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C. (Cristina) Batista Paulino, PhD

Assistant Professor, Head of cryo-EM unit

C. (Cristina) Batista Paulino, PhD
Telephone:
+31 50 36 33402 (Office)
Jannet Nijhuis-Kampen (Secretary):
+31 50 36 32400 (Office)
E-mail:
c.paulino rug.nl

Research

Research units:

Postal address:
Nijenborgh4
Gebouw 5171, ruimte 0054
9747 AG
Groningen
Netherlands
Phone: +31 50 363 3402Fax: +31 50 363 4165
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1 - 12 out of 12Page size: 50
  1. 2019
  2. Garaeva, A. A., Guskov, A., Slotboom, D. J., & Paulino, C. (2019). A one-gate elevator mechanism for the human neutral amino acid transporter ASCT2. Nature Communications, 10, [3427]. https://doi.org/10.1038/s41467-019-11363-x
  3. Kalienkova, V., Mosina, V. C., Bryner, L., Oostergetel, G. T., Dutzler, R., & Paulino, C. (2019). Stepwise activation mechanism of the scramblase nhTMEM16 revealed by cryo-EM. eLife, 8, [44364]. https://doi.org/10.7554/eLife.44364
  4. Alvadia, C., Lim, N. K., Mosina, V. C., Oostergetel, G. T., Dutzler, R., & Paulino, C. (2019). Cryo-EM structures and functional characterization of the murine lipid scramblase TMEM16F. eLife, 8, [44365]. https://doi.org/10.7554/eLife.44365
  5. 2018
  6. Stock, C., Hielkema, L., Tascón, I., Wunnicke, D., Oostergetel, G. T., Azkargorta, M., ... Hänelt, I. (2018). Cryo-EM structures of KdpFABC suggest a K transport mechanism via two inter-subunit half-channels. Nature Communications, 9(1), [4971]. https://doi.org/10.1038/s41467-018-07319-2
  7. Deneka, D., Sawicka, M., Lam, A. K. M., Batista Paulino, C., & Dutzler, R. (2018). Structure of a volume-regulated anion channel of the LRRC8 family. Nature, 558, 254-259. https://doi.org/10.1038/s41586-018-0134-y
  8. Garaeva, A., Oostergetel, G., Gati, C., Guskov, A., Batista Paulino, C., & Slotboom, D. (2018). Cryo-EM structure of the human neutral amino acid transporter ASCT2. Nature Structural & Molecular Biology, 25, 515-521. https://doi.org/10.1038/s41594-018-0076-y
  9. 2017
  10. Batista Paulino, C., Kalienkova, V., Lam, A. KM., Neldner, Y., & Dutzler, R. (2017). Activation mechanism of the chloride channel TMEM16A revealed by cryo-EM. Nature, 552(7685), 421-425. [24652]. https://doi.org/10.1038/nature24652
  11. Batista Paulino, C., Neldner, Y., Lam, A. KM., Kalienkova, V., Brunner, J. D., Schenck, S., & Dutzler, R. (2017). Structural basis for anion conduction in the calcium-activated chloride channel TMEM16A. eLife, 6, 1-23. [e26232]. https://doi.org/10.7554/eLife.26232
  12. 2014
  13. Batista Paulino, C., Woehlert, D., Karpotova, E., Yildiz, Ö., & Kuehlbrandt, W. (2014). Structure and transport mechanism of the sodium/proton antiporter MjNhaP1. eLife, 3, 1-21. [e03583]. https://doi.org/10.7554/eLife.03583
  14. Calinescu, O., Batista Paulino, C., Kuehlbrandt, W., & Fendler, K. (2014). Keeping It Simple, Transport Mechanism and pH Regulation in Na (+)/H (+) Exchangers. The Journal of Biological Chemistry, 289(19), 13168-13176. https://doi.org/10.1074/jbc.M113.542993
  15. Batista Paulino, C., & Kuehlbrandt, W. (2014). pH- and sodium-induced changes in a sodium/proton antiporter. eLife, 3, 1-13. [e01412]. https://doi.org/10.7554/eLife.01412
  16. 2011
  17. Goswami, P., Batista Paulino, C., Hizlan, D., Vonck, J., Yildiz, Ö., & Kuehlbrandt, W. (2011). Structure of the archaeal Na+/H+ antiporter NhaP1 and functional role of transmembrane helix 1. The EMBO Journal, 30, 439-449. https://doi.org/10.1038/emboj.2010.321

ID: 45996756

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