Author
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
9 papers
Recent·Most cited
H. Jiang, K. M. Jude, K. Wu, J. Fallas, G. Ueda, T. Brunette, D. Hicks, H. Pyles, A. Yang, L. Carter, M. Lamb, X. Li, P. M. Levine, L. J. Stewart, K. C. Garcia, D. Baker
This paper designs proteins with structured loops supported by hydrogen bonds, demonstrating their stability and functionality in binding extended peptides.
bioRxiv · Aug 22, 2023 · PreprintBiochemistry
R. Mout, R. C. Bretherton, J. Decarreau, S. Lee, N. I. Edman, M. Ahlrichs, Y. Hsia, D. D. Sahtoe, G. Ueda, N. Gregorio, A. Sharma, R. Schulman, C. A. DeForest, D. Baker
This paper designs modular protein hydrogels with tunable viscoelasticity by controlling molecular parameters and demonstrates their use both intra- and extracellularly.
bioRxiv · Jun 2, 2023Bioengineering
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
E. C. Yang, R. Divine, M. C. Miranda, A. J. Borst, W. Sheffler, J. Z. Zhang, J. Decarreau, A. Sarajovi, M. Abedi, N. Goldbach, M. Ahlrichs, C. Dobbins, A. Hand, S. Cheng, M. Lamb, , D. Baker
This paper designs pH-responsive antibody nanoparticles with three distinct protein components that disassemble at tunable pH levels, enabling targeted delivery of biologics.
bioRxiv · Apr 17, 2023Bioengineering
R. Divine, H. V. Dang, G. Ueda, J. A. Fallas, I. Vulovic, W. Sheffler, S. Saini, Y. T. Zhao, I. X. Raj, P. A. Morawski, M. F. Jennewein, L. J. Homad, Y.-H. Wan, M. R. Tooley, F. Seeger, , D. Baker
The paper designs modular nanocages that assemble antibodies into precise geometries, enhancing signaling and neutralization compared to free antibodies.
bioRxiv · Dec 1, 2020Biochemistry
Y. T. Zhao, J. A. Fallas, S. Saini, G. Ueda, L. Somasundaram, Z. Zhou, I. Xavier, D. Ehnes, C. Xu, L. Carter, S. Wrenn, J. Mathieu, D. L. Sellers, D. Baker, H. Ruohola-Baker
The paper investigates how the valency of F-domain scaffolds affects signaling through the angiopoietin pathway, finding that higher valency mimics Ang1's pro-angiogenic effects while lower valency mimics Ang2's antagonistic effects.
bioRxiv · Sep 19, 2020Biochemistry
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
J. T. Martin, C. T. Cottrell, A. Antanasijevic, D. G. Carnathan, B. J. Cossette, C. A. Enemuo, E. H. Gebru, Y. Choe, F. Viviano, T. Tokatlian, K. M. Cirelli, G. Ueda, J. Copps, T. Schiffner, S. Menis, , D. J. Irvine
This study shows that HIV Env immunogens can be concentrated in B cell follicles using immune complexes or protein nanoparticles, enhancing their localization in lymph nodes and potentially improving immune responses.
bioRxiv · Feb 19, 2020Immunology
A. Antanasijevic, G. Ueda, J. Copps, P. J. Brouwer, D. Huang, J. D. Allen, C. A. Cottrell, A. Yasmeen, L. M. Sewall, I. Bontjer, T. J. Ketas, H. L. Turner, Z. T. Berndsen, P. J. Klasse, M. Crispin, , A. B. Ward
The paper evaluates de novo-designed two-component nanoparticles for presenting HIV Env trimers, showing improved antibody responses through multivalent display.
bioRxiv · Jan 31, 2020Immunology