Because of a lapse in government funding, the information on this website may not be up to date, transactions submitted via the website may not be processed, and the agency may not be able to respond to inquiries until appropriations are enacted.

The NIH Clinical Center (the research hospital of NIH) is open. For more details about its operating status, please visit cc.nih.gov.

Updates regarding government operating status and resumption of normal operations can be found at OPM.gov.

Publications

  • Richard, J., Grunst, M.W., Niu, L., Díaz-Salinas, M.A., Tolbert, W.D., Marchitto, L., Zhou F., Bourassa C., Yang, D., Chiu, T.J., Chen, H.C., Benlarbi, M, Guillaume-Beaudoin-Buissières, Gottumukkala, S., Li, W., Dionne, K., Bélanger, E., Chatterjee, D., Medjahed, H., Hendrickson, W.A., Sodroski, J., Lang, Z.C, J. Morton, A., Huang, R.K., Matthies, D., Smith, A.B. III, Mothes, W., Munro, J.B., Pazgier, M., Finzi, A. (2024). The asymmetric opening of HIV-1 Env by a potent CD4 mimetic enables anti-coreceptor binding site antibodies to mediate ADCC . bioRxiv 2024.08.27.609961. https://doi.org/10.1101/2024.08.27.609961 external link
  • 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, Zöller J, Madni ZK, Lessen H, Aravind L, Langer JD, Sodt AJ, Storz G, Matthies D. P-type ATPase magnesium transporter MgtA acts as a dimer. Nat Struct Mol Biol. 2025 Jun 23. doi: 10.1038/s41594-025-01593-7. Epub ahead of print. PMID: 40550995.
  • 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
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