Publications

  • Than, N. G., Romero, R., Fitzgerald, W., Gudicha, D. W., Gomez-Lopez, N., Posta, M., Zhou, F., Bhatti, G., Meyyazhagan, A., Awonuga, A. O., Chaiworapongsa, T., Matthies, D., Bryant, D. R., Erez, O., Margolis, L., & Tarca, A. L. (2024). Proteomic profiles of maternal plasma extracellular vesicles for prediction of preeclampsia. American Journal of Reproductive Immunology (New York, N.Y. : 1989), 92(4), e13928. PMID: 39347565
  • Vanpouille, C., Brichacek, B., Pushkarsky, T., Dubrovsky, L., Fitzgerald, W., Mukhamedova, N., Garcia-Hernandez, S., Matthies, D., Popratiloff, A., Sviridov, D., Margolis, L., & Bukrinsky, M. (2024). HIV-1 Nef is carried on the surface of extracellular vesicles. Journal of Extracellular Vesicles, 13(7), e12478. PMID: 39016173
  • Zeinert, R., Zhou, F., Franco, P. H. C., Zoeller, J., Lessen, H., Aravind, L., Langer, J., Sodt, A. J., Storz, G., & Matthies, D. (2024). Magnesium transporter MgtA revealed as a dimeric P-type ATPase. bioRxiv, March 1. Preprint article.  https://doi.org/10.1101/2024.02.28.582502 external link
  • Moller, E., Britt, M., Zhou, F., Yang, H., Anishkin, A., Ernst, R. K., Sukharev, S. I., & Matthies, D. (2024). Polymer-extracted structure of the mechanosensitive channel MscS reveals the role of protein-lipid interactions in the gating cycle. bioRxiv, February 5. Preprint article. https://doi.org/10.1101/2024.01.22.576751 external link
  • Lai L. T. F., Balaraman J., Zhou F., & Matthies D. (2023.) Cryo-EM structures of human magnesium channel MRS2 reveal gating and regulatory mechanisms. Nature Communications, 14(1), 7207. PMID: 37938562
  • Prévost, J., Chen, Y., Zhou, F., Tolbert, W. D., Gasser, R., Medjahed, H., Nayrac, M., Nguyen, D. N., Gottumukkala, S., Hessell, A. J., Rao, V. B., Pozharski, E., Huang, R. K., Matthies, D., Finzi, A., & Pazgier, M. (2023). Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir. Nature Communications, 14(1), 6710. PMID: 37872202
  • Nguyen, C., Lei, H. T., Lai, L. T. F., Gallenito, M. J., Mu, X., Matthies, D., & Gonen, T. (2023). Lipid flipping in the omega-3 fatty-acid transporter. Nature Communications, 14(1), 2571. PMID: 37156797
  • Ralhan, I., Chang, J., Moulton, M. J., Goodman, L. D., Lee, N. Y. J., Plummer, G., Pasolli, H. A., Matthies, D., Bellen, H. J., & Ioannou, M. S. (2023). Autolysosomal exocytosis of lipids protect neurons from ferroptosis. The Journal of Cell Biology, 222(6), e202207130. PMID: 37036445
  • Miller, A. N., Houlihan, P. R., Matamala, E., Cabezas-Bratesco, D., Lee, G. Y., Cristofori-Armstrong, B., Dilan, T. L., Sanchez-Martinez, S., Matthies, D., Yan, R., Yu, Z., Ren, D., Brauchi, S. E., & Clapham, D. E. (2023). The SARS-CoV-2 accessory protein Orf3a is not an ion channel, but does interact with trafficking proteins. eLife, 12, e84477. Advance online publication. PMID: 36695574
  • Chen, Y., Prévost, J., Ullah, I., Romero, H., Lisi, V., Tolbert, W. D., Grover, J. R., Ding, S., Gong, S. Y., Beaudoin-Bussières, G., Gasser, R., Benlarbi, M., Vézina, D., Anand, S. P., Chatterjee, D., Goyette, G., Grunst, M. W., Yang, Z., Bo, Y., Zhou, F., Béland, K., Bai, X., Zeher, A. R., Huang, R. K., Nguyen, D. N., Sherburn, R., Wu, D., Piszczek, G., Paré, B., Matthies, D., Xia, D., Richard, J., Kumar, P., Mothes, W., Côté, M., Uchil, P. D., Lavallée, V. P., Smith, M. A., Pazgier, M., Haddad, E., & Finzi, A. (2023). Molecular basis for antiviral activity of two pediatric neutralizing antibodies targeting SARS-CoV-2 Spike RBD. iScience, 26(1), 105783. PMID: 36514310
  • Petersen, J. D., Lu, J., Fitzgerald, W., Zhou, F., Blank, P. S., Matthies, D., & Zimmerberg, J. (2022). Unique aggregation of retroviral particles pseudotyped with the Delta variant SARS-CoV-2 spike protein. Viruses, 14(1024). PMID: 35632764
  • Wasmuth, E. V., Broeck, A. V., LaClair, J. R., Hoover, E. A., Lawrence, K. E., Paknejad, N., Pappas, K., Matthies, D., Wang, B., Feng, W., Watson, P. A., Zinder, J. C., Karthaus, W. R., de la Cruz, M. J., Hite, R. K., Manova-Todorova, K., Yu, Z., Weintraub, S. T., Klinge, S., & Sawyers, C. L. (2022). Allosteric interactions prime androgen receptor dimerization and activation. Molecular Cell, S1097-2765(22)00291-X. Online ahead of print. PMID: 35447082
  • Qiu, B., Matthies, D., Fortea, E., Yu, Z., & Boudker, O. (2021). Cryo-EM structures of excitatory amino acid transporter 3 visualize coupled substrate, sodium, and proton binding and transport. Science Advances, 7(10), eabf5814. PMID: 33658209
  • He, S., Chou, H. T., Matthies, D., Wunder, T., Meyer, M. T., Atkinson, N., Martinez-Sanchez, A., Jeffrey, P. D., Port, S. A., Patena, W., He, G., Chen, V. K., Hughson, F. M., McCormick, A. J., Mueller-Cajar, O., Engel, B. D., Yu, Z., & Jonikas, M. C. (2020). The structural basis of Rubisco phase separation in the pyrenoid. Nature Plants, 6(12), 1480–1490. PMID: 33230314
  • Matthies, D., Lee, N., Gatera, I., Pasolli, H. A., Zhao, X., Liu, H., Walpita, D., Liu, Z., Yu, Z., & Ioannou, M. S. (2020). Microdomains form on the luminal face of neuronal extracellular vesicle membranes. Scientific Reports, 10(1), 11953. PMID: 32686698
  • Ioannou, M. S., Jackson, J., Sheu, S. H., Chang, C. L., Weigel, A. V., Liu, H., Pasolli, H. A., Xu, C. S., Pang, S., Matthies, D., Hess, H. F., Lippincott-Schwartz, J., & Liu, Z. (2019). Neuron-astrocyte metabolic coupling protects against activity-induced fatty acid toxicity. Cell, 177(6), 1522–1535.e14. PMID: 31130380
  • Matthies, D., Bae, C., Toombes, G. E., Fox, T., Bartesaghi, A., Subramaniam, S., & Swartz, K. J. (2018). Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs. eLife, 7, e37558. PMID: 30109985
  • Puppala, A. K., French, R. L., Matthies, D., Baxa, U., Subramaniam, S., & Simonović, M. (2016). Structural basis for early-onset neurological disorders caused by mutations in human selenocysteine synthase. Scientific Reports, 6, 32563. PMID: 27576344
  • Borgnia, M. J., Banerjee, S., Merk, A., Matthies, D., Bartesaghi, A., Rao, P., Pierson, J., Earl, L. A., Falconieri, V., Subramaniam, S., & Milne, J. L. (2016). Using cryo-EM to map small ligands on dynamic metabolic enzymes: Studies with glutamate dehydrogenase. Molecular Pharmacology, 89(6), 645–651. PMID: 27036132
  • Matthies, D., Dalmas, O., Borgnia, M. J., Dominik, P. K., Merk, A., Rao, P., Reddy, B. G., Islam, S., Bartesaghi, A., Perozo, E., & Subramaniam, S. (2016). Cryo-EM structures of the magnesium channel CorA reveal symmetry break upon gating. Cell, 164(4), 747–756. PMID: 26871634
  • Ognjenović, J., Wu, J., Matthies, D., Baxa, U., Subramaniam, S., Ling, J., & Simonović, M. (2016). The crystal structure of human GlnRS provides basis for the development of neurological disorders. Nucleic Acids Research, 44(7), 3420–3431. PMID: 26869582
  • Bartesaghi, A., Merk, A., Banerjee, S., Matthies, D., Wu, X., Milne, J. L., & Subramaniam, S. (2015). 2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor. Science (New York, N.Y.), 348(6239), 1147–1151. PMID: 25953817
  • Matthies, D., Zhou, W., Klyszejko, A. L., Anselmi, C., Yildiz, Ö., Brandt, K., Müller, V., Faraldo-Gómez, J. D., & Meier, T. (2014). High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase. Nature Communications, 5, 5286. PMID: 25381992
  • Bartesaghi, A., Matthies, D., Banerjee, S., Merk, A., & Subramaniam, S. (2014). Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy. Proceedings of the National Academy of Sciences of the United States of America, 111(32), 11709–11714. PMID: 25071206
  • Schulz, S., Iglesias-Cans, M., Krah, A., Yildiz, O., Leone, V., Matthies, D., Cook, G. M., Faraldo-Gómez, J. D., & Meier, T. (2013). A new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif. PLoS Biology, 11(6), e1001596. PMID: 23824040
  • Hammann, E., Zappe, A., Keis, S., Ernst, S., Matthies, D., Meier, T., Cook, G. M., & Börsch, M. (2012). Step size of the rotary proton motor in single FoF1-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET. Proceedings of the SPIE – The International Society for Optical Engineering, 8228-82280A. https://doi.org/10.1117/12.907242 external link
  • Matthies, D., Haberstock, S., Joos, F., Dötsch, V., Vonck, J., Bernhard, F., & Meier, T. (2011). Cell-free expression and assembly of ATP synthase. Journal of Molecular Biology, 413(3), 593–603. PMID: 21925509
  • Kalamorz, F., Keis, S., McMillan, D. G., Olsson, K., Stanton, J. A., Stockwell, P., Black, M. A., Klingeman, D. M., Land, M. L., Han, C. S., Martin, S. L., Becher, S. A., Peddie, C. J., Morgan, H. W., Matthies, D., Preiss, L., Meier, T., Brown, S. D., & Cook, G. M. (2011). Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus thermarum strain TA2.A1. Journal of Bacteriology, 193(16), 4290–4291. PMID: 21685297
  • Matthies, D., Preiss, L., Klyszejko, A. L., Muller, D. J., Cook, G. M., Vonck, J., & Meier, T. (2009). The c13 ring from a thermoalkaliphilic ATP synthase reveals an extended diameter due to a special structural region. Journal of Molecular Biology, 388(3), 611–618. PMID: 19327366
  • Meier, T., Morgner, N., Matthies, D., Pogoryelov, D., Keis, S., Cook, G. M., Dimroth, P., & Brutschy, B. (2007). A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic Bacillus sp. strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential. Molecular Microbiology, 65(5), 1181–1192. PMID: 17645441
top of page BACK TO TOP