@article{kim_van den broeck_karre_choi_christensen_wang_jo_cho_balint‐kurti_2021, title={Analysis of the transcriptomic, metabolomic, and gene regulatory responses to
            <i>Puccinia sorghi
            in maize}, volume={22}, ISSN={1464-6722 1364-3703}, url={http://dx.doi.org/10.1111/mpp.13040}, DOI={10.1111/mpp.13040}, abstractNote={Abstract}, number={4}, journal={Molecular Plant Pathology}, publisher={Wiley}, author={Kim, Saet‐Byul and Van den Broeck, Lisa and Karre, Shailesh and Choi, Hoseong and Christensen, Shawn A. and Wang, Guan‐Feng and Jo, Yeonhwa and Cho, Won Kyong and Balint‐Kurti, Peter}, year={2021}, month={Feb}, pages={465–479} }
 @article{garcía-lópez_chen_nilewski_duret_aliyan_kolomeisky_robinson_wang_pal_tour_2017, title={Molecular machines open cell membranes}, volume={548}, ISSN={0028-0836 1476-4687}, url={http://dx.doi.org/10.1038/NATURE23657}, DOI={10.1038/nature23657}, abstractNote={Beyond the more common chemical delivery strategies, several physical techniques are used to open the lipid bilayers of cellular membranes. These include using electric and magnetic fields, temperature, ultrasound or light to introduce compounds into cells, to release molecular species from cells or to selectively induce programmed cell death (apoptosis) or uncontrolled cell death (necrosis). More recently, molecular motors and switches that can change their conformation in a controlled manner in response to external stimuli have been used to produce mechanical actions on tissue for biomedical applications. Here we show that molecular machines can drill through cellular bilayers using their molecular-scale actuation, specifically nanomechanical action. Upon physical adsorption of the molecular motors onto lipid bilayers and subsequent activation of the motors using ultraviolet light, holes are drilled in the cell membranes. We designed molecular motors and complementary experimental protocols that use nanomechanical action to induce the diffusion of chemical species out of synthetic vesicles, to enhance the diffusion of traceable molecular machines into and within live cells, to induce necrosis and to introduce chemical species into live cells. We also show that, by using molecular machines that bear short peptide addends, nanomechanical action can selectively target specific cell-surface recognition sites. Beyond the in vitro applications demonstrated here, we expect that molecular machines could also be used in vivo, especially as their design progresses to allow two-photon, near-infrared and radio-frequency activation.}, number={7669}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={García-López, Víctor and Chen, Fang and Nilewski, Lizanne G. and Duret, Guillaume and Aliyan, Amir and Kolomeisky, Anatoly B. and Robinson, Jacob T. and Wang, Gufeng and Pal, Robert and Tour, James M.}, year={2017}, month={Aug}, pages={567–572} }
 @article{wang_balint-kurti_2016, title={Maize Homologs of CCoAOMT and HCT, Two Key Enzymes in Lignin Biosynthesis, Form Complexes with the NLR Rp1 Protein to Modulate the Defense Response}, volume={171}, ISSN={0032-0889 1532-2548}, url={http://dx.doi.org/10.1104/pp.16.00224}, DOI={10.1104/pp.16.00224}, abstractNote={Maize caffeoyl CoA O-methyltransferase and hydroxycinnamoyltransferase proteins, which are key enzymes in lignin biosynthesis, form a complex with NLR Rp1 protein to regulate the hypersensitive defense response. Disease resistance (R) genes encode nucleotide binding Leu-rich-repeat (NLR) proteins that confer resistance to specific pathogens. Upon pathogen recognition they trigger a defense response that usually includes a so-called hypersensitive response (HR), a rapid localized cell death at the site of pathogen infection. Intragenic recombination between two maize (Zea mays) NLRs, Rp1-D and Rp1-dp2, resulted in the formation of a hybrid NLR, Rp1-D21, which confers an autoactive HR in the absence of pathogen infection. From a previous quantitative trait loci and genome-wide association study, we identified genes encoding two key enzymes in lignin biosynthesis, hydroxycinnamoyltransferase (HCT) and caffeoyl CoA O-methyltransferase (CCoAOMT), adjacent to the nucleotide polymorphisms that were highly associated with variation in the severity of Rp1-D21-induced HR. We have previously shown that the two maize HCT homologs suppress the HR conferred by Rp1-D21 in a heterologous system, very likely through physical interaction. Here, we show, similarly, that CCoAOMT2 suppresses the HR induced by either the full-length or by the N-terminal coiled-coil domain of Rp1-D21 also likely via physical interaction and that the metabolic activity of CCoAOMT2 is unlikely to be necessary for its role in suppressing HR. We also demonstrate that CCoAOMT2, HCTs, and Rp1 proteins can form in the same complexes. A model is derived to explain the roles of CCoAOMT and HCT in Rp1-mediated defense resistance.}, number={3}, journal={Plant Physiology}, publisher={Oxford University Press (OUP)}, author={Wang, Guan-Feng and Balint-Kurti, Peter J.}, year={2016}, month={May}, pages={2166–2177} }
 @article{wang_balint-kurti_2015, title={Cytoplasmic and Nuclear Localizations Are Important for the Hypersensitive Response Conferred by Maize Autoactive Rp1-D21 Protein}, volume={28}, ISSN={["1943-7706"]}, url={http://www.scopus.com/inward/record.url?eid=2-s2.0-84942513115&partnerID=MN8TOARS}, DOI={10.1094/mpmi-01-15-0014-r}, abstractNote={ Disease resistance (R) genes have been isolated from many plant species. Most encode nucleotide binding leucine-rich repeat (NLR) proteins that trigger a rapid localized programmed cell death called the hypersensitive response (HR) upon pathogen recognition. Despite their structural similarities, different NLR are distributed in a range of subcellular locations, and analogous domains play diverse functional roles. The autoactive maize NLR gene Rp1-D21 derives from an intragenic recombination between two NLR genes, Rp1-D and Rp1-dp2, and confers a HR independent of the presence of a pathogen. Rp1-D21 and its N-terminal coiled coil (CC) domain (CCD21) confer autoactive HR when transiently expressed in Nicotiana benthamiana. Rp1-D21 was predominantly localized in cytoplasm with a small amount in the nucleus, while CCD21 was localized in both nucleus and cytoplasm. Targeting of Rp1-D21 or CCD21 predominantly to either the nucleus or the cytoplasm abolished HR-inducing activity. Coexpression of Rp1-D21 or CCD21 constructs confined, respectively, to the nucleus and cytoplasm did not rescue full activity, suggesting nucleocytoplasmic movement was important for HR induction. This work emphasizes the diverse structural and subcellular localization requirements for activity found among plant NLR R genes. }, number={9}, journal={MOLECULAR PLANT-MICROBE INTERACTIONS}, publisher={Scientific Societies}, author={Wang, Guan-Feng and Balint-Kurti, Peter J.}, year={2015}, month={Sep}, pages={1023–1031} }
 @article{wang_he_strauch_olukolu_nielsen_li_balint-kurti_2015, title={Maize homologs of hydroxycinnamoyltransferase, a key enzyme in lignin biosynthesis, bind the nucleotide binding leucine-rich repeat Rp1 proteins to modulate the defense response}, volume={169}, number={3}, journal={Plant Physiology}, author={Wang, G. F. and He, Y. J. and Strauch, R. and Olukolu, B. A. and Nielsen, D. and Li, X. and Balint-Kurti, P. J.}, year={2015}, pages={2230–2243} }
 @article{wang_ji_ei-kasmi_dangl_johal_balint-kurti_2015, title={Molecular and functional analyses of a maize autoactive NB-LRR protein identify precise structural requirements for activity}, volume={11}, number={2}, journal={PLoS Pathogens}, author={Wang, G. F. and Ji, J. B. and Ei-Kasmi, F. and Dangl, J. L. and Johal, G. and Balint-Kurti, P. J.}, year={2015} }
 @article{negeri_wang_benavente_kibiti_chaikam_johal_balint-kurti_2013, title={Characterization of temperature and light effects on the defense response phenotypes associated with the maize Rp1-D21 autoactive resistance gene}, volume={13}, journal={BMC Plant Biology}, author={Negeri, A. and Wang, G. F. and Benavente, L. and Kibiti, C. M. and Chaikam, V. and Johal, G. and Balint-Kurti, P.}, year={2013} }