Two Enzymes in One: Two Yeast Peroxiredoxins Display Oxidative Stress-Dependent Switching from a Peroxidase to a Molecular Chaperone Function
By H. Jang, Kyun Oh Lee, Y. Chi, B. Jung, Soo-Kwon Park, Jin Ho Park, Jung Ro Lee, Seung Sik Lee, Jeong Chan Moon, J. Yun and 8 more. 2004
749 citations recorded by the source corpus.
Subfields: Biochemistry, Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/46dd56964ee186d86652702aaf3b83234ccbcda0
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In Biochemistry
In Molecular Biology
Citations in the corpus
- The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “Three cytoplasmic 2-Cys Prx’s (Tsa1, Tsa2, and Ahp1) have been described in yeast (Morgan and Veal 2007).”
- Redox redux: revisiting PTPs and the control of cell signaling. (2005, background): “Interestingly, yeast cytosolic peroxiredoxins (Prx) also undergo a shift from low Mr to high Mr forms following oxidative stress of the cells, inducing a functional change in Prx, from a peroxidase to a chaperone, which helps the yeast cell adapt to the stress response (Jang et al., 2004).”
- Antioxidants and Antioxidant Enzymes in Higher Plants (2018, background): “The oligomerization confers other relevant functions to these peroxiredoxins as chaperones that protect proteins from denaturalization when they are exposed to heat and oxidative shocks (Jang et al. 2004; Moon et al. 2005).”