycoproteins and shows they use a different receptor than NiV and HeV, with no cross-reactivity of antibodies.

bioRxiv · Aug 20, 2023Biochemistry

Hierarchical design of pseudosymmetric protein nanoparticles

Q. Dowling, Y.-J. Park, N. Gerstenmaier, E. Yang, A. Wargacki, Y. Hsia, C. Fries, R. Ravichandran, C. Walkey, A. Burrell, D. Veesler, D. Baker, N. King

The paper designs large pseudosymmetric protein nanoparticles using a hierarchical computational method, achieving sizes up to 96 nm with 960 subunits.

bioRxiv · Jun 16, 2023 · PreprintBioengineering

Antigen spacing on protein nanoparticles influences antibody responses to vaccination

D. Ellis, A. Dosey, S. Boyoglu-Barnum, Y.-J. Park, R. Gillespie, H. Syeda, Y. Tsybovsky, M. Murphy, D. Pettie, N. Matheson, S. Chan, G. Ueda, J. Fallas, L. Carter, B. Graham, , N. P. King

This study shows that antigen spacing on protein nanoparticles affects antibody responses to vaccination, with decreased spacing improving hemagglutination inhibition and neutralization potency.

bioRxiv · May 23, 2023Immunology

Therapeutic and vaccine-induced cross-reactive antibodies with effector function against emerging Omicron variants

A. Addetia, L. Piccoli, J. B. Case, Y.-J. Park, M. Beltramello, B. Guarino, H. Dang, D. Pinto, S. Scheaffer, K. Sprouse, J. Bassi, C. Silacci-Fregni, F. Muoio, M. Dini, L. Vincenzetti, , Fran

The paper shows that cross-reactive antibodies, like S309, retain effector functions against emerging Omicron variants despite reduced neutralization.

bioRxiv · Jan 17, 2023 · PreprintImmunology

MARCH5-dependent NLRP3 ubiquitination is an essential step for NEK7 docking on the mitochondria

Y.-J. Park, N. Dodantenna, T.-H. Kim, H.-S. Lee, Y.-S. Yoo, E.-S. Lee, J.-H. Lee, M.-H. Kwon, H. C. Kang, J.-S. Lee, H. Cho

This study identifies MARCH5-dependent NLRP3 ubiquitination as essential for NEK7 mitochondrial docking during inflammasome assembly.

bioRxiv · Jan 12, 2023 · PreprintImmunology

Imprinted antibody responses against SARS-CoV-2 Omicron sublineages

Y.-J. Park, D. Pinto, A. C. Walls, Z. Liu, A. De Marco, F. Benigni, F. Zatta, C. Silacci-Fregni, J. Bassi, K. R. Sprouse, A. Addetia, J. E. Bowen, C. Stewart, M. Giurdanella, C. Saliba, , Piccoli

This study shows that hybrid immunity and vaccine boosters provide potent neutralizing activity against Omicron BA.1 and BA.2, while breakthrough infections induce nasal mucosal neutralization and identify an ultrapotent pan-variant antibody.

bioRxiv · May 8, 2022Immunology

Structural changes in the SARS-CoV-2 spike E406W mutant escaping a clinical monoclonal antibody cocktail

A. Addetia, Y.-J. Park, T. Starr, A. J. Greaney, K. Sprouse, J. E. Bowen, S. W. Tiles, W. C. Van Voorhis, J. D. Bloom, D. Corti, A. C. Walls, D. Veesler

The paper examines structural changes in the SARS-CoV-2 spike E406W mutant that reduce neutralization by a monoclonal antibody cocktail and alters epitope recognition.

bioRxiv · Jan 21, 2022Biochemistry

Structure, receptor recognition and antigenicity of the human coronavirus CCoV-HuPn-2018 spike glycoprotein

M. A. Tortorici, A. C. Walls, A. Joshi, Y.-J. Park, R. T. Eguia, T. Stevens-Ayers, M. J. Boeckh, A. Talenti, A. Lanzavecchia, D. Corti, J. D. Bloom, D. Veesler

The paper determines the structure of the CCoV-HuPn-2018 spike glycoprotein, identifies its receptor, and shows cross-neutralizing antibodies against related coronaviruses.

bioRxiv · Oct 25, 2021Microbiology

Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry

Y.-J. Park, A. De Marco, T. N. Starr, Z. Liu, D. Pinto, A. C. Walls, F. Zatta, S. K. Zepeda, J. E. Bowen, K. S. Sprouse, A. Joshi, M. Giurdanella, B. Guarino, J. Noack, R. Abdelnabi, , D. Veesler

This study identifies a broadly neutralizing antibody against sarbecoviruses that targets the ACE2 binding site and shows high resistance to escape mutations.

bioRxiv · Oct 13, 2021Immunology

Structure-based design of stabilized recombinant influenza neuraminidase tetramers

D. Ellis, J. Lederhofer, O. J. Acton, Y. Tsybovsky, S. Kephart, C. Yap, R. A. Gillespie, A. Creanga, T. Stephens, D. Pettie, M. Murphy, A. J. Borst, Y.-J. Park, K. K. Lee, B. S. Graham, , M. Kanekiyo

This study designs stabilized recombinant influenza neuraminidase tetramers by uncovering structural principles and improving thermal stability and antibody affinity.

bioRxiv · May 17, 2021Microbiology

Antibodies to the SARS-CoV-2 receptor-binding domain that maximize breadth and resistance to viral escape

T. N. Starr, N. Czudnochowski, F. Zatta, Y.-J. Park, Z. Liu, A. Addetia, D. Pinto, M. Beltramello, P. Hernandez, A. J. Greaney, R. Marzi, W. G. Glass, I. Zhang, A. S. Dingens, J. E. Bowen, , Veesler

This study identifies antibodies against SARS-CoV-2 that balance neutralization potency and breadth, with some showing high resistance to viral escape.

bioRxiv · Apr 6, 2021 · PreprintMicrobiology

Membrane lectins enhance SARS-CoV-2 infection and influence the neutralizing activity of different classes of antibodies

F. A. Lempp, L. Soriaga, M. Montiel-Ruiz, F. Benigni, J. Noack, Y.-J. Park, S. Bianchi, A. C. Walls, J. E. Bowen, J. Zhou, H. Kaiser, M. Agostini, M. Meury, E. Dellota, S. Jaconi, , D. Corti

This study identifies membrane lectins that enhance SARS-CoV-2 infection and show how different antibodies neutralize infection through distinct mechanisms.

bioRxiv · Apr 3, 2021 · PreprintMicrobiology

Structural basis for broad coronavirus neutralization

M. Sauer, Y.-J. Park, M. A. Tortorici, A. C. Walls, L. Homad, O. Acton, J. E. Bowen, C. Wang, X. Xiong, W. de van der Schueren, J. Quispe, B.-J. Bosch, B. G. Hoffstrom, A. T. McGuire, D. Veesler

This study identifies a monoclonal antibody that broadly neutralizes multiple beta-coronaviruses by targeting a conserved epitope, providing a structural basis for designing pan-coronavirus vaccines.

bioRxiv · Dec 29, 2020Biochemistry

Hierarchical design of multi-scale protein complexes by combinatorial assembly of oligomeric helical bundle and repeat protein building blocks

Y. Hsia, R. Mout, W. Sheffler, N. I. Edman, I. Vulovic, Y.-J. Park, R. L. Redler, M. J. Bick, A. K. Bera, A. Courbet, A. Kang, T. Brunette, U. Nattermann, E. Tsai, A. Saleem, , D. Baker

This paper describes a hierarchical method to design multi-scale symmetric protein complexes using repeat proteins and helical bundles, resulting in large symmetric assemblies like an icosahedral nanocage.

bioRxiv · Jul 27, 2020Biochemistry

Elicitation of broadly protective immunity to influenza by multivalent hemagglutinin nanoparticle vaccines

S. Boyoglu-Barnum, D. Ellis, R. A. Gillespie, G. B. Hutchinson, Y.-J. Park, S. M. Moin, O. Acton, R. Ravichandran, M. Murphy, D. Pettie, N. Matheson, L. Carter, A. Creanga, M. J. Watson, S. Kephart, , M. Kanekiyo

Nanoparticle immunogens with four seasonal influenza hemagglutinins elicit neutralizing antibodies against both the head and stem, providing broad protection against diverse influenza strains.

bioRxiv · May 30, 2020 · PreprintImmunology

Structural and functional analysis of a potent sarbecovirus neutralizing antibody

D. Pinto, Y.-J. Park, M. Beltramello, A. C. Walls, M. A. Tortorici, S. Bianchi, S. Jaconi, K. Culap, F. Zatta, A. De Marco, A. Peter, B. Guarino, R. Spreafico, E. Cameroni, J. B. Case, , D. Corti

This study identifies and characterizes a potent neutralizing antibody, S309, against SARS-CoV-2 and related sarbecoviruses, showing its efficacy in preventing viral entry and potential for therapeutic use.

bioRxiv · Apr 7, 2020Immunology

Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein

A. C. Walls, Y.-J. Park, M. A. Tortorici, A. Wall, A. T. McGuire, D. Veesler

This study characterizes the structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein, showing its receptor-binding properties, furin cleavage site, and potential for cross-neutralizing antibodies.

bioRxiv · Feb 19, 2020Biochemistry

Although host-related factors are important for the formation of gut microbiota, environmental factors cannot be ignored

Y. Jung, D. Kerfahi, H. Q. Pham, H. Son, J. C. Ibal, M.-K. Park, Y.-J. Park, C. E. Park, S.-D. Choi, Y. Jo, M.-C. Kim, M. J. Kim, G. U. Kang, H. W. Jo, H. Yun, , J.-H. Shin

This study compares host-related factors and environmental factors in shaping gut microbiota using fecal samples from naval trainees and healthy individuals, finding host factors more influential.

bioRxiv · Feb 3, 2020 · PreprintMicrobiology