@article{raghuvanshi_zhu_ramezani_menegatti_santiso_mason_rodgers_janka_abolhasani_2020, title={Highly Efficient 1-Octene Hydroformylation at Low Syngas Pressure: From Single-Droplet Screening to Continuous Flow Synthesis}, volume={10}, ISSN={["2155-5435"]}, DOI={10.1021/acscatal.0c01515}, abstractNote={We present a reconfigurable flow chemistry strategy for facile transition between accelerated screening and continuous synthesis of linear aldehydes through homogeneous rhodium-catalyzed hydroformy...}, number={14}, journal={ACS CATALYSIS}, author={Raghuvanshi, Keshav and Zhu, Cheng and Ramezani, Mahdi and Menegatti, Stefano and Santiso, Erik E. and Mason, Dawn and Rodgers, Jody and Janka, Mesfin E. and Abolhasani, Milad}, year={2020}, month={Jul}, pages={7535–7542} } @article{zhu_dukhovlinova_council_ping_faison_prabhu_potter_upton_yin_fay_et al._2019, title={Rationally designed carbohydrate-occluded epitopes elicit HIV-1 Env-specific antibodies}, volume={10}, ISSN={["2041-1723"]}, DOI={10.1038/s41467-019-08876-w}, abstractNote={AbstractAn array of carbohydrates masks the HIV-1 surface protein Env, contributing to the evasion of humoral immunity. In most HIV-1 isolates ‘glycan holes’ occur due to natural sequence variation, potentially revealing the underlying protein surface to the immune system. Here we computationally design epitopes that mimic such surface features (carbohydrate-occluded neutralization epitopes or CONE) of Env through ‘epitope transplantation’, in which the target region is presented on a carrier protein scaffold with preserved structural properties. Scaffolds displaying the four CONEs are examined for structure and immunogenicity. Crystal structures of two designed proteins reflect the computational models and accurately mimic the native conformations of CONEs. The sera from rabbits immunized with several CONE immunogens display Env binding activity. Our method determines essential structural elements for targets of protective antibodies. The ability to design immunogens with high mimicry to viral proteins also makes possible the exploration of new templates for vaccine development.}, journal={NATURE COMMUNICATIONS}, author={Zhu, Cheng and Dukhovlinova, Elena and Council, Olivia and Ping, Lihua and Faison, Edgar M. and Prabhu, Shamit S. and Potter, E. Lake and Upton, Stephen L. and Yin, Guowei and Fay, James M. and et al.}, year={2019}, month={Feb} } @article{zhu_raghuvanshi_coley_mason_rodgers_janka_abolhasani_2018, title={Flow chemistry-enabled studies of rhodium-catalyzed hydroformylation reactions}, volume={54}, ISSN={["1364-548X"]}, url={https://doi.org/10.1039/C8CC04650F}, DOI={10.1039/c8cc04650f}, abstractNote={We present an autonomous microscale flow chemistry platform for high-throughput fundamental and applied studies of homogeneous hydroformylation reactions.}, number={62}, journal={CHEMICAL COMMUNICATIONS}, publisher={Royal Society of Chemistry (RSC)}, author={Zhu, Cheng and Raghuvanshi, Keshav and Coley, Connor W. and Mason, Dawn and Rodgers, Jody and Janka, Mesfin E. and Abolhasani, Milad}, year={2018}, month={Aug}, pages={8567–8570} }