{"id":2,"date":"2017-12-06T13:06:04","date_gmt":"2017-12-06T13:06:04","guid":{"rendered":"http:\/\/sites.rutgers.edu\/department-of-example\/?page_id=2"},"modified":"2026-08-31T15:05:40","modified_gmt":"2026-08-31T15:05:40","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.rutgers.edu\/schuster-lab\/publications\/","title":{"rendered":"Publications"},"content":{"rendered":"

2026<\/h2>\n
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Barai, M., Chuang, E., Weng, S.-L., Mittal, J., Driscoll, M., & Schuster, B. S. (2026). Condensate material properties influence cargo selection for neuronal extrusion via large extracellular exopher vesicles<\/i>. https:\/\/doi.org\/10.64898\/2026.08.17.745362<\/a><\/div>\n

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Wake, N., Alcalde, J., Jutzi, D., Bajaj, A., Kour, S., Barai, M., Weng, S.-L., Cummings, S., Zheng, T., Anderson, E. N., Wang, S.-H., Puterbaugh, R., Bosco, D. A., Schuster, B. S., Mittal, J., Pandey, U. B., Ruepp, M.-D., & Fawzi, N. L. (2026). Breaking \u03b2-sheets in FUS prion-like domain preserves phase separation and function but prevents aggregation and toxicity<\/i>. https:\/\/doi.org\/10.64898\/2026.02.17.706410<\/a><\/div>\n

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Wang, H., Favetta, B., Wang, J., Hoffmann, C., Maloku, E., Xia, Y., Baum, J., Milovanovic, D., Schuster, B. S., & Shi, Z. (2026). Biomolecular condensates provide a unique environment for redox-mediated protein crosslinking<\/i>. https:\/\/doi.org\/10.64898\/2026.04.14.718453<\/a><\/div>\n

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Mulay, P. B., Radford, D. C., Rondon, B., Favetta, B., Schuster, B. S., Niu, J., & Gormley, A. J. (2026). Gene delivery mediated by backbone-degradable RAFT copolymers. Biomacromolecules<\/i>, 27<\/i>(3), 1846\u20131856. https:\/\/doi.org\/10.1021\/acs.biomac.5c01662<\/a><\/div>\n

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Schuster, B. S. (2026). Putting protein \u201cmembranes\u201d on membrane-less organelles. Biophysical Journal<\/i>, 125<\/i>(3), 679\u2013681. https:\/\/doi.org\/10.1016\/j.bpj.2025.12.018<\/a><\/div>\n

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2025<\/h2>\n
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Park, A. S., Ding, E. A., & Schuster, B. S. (2025). POMPOMS: Crosslinked biomolecular condensates as a versatile platform for multifunctional protein microparticles. Biomacromolecules<\/i>, 26<\/i>(11), 7605\u20137620. https:\/\/doi.org\/10.1021\/acs.biomac.5c01130<\/a><\/div>\n

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Favetta, B., Wang, H., Cubuk, J., Singh, A., Barai, M., Ramirez, C., Zheng, H., Gormley, A. J., Murthy, N. S., Dignon, G., Soranno, A., Shi, Z., & Schuster, B. S. (2025). Phosphorylation toggles the SARS-CoV-2 nucleocapsid protein between two membrane-associated condensate states. Nature Communications<\/i>, 16<\/i>(1), 7970. https:\/\/doi.org\/10.1038\/s41467-025-62922-4<\/a><\/div>\n

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Favetta, B., Wang, H., Shi, Z., & Schuster, B. S. (2025). Amphiphilic protein surfactants reduce the interfacial tension of biomolecular condensates. Langmuir<\/i>, 41<\/i>(35), 23827\u201323836. https:\/\/doi.org\/10.1021\/acs.langmuir.5c03118<\/a><\/p>\n<\/div>\n<\/div>\n<\/div>\n

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Kelley, F. M., Ani, A., Pinlac, E. G., Linders, B., Favetta, B., Barai, M., Ma, Y., Singh, A., Dignon, G. L., Gu, Y., & Schuster, B. S. (2025). Controlled and orthogonal partitioning of large particles into biomolecular condensates. Nature Communications<\/i>, 16<\/i>(1), 3521. https:\/\/doi.org\/10.1038\/s41467-025-58900-5<\/a><\/div>\n

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2024<\/h2>\n
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Rizvi, A., Favetta, B., Jaber, N., Lee, Y.-K., Jiang, J., Idris, N. S., Schuster, B. S., Dai, W., & Patterson, J. P. (2024). Revealing nanoscale structure and interfaces of protein and polymer condensates via<\/i> cryo-electron microscopy. Nanoscale<\/i>, 16<\/i>(35), 16706\u201316717. https:\/\/doi.org\/10.1039\/D4NR01877J<\/a><\/div>\n

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Li, X., Kuchinski, L. M., Park, A., Murphy, G. S., Soto, K. C., & Schuster, B. S. (2024). Enzyme purification and sustained enzyme activity for pharmaceutical biocatalysis by fusion with phase\u2010separating intrinsically disordered protein. Biotechnology and Bioengineering<\/i>, 121<\/i>(10), 3155\u20133168. https:\/\/doi.org\/10.1002\/bit.28787<\/a><\/div>\n

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Rekhi, S., Garcia, C. G., Barai, M., Rizuan, A., Schuster, B. S., Kiick, K. L., & Mittal, J. (2024). Expanding the molecular language of protein liquid\u2013liquid phase separation. Nature Chemistry<\/i>, 16<\/i>(7), 1113\u20131124. https:\/\/doi.org\/10.1038\/s41557-024-01489-x<\/a><\/div>\n

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2021<\/h2>\n
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Kelley, F. M., Favetta, B., Regy, R. M., Mittal, J., & Schuster, B. S. (2021). Amphiphilic proteins coassemble into multiphasic condensates and act as biomolecular surfactants. Proceedings of the National Academy of Sciences<\/i>, 118<\/i>(51), e2109967118. https:\/\/doi.org\/10.1073\/pnas.2109967118<\/a><\/div>\n

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Garabedian, M. V., Wang, W., Dabdoub, J. B., Tong, M., Caldwell, R. M., Benman, W., Schuster, B. S., Deiters, A., & Good, M. C. (2021). Designer membraneless organelles sequester native factors for control of cell behavior. Nature Chemical Biology<\/i>, 17<\/i>(9), 998\u20131007. https:\/\/doi.org\/10.1038\/s41589-021-00840-4<\/a><\/div>\n

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Wang, H., Kelley, F. M., Milovanovic, D., Schuster, B. S., & Shi, Z. (2021). Surface tension and viscosity of protein condensates quantified by micropipette aspiration. Biophysical Reports<\/i>, 1<\/i>(1), 100011. https:\/\/doi.org\/10.1016\/j.bpr.2021.100011<\/a><\/div>\n

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Schuster, B. S., Regy, R. M., Dolan, E. M., Kanchi Ranganath, A., Jovic, N., Khare, S. D., Shi, Z., & Mittal, J. (2021). Biomolecular condensates: Sequence determinants of phase separation, microstructural organization, enzymatic activity, and material properties. The Journal of Physical Chemistry B<\/i>, 125<\/i>(14), 3441\u20133451. https:\/\/doi.org\/10.1021\/acs.jpcb.0c11606<\/a><\/div>\n

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2020<\/h2>\n
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Schuster, B. S., Dignon, G. L., Tang, W. S., Kelley, F. M., Ranganath, A. K., Jahnke, C. N., Simpkins, A. G., Regy, R. M., Hammer, D. A., Good, M. C., & Mittal, J. (2020). Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior. Proceedings of the National Academy of Sciences<\/i>, 117<\/i>(21), 11421\u201311431. https:\/\/doi.org\/10.1073\/pnas.2000223117<\/a><\/p>\n<\/div>\n
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Reed, E. H., Schuster, B. S., Good, M. C., & Hammer, D. A. (2020). SPLIT: Stable protein coacervation using a light induced transition. ACS Synthetic Biology<\/i>, 9<\/i>(3), 500\u2013507. https:\/\/doi.org\/10.1021\/acssynbio.9b00503
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Before Schuster Lab Founding<\/h1>\n

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Schuster BS, Reed EH, Parthasarathy R, Janke CN, Caldwell RM, Bermudez JG, Ramage H, Good MC, Hammer DA. Controllable protein phase separation and modular recruitment to form responsive, membraneless organelles. Nature Communications 2018; 9(1):2985.\u00a0https:\/\/doi.org\/10.1038\/s41467-018-05403-1<\/a><\/p>\n

Glantz ST, Berlew EE, Jaber Z, Schuster BS, Gardner KH, Chow BY. Directly light-activated binding of RGS-LOV photoreceptors to anionic membrane phospholipids. PNAS 115(33):E7720-E7727.<\/p>\n

Caldwell RM, Bermudez JG, Thai D, Aonbangkhen C, Schuster BS, Courtney T, Deiters A, Hammer DA, Chenoweth DM, Good MC. Optochemical control of protein localization and activity within cell-like compartments. Biochemistry 2018; 57:2590-2596.<\/p>\n

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Schuster BS, Allan DB, Kays JC, Hanes J, Leheny R. Photoactivatable fluorescent probes reveal heterogeneous nanoparticle permeation through biological gels at multiple scales. Journal of Controlled Release 2017; 260:124-133.<\/p>\n

Schneider CS, Xu Q, Boylan NJ, Chisholm J, Tang B, Schuster BS, Henning A, Ensign LM, Lee E, Adstamongkonkul P, Simons BW, Wang SS, Gong X, Yu T, Boyle MP, Suk JS, and Hanes J. Nanoparticles that do not adhere to mucus provide uniform and long-lasting drug delivery to airways following inhalation. Science Advances 2017; 3(4):e1601556.<\/p>\n

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Chu KK, Mojahed D, Fernandez CM, Li Y, Liu L, Wilsterman EJ, Diephuis B, Birket SE, Bowers H, Martin Solomon G, Schuster BS, Hanes J, Rowe SM, Tearney GJ. Particle-tracking microrheology using micro-optical coherence tomography. Biophysical Journal 2016; 111:1053-63.<\/p>\n

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Schuster BS, Ensign LM, Allan DB, Suk JS, Hanes J. Particle tracking in drug and gene delivery research: state-of-the-art applications and methods. Advanced Drug Delivery Reviews 2015; 91:70-91.<\/p>\n

Yu T, Chan KW, Anonuevo A, Song X, Schuster BS, Chattopadhyay S, Xu Q, Oskolkov N, Patel H, Ensign LM, van Zjil PC, McMahon MT, Hanes J. Liposome-based mucus-penetrating particles (MPP) for mucosal theranostics: demonstration of diamagnetic chemical exchange saturation transfer (diaCEST) magnetic resonance imaging (MRI). Nanomedicine 2015; 11:401-5.<\/p>\n

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Nance E, Zhang C, Shih TY, Xu Q, Schuster BS, Hanes J. Brain-penetrating nanoparticles improve paclitaxel efficacy in malignant glioma following local administration. ACS Nano 2014; 8:10655-64.<\/p>\n

Birket SE, Chu KK, Liu L, Houser GH, Diephuis BJ, Wilsterman EJ, Dierksen G, Mazur M, Shastry S, Li Y, Watson JD, Smith AT, Schuster BS, Hanes J, Grizzle WE, Sorscher EJ, Tearney GJ, Rowe SM. A functional anatomic defect of the cystic fibrosis airway. Am J Respir Crit Care Med 2014; 190:421-32.<\/p>\n

Schuster BS, Kim AJ, Kays JC, Kanzawa MM, Guggino WB, Boyle MP, Rowe SM, Muzyczka N, Suk JS, Hanes J. Overcoming the cystic fibrosis sputum barrier to leading adeno-associated virus gene therapy vectors. Molecular Therapy 2014; 22:14841493.<\/p>\n

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Kim AJ, Boylan NJ, Suk JS, Hwangbo M, Yu T, Schuster BS, Cebotaru L, Lesniak WG, Oh JS, Adstamongkonkul P, Choi AY, Kannan RM, Hanes J. Use of single-site-functionalized PEG dendrons to prepare gene vectors that penetrate human mucus barriers. Angew Chem Int Ed 2013; 52:3985-8.<\/p>\n

Schuster BS, Suk JS, Woodworth GF, Hanes J. Nanoparticle diffusion in respiratory mucus from humans without lung disease. Biomaterials 2013; 34:3439-46.<\/p>\n

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Langham AA, Khandelia H, Schuster B, Waring AJ, Lehrer RI, Kaznessis YN. Correlation between simulated physicochemical properties and hemolycity of protegrin-like antimicrobial peptides: predicting experimental toxicity. Peptides 2008; 29:1085-93.<\/p>\n","protected":false},"excerpt":{"rendered":"

2026 Barai, M., Chuang, E., Weng, S.-L., Mittal, J., Driscoll, M., & Schuster, B. S. (2026). 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