Miklós Geiszt - Selected Publications#

1. Sirokmány G, Geiszt M. The Relationship of NADPH Oxidases and Heme Peroxidases: Fallin' in and Out. Front. Immunol. 2019 Mar 5;10:394. doi: 10.3389/fimmu.2019.00394. eCollection 2019.

2. Sirokmány G, Kovács HA, Lázár E, Kónya K, Donkó Á, Enyedi B, Grasberger H, Geiszt M. Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases. Redox. Biol. (2018) 16:314-321.
3. Zana M, Péterfi Z, Kovács HA, Tóth ZE, Enyedi B, Morel F, Paclet MH, Donkó Á, Morand S, Leto TL, Geiszt M. Interaction between p22(phox) and Nox4 in the endoplasmic reticulum suggests a unique mechanism of NADPH oxidase complex formation. Free. Radic. Biol. Med. (2017) 116:41-49.

4. Sirokmány G, Pató A, Zana M, Donkó Á, Bíró A, Nagy P, Geiszt M. Epidermal growth factor-induced hydrogen peroxide production is mediated by dual oxidase 1. Free. Radic. Biol. Med. (2016) 97:204-211.

5. Sirokmány G, Donkó Á, Geiszt M Nox/Duox Family of NADPH Oxidases: Lessons from Knockout Mouse Models. TRENDS IN PHARMACOLOGICAL SCIENCES (2016) 37:318-327

6. Péterfi Z , Tóth ZE , Kovács HA , Lázár E , Sum A , Donkó Á , Sirokmány G , Shah AM , Geiszt M Peroxidasin-like protein: A novel peroxidase homologue in the human heart CARDIOVASCULAR RESEARCH 101:(3) pp. 393-399. (2014)
7. Péterfi Z , Geiszt M Peroxidasins: novel players in tissue genesis. TRENDS IN BIOCHEMICAL SCIENCES 39:(7) pp. 305-307. (2014)

8. Enyedi B, Várnai P, Geiszt M. Redox state of the endoplasmic reticulum is controlled by Ero1L-alpha and intraluminal calcium. (2010) Antioxid. Redox. Signal. 13, 721-9.

9. Geiszt M., Witta J., Baffi J., Lekstrom K., Leto T.L. Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. (2003) FASEB J. 17, 1502-1504.

10. Geiszt M., Kopp JB., Varnai P., Leto TL. Identification of Renox, an NAD(P)H-oxidase in kidney. Proc. Natl. Acad. Sci. USA. (2000) 97, 8010-8014.