An essential thioredoxin-type protein of Trypanosoma brucei acts as redox-regulated mitochondrial chaperone

Most known thioredoxin-type proteins (Trx) participate in redox pathways, using two highly conserved cysteine residues to catalyze thiol-disulfide exchange reactions. Here we demonstrate that the so far unexplored Trx2 from African trypanosomes (Trypanosoma brucei) lacks protein disulfide reductase...

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Bibliografiske detaljer

Hovedforfatter:	Currier, R. (author)
Andre forfattere:	Ulrich, K. (author), Leroux, A. (author), Dirdjaja, N. (author), Deambrosi Borrat, Matías (author), Bonilla Chao, Mariana Magdalena (author), Luqman Ahmed, Y. (author), Adrian, L. (author), Antelmann, H. (author), Jakob, U. (author), Comini, Marcelo A. (author), Krauth-Siegel, R.L. (author)
Format:	article
Sprog:	engelsk
Udgivet:	2019
Fag:	Trypanosome Oxidation-reduction
Online adgang:	https://hdl.handle.net/20.500.12008/28465
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