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PUBLICAÇÕES

  1. Sepulveda, M., Martínez Traub, F., Ojeda, P., Perez, V., Ojeda, J., Mella, J., Diaz, R., Rozas, P., Mansilla-Jaramillo, M., Zuleta, A., Diaz, G., Kerr, B., Woehlbier, U., Henríquez, J. P., Medinas, D. B., & Hetz, C. (2025). Expression of protein disulfide isomerase A3Q481K variant associated with amyotrophic lateral sclerosis triggers disease features in mice. Neurobiology of disease, 212, 106947. https://doi.org/10.1016/j.nbd.2025.106947

  2. Cabral-Miranda, F., Araujo, A. P. B., Medinas, D. B., & Gomes, F. C. A. (2025). Astrocytic Hevin/SPARCL-1 Regulates Cognitive Decline in Pathological and Normal Brain Aging. Aging cell, 24(5), e14493. https://doi.org/10.1111/acel.14493

  3. Labrador, L., Rodriguez, L., Beltran, S., Hernandez, F., Gomez, L., Ojeda, P., Bergmann, C., Calegaro-Nassif, M., Kerr, B., Medinas, D. B., Manque, P., & Woehlbier, U. (2024). Overexpression of autophagy enhancer PACER/RUBCNL in neurons accelerates disease in the SOD1G93A ALS mouse model. Biological research, 57(1), 86. https://doi.org/10.1186/s40659-024-00567-1

  4. Borgonovo, J., Allende-Castro, C., Medinas, D. B., Cárdenas, D., Cuevas, M. P., Hetz, C., & Concha, M. L. (2024). Immunohistochemical characterisation of the adult Nothobranchius furzeri intestine. Cell and tissue research, 395(1), 21–38. https://doi.org/10.1007/s00441-023-03845-8

  5. Duran-Aniotz, C., Poblete, N., Rivera-Krstulovic, C., Ardiles, Á. O., Díaz-Hung, M. L., Tamburini, G., Sabusap, C. M. P., Gerakis, Y., Cabral-Miranda, F., Diaz, J., Fuentealba, M., Arriagada, D., Muñoz, E., Espinoza, S., Martinez, G., Quiroz, G., Sardi, P., Medinas, D. B., Contreras, D., Piña, R., … Hetz, C. (2023). The unfolded protein response transcription factor XBP1s ameliorates Alzheimer’s disease by improving synaptic function and proteostasis. Molecular therapy : the journal of the American Society of Gene Therapy, 31(7), 2240–2256. https://doi.org/10.1016/j.ymthe.2023.03.028

  6. Medinas, D. B., Arshad, N., Parakh, S., Miyamoto, S., & Zambelli, V. O. (2023). Editorial: Restoring endoplasmic reticulum proteostasis to treat neurological disorders. Frontiers in pharmacology, 14, 1176805. https://doi.org/10.3389/fphar.2023.1176805

  7. Cabral-Miranda, F., Tamburini, G., Martinez, G., Ardiles, A. O., Medinas, D. B., Gerakis, Y., Hung, M. D., Vidal, R., Fuentealba, M., Miedema, T., Duran-Aniotz, C., Diaz, J., Ibaceta-Gonzalez, C., Sabusap, C. M., Bermedo-Garcia, F., Mujica, P., Adamson, S., Vitangcol, K., Huerta, H., Zhang, X., … Hetz, C. (2022). Unfolded protein response IRE1/XBP1 signaling is required for healthy mammalian brain aging. The EMBO journal, 41(22), e111952. https://doi.org/10.15252/embj.2022111952

  8. Medinas, D. B., Rozas, P., & Hetz, C. (2022). Critical roles of protein disulfide isomerases in balancing proteostasis in the nervous system. The Journal of biological chemistry, 298(7), 102087. https://doi.org/10.1016/j.jbc.2022.102087

  9. Vásquez, G. E., Medinas, D. B., Urra, H., & Hetz, C. (2022). Emerging roles of endoplasmic reticulum proteostasis in brain development. Cells & development, 170, 203781. https://doi.org/10.1016/j.cdev.2022.203781

  10. Duran-Aniotz, C., Moreno-Gonzalez, I., Medinas, D. B., & Morales, R. (2022). Editorial: Protein Misfolding and Proteostasis Impairment in Aging and Neurodegeneration: From Spreading Studies to Therapeutic Approaches. Frontiers in aging neuroscience, 13, 830779. https://doi.org/10.3389/fnagi.2021.830779

  11. Medinas, D. B., Hazari, Y., & Hetz, C. (2021). Disruption of Endoplasmic Reticulum Proteostasis in Age-Related Nervous System Disorders. Progress in molecular and subcellular biology, 59, 239–278. https://doi.org/10.1007/978-3-030-67696-4_12

  12. Rozas, P., Pinto, C., Martínez Traub, F., Díaz, R., Pérez, V., Becerra, D., Ojeda, P., Ojeda, J., Wright, M. T., Mella, J., Plate, L., Henríquez, J. P., Hetz, C., & Medinas, D. B. (2021). Protein disulfide isomerase ERp57 protects early muscle denervation in experimental ALS. Acta neuropathologica communications, 9(1), 21. https://doi.org/10.1186/s40478-020-01116-z

  13. Pinto, C., Medinas, D. B., Fuentes-Villalobos, F., Maripillán, J., Castro, A. F., Martínez, A. D., Osses, N., Hetz, C., & Henríquez, J. P. (2019). β-catenin aggregation in models of ALS motor neurons: GSK3β inhibition effect and neuronal differentiation. Neurobiology of disease, 130, 104497. https://doi.org/10.1016/j.nbd.2019.104497

  14. Beltran, S., Nassif, M., Vicencio, E., Arcos, J., Labrador, L., Cortes, B. I., Cortez, C., Bergmann, C. A., Espinoza, S., Hernandez, M. F., Matamala, J. M., Bargsted, L., Matus, S., Rojas-Rivera, D., Bertrand, M. J. M., Medinas, D. B., Hetz, C., Manque, P. A., & Woehlbier, U. (2019). Network approach identifies Pacer as an autophagy protein involved in ALS pathogenesis. Molecular neurodegeneration, 14(1), 14. https://doi.org/10.1186/s13024-019-0313-9

  15. Medinas, D. B., Cabral-Miranda, F., & Hetz, C. (2019). ER stress links aging to sporadic ALS. Aging, 11(1), 5–6. https://doi.org/10.18632/aging.101705

  16. Medinas, D. B., Rozas, P., Martínez Traub, F., Woehlbier, U., Brown, R. H., Bosco, D. A., & Hetz, C. (2018). Endoplasmic reticulum stress leads to accumulation of wild-type SOD1 aggregates associated with sporadic amyotrophic lateral sclerosis. Proceedings of the National Academy of Sciences of the United States of America, 115(32), 8209–8214. https://doi.org/10.1073/pnas.1801109115

  17. Bargsted, L., Medinas, D. B., Martínez Traub, F., Rozas, P., Muñoz, N., Nassif, M., Jerez, C., Catenaccio, A., Court, F. A., Hetz, C., & Matus, S. (2017). Disulfide cross-linked multimers of TDP-43 and spinal motoneuron loss in a TDP-43A315T ALS/FTD mouse model. Scientific reports, 7(1), 14266. https://doi.org/10.1038/s41598-017-14399-5

  18. Medinas, D. B., Valenzuela, V., & Hetz, C. (2017). Proteostasis disturbance in amyotrophic lateral sclerosis. Human molecular genetics, 26(R2), R91–R104. https://doi.org/10.1093/hmg/ddx274

  19. Medinas, D. B., González, J. V., Falcon, P., & Hetz, C. (2017). Fine-Tuning ER Stress Signal Transducers to Treat Amyotrophic Lateral Sclerosis. Frontiers in molecular neuroscience, 10, 216. https://doi.org/10.3389/fnmol.2017.00216

  20. Duran-Aniotz, C., Cornejo, V. H., Espinoza, S., Ardiles, Á. O., Medinas, D. B., Salazar, C., Foley, A., Gajardo, I., Thielen, P., Iwawaki, T., Scheper, W., Soto, C., Palacios, A. G., Hoozemans, J. J. M., & Hetz, C. (2017). IRE1 signaling exacerbates Alzheimer’s disease pathogenesis. Acta neuropathologica, 134(3), 489–506. https://doi.org/10.1007/s00401-017-1694-x

  21. Rozas, P., Bargsted, L., Martínez, F., Hetz, C., & Medinas, D. B. (2017). The ER proteostasis network in ALS: Determining the differential motoneuron vulnerability. Neuroscience letters, 636, 9–15. https://doi.org/10.1016/j.neulet.2016.04.066

  22. Mollereau, B., Rzechorzek, N. M., Roussel, B. D., Sedru, M., Van den Brink, D. M., Bailly-Maitre, B., Palladino, F., Medinas, D. B., Domingos, P. M., Hunot, S., Chandran, S., Birman, S., Baron, T., Vivien, D., Duarte, C. B., Ryoo, H. D., Steller, H., Urano, F., Chevet, E., Kroemer, G., … Hetz, C. (2016). Adaptive preconditioning in neurological diseases – therapeutic insights from proteostatic perturbations. Brain research, 1648(Pt B), 603–616. https://doi.org/10.1016/j.brainres.2016.02.033

  23. Woehlbier, U., Colombo, A., Saaranen, M. J., Pérez, V., Ojeda, J., Bustos, F. J., Andreu, C. I., Torres, M., Valenzuela, V., Medinas, D. B., Rozas, P., Vidal, R. L., Lopez-Gonzalez, R., Salameh, J., Fernandez-Collemann, S., Muñoz, N., Matus, S., Armisen, R., Sagredo, A., Palma, K., … Hetz, C. (2016). ALS-linked protein disulfide isomerase variants cause motor dysfunction. The EMBO journal, 35(8), 845–865. https://doi.org/10.15252/embj.201592224

  24. Sepulveda, M., Rozas, P., Hetz, C., & Medinas, D. B. (2016). ERp57 as a novel cellular factor controlling prion protein biosynthesis: Therapeutic potential of protein disulfide isomerases. Prion, 10(1), 50–56. https://doi.org/10.1080/19336896.2015.1129485

  25. Torres, M., Medinas, D. B., Matamala, J. M., Woehlbier, U., Cornejo, V. H., Solda, T., Andreu, C., Rozas, P., Matus, S., Muñoz, N., Vergara, C., Cartier, L., Soto, C., Molinari, M., & Hetz, C. (2015). The Protein-disulfide Isomerase ERp57 Regulates the Steady-state Levels of the Prion Protein. The Journal of biological chemistry, 290(39), 23631–23645. https://doi.org/10.1074/jbc.M114.635565

  26. Appolinário, P. P., Medinas, D. B., Chaves-Filho, A. B., Genaro-Mattos, T. C., Cussiol, J. R., Netto, L. E., Augusto, O., & Miyamoto, S. (2015). Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols. PloS one, 10(4), e0125146. https://doi.org/10.1371/journal.pone.0125146

  27. Medinas, D. B., & Hetz, C. (2014). Protein homeostasis: Modeling UPR adaptive responses. Nature chemical biology, 10(11), 879–880. https://doi.org/10.1038/nchembio.1653

  28. Matus, S., Medinas, D. B., & Hetz, C. (2014). Common ground: stem cell approaches find shared pathways underlying ALS. Cell stem cell, 14(6), 697–699. https://doi.org/10.1016/j.stem.2014.05.001

  29. Campos, G., Schmidt-Heck, W., Ghallab, A., Rochlitz, K., Pütter, L., Medinas, D. B., Hetz, C., Widera, A., Cadenas, C., Begher-Tibbe, B., Reif, R., Günther, G., Sachinidis, A., Hengstler, J. G., & Godoy, P. (2014). The transcription factor CHOP, a central component of the transcriptional regulatory network induced upon CCl4 intoxication in mouse liver, is not a critical mediator of hepatotoxicity. Archives of toxicology, 88(6), 1267–1280. https://doi.org/10.1007/s00204-014-1240-8

  30. Matus, S., Valenzuela, V., Medinas, D. B., & Hetz, C. (2013). ER Dysfunction and Protein Folding Stress in ALS. International journal of cell biology, 2013, 674751. https://doi.org/10.1155/2013/674751

  31. Medinas, D. B., & Hetz, C. (2013). Proteostasis impairment: at the intersection between Alzheimer’s disease and diabetes. Cell metabolism, 18(6), 771–772. https://doi.org/10.1016/j.cmet.2013.11.009

  32. Massari, J., Tokikawa, R., Medinas, D. B., Angeli, J. P., Di Mascio, P., Assunção, N. A., & Bechara, E. J. (2011). Generation of singlet oxygen by the glyoxal-peroxynitrite system. Journal of the American Chemical Society, 133(51), 20761–20768. https://doi.org/10.1021/ja2051414

  33. Medinas, D. B., Gozzo, F. C., Santos, L. F., Iglesias, A. H., & Augusto, O. (2010). A ditryptophan cross-link is responsible for the covalent dimerization of human superoxide dismutase 1 during its bicarbonate-dependent peroxidase activity. Free radical biology & medicine, 49(6), 1046–1053. https://doi.org/10.1016/j.freeradbiomed.2010.06.018

  34. Medinas, D. B., & Augusto, O. (2010). Mechanism of the peroxidase activity of superoxide dismutase 1. Free radical biology & medicine, 49(4), 682–684. https://doi.org/10.1016/j.freeradbiomed.2010.04.040

  35. Medinas, D. B., Toledo, J. C., Jr, Cerchiaro, G., do-Amaral, A. T., de-Rezende, L., Malvezzi, A., & Augusto, O. (2009). Peroxymonocarbonate and carbonate radical displace the hydroxyl-like oxidant in the Sod1 peroxidase activity under physiological conditions. Chemical research in toxicology, 22(4), 639–648. https://doi.org/10.1021/tx800287m

  36. Medinas, D. B., Cerchiaro, G., Trindade, D. F., & Augusto, O. (2007). The carbonate radical and related oxidants derived from bicarbonate buffer. IUBMB life, 59(4-5), 255–262. https://doi.org/10.1080/15216540701230511

  37. Fernandes, D. C., Medinas, D. B., Alves, M. J., & Augusto, O. (2005). Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation. Free radical biology & medicine, 38(2), 189–200. https://doi.org/10.1016/j.freeradbiomed.2004.09.027