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Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha

Autor: Hannes Juergens, Robert Mans, Nijenhuis Jm, McMillan Dgg, Mielgo-Gómez Á, ter Horst J, Godoy-Hernández A

Mitochondria from Ogataea parapolymorpha harbor a branched electron-transport chain containing a proton-pumping Complex I NADH dehydrogenase and three alternative (type II) NADH dehydrogenases (NDH2s). To investigate the physiological role, localizat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8e117b0807dad001c38ec4a30f19d122
https://doi.org/10.1101/2021.04.28.441406

Sex differences in fear memory and extinction of mice with forebrain-specific disruption of the mineralocorticoid receptor.

Autor: ter Horst, J. P.¹ (AUTHOR), Carobrez, A. P.² (AUTHOR), van der Mark, M. H.¹ (AUTHOR), de Kloet, E. R.¹ (AUTHOR), Oitzl, M. S.¹ (AUTHOR)

Publikováno v: European Journal of Neuroscience. Oct2012, Vol. 36 Issue 8, p3096-3102. 7p.

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A cytochrome b5 is required for cytochrome P450 activity and blue flower colours

Autor: de Vetten, N., ter Horst, J., van Schaik, H.-P., de Boer, A.H., Mol, J.N.M., Koes, R.E.

Publikováno v: de Vetten, N, ter Horst, J, van Schaik, H-P, de Boer, A H, Mol, J N M & Koes, R E 1998, ' A cytochrome b5 is required for cytochrome P450 activity and blue flower colours ', Proceedings of the National Academy of Sciences of the United States of America, vol. 2, pp. 778-783 . https://doi.org/10.1073/pnas.96.2.778
Proceedings of the National Academy of Sciences of the United States of America, 2, 778-783. National Acad Sciences

The substitution pattern of anthocyanin pigments is a main determinant of flower color. Flavonoid 3',5'-hydroxylase (F3'5'H) is a cytochrome P450 enzyme (Cyt P450) that catalyzes the 3',5'-hydroxylation of dihydroflavonols, the precursors of purple a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::61242b4d3b6dd4d2e808e67e6dbc69da
https://doi.org/10.1073/pnas.96.2.778