Journal article
Authors list: Rahlfs, S; Nickel, C; Deponte, M; Schirmer, RH; Becker, K
Publication year: 2003
Pages: 246-250
Journal: Redox Report: Communications in Free Radical Research
Volume number: 8
Issue number: 5
ISSN: 1351-0002
eISSN: 1743-2928
Open access status: Bronze
DOI Link: https://doi.org/10.1179/135100003225002844
Publisher: Taylor and Francis Group
Abstract:
Over the last few years, an increasing number of different functions have been ascribed to small redox-active proteins like thioredoxins (Trx) and glutaredoxins (Grx). These functions include redox regulation of transcription and translation, antioxidant defence, involvement in protein folding and cellular signalling, and reduction of ribonucleotide reductase. In the malarial parasite Plasmodium falciparum, a classical Trx and a typical Grx have been described as well as a number of Trx- and Grx-like proteins including monothiol glutaredoxins. Furthermore, plasmoredoxin, a redox-active protein related to Trx, has been characterized; plasmoredoxin is unique for malarial parasites, therefore having great potential as diagnostic tool. In this minireview, we summarize the current knowledge on members of the thioredoxin superfamily and their function in the malarial parasite P. falciparum.
Citation Styles
Harvard Citation style: Rahlfs, S., Nickel, C., Deponte, M., Schirmer, R. and Becker, K. (2003) Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism, Redox Report: Communications in Free Radical Research, 8(5), pp. 246-250. https://doi.org/10.1179/135100003225002844
APA Citation style: Rahlfs, S., Nickel, C., Deponte, M., Schirmer, R., & Becker, K. (2003). Plasmodium falciparum thioredoxins and glutaredoxins as central players in redox metabolism. Redox Report: Communications in Free Radical Research. 8(5), 246-250. https://doi.org/10.1179/135100003225002844