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
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
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
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