Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
SG Rhee, HZ Chae, K Kim - Free radical biology and Medicine, 2005 - Elsevier
The observation that purified yeast glutamine synthetase is rapidly inactivated in a thiol-containing
buffer yet retains activity in crude extracts containing the same thiol led to our …
buffer yet retains activity in crude extracts containing the same thiol led to our …
[HTML][HTML] Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-α
Mammalian tissues express three immunologically distinct peroxiredoxin (Prx) proteins (Prx I,
II, and III), which are the products of distinct genes. With the use of recombinant proteins …
II, and III), which are the products of distinct genes. With the use of recombinant proteins …
Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during
catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to …
catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to …
[HTML][HTML] Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
Peroxidases of the peroxiredoxin (Prx) family contain a Cys residue that is preceded by a
conserved sequence in the NH 2 -terminal region. A new type of mammalian Prx, designated …
conserved sequence in the NH 2 -terminal region. A new type of mammalian Prx, designated …
[HTML][HTML] Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
By following peroxiredoxin I (Prx I)-dependent NADPH oxidation spectrophotometrically, we
observed that Prx I activity decreased gradually with time. The decay in activity was …
observed that Prx I activity decreased gradually with time. The decay in activity was …
The isolation and purification of a specific “protector” protein which inhibits enzyme inactivation by a thiol/Fe (III)/O2 mixed-function oxidation system.
K Kim, IH Kim, KY Lee, SG Rhee… - Journal of Biological …, 1988 - Elsevier
Mixed-function oxidation systems comprised of Fe3+, O2, and electron donors such as thiol
compounds, ascorbate, NAD(P)H/NAD(P)H oxidase, and xanthine oxidase/hypoxanthine, …
compounds, ascorbate, NAD(P)H/NAD(P)H oxidase, and xanthine oxidase/hypoxanthine, …
[HTML][HTML] Cyclophilin a binds to peroxiredoxins and activates its peroxidase activity
…, YS Hwang, YJ Kim, KS Kwon, HJ Kim, K Kim… - Journal of Biological …, 2001 - ASBMB
Six distinct peroxiredoxin (Prx) proteins (Prx I-VI) from distinct genes have been identified in
mammalian tissues. Prxs are members of a group of peroxidases that have conserved …
mammalian tissues. Prxs are members of a group of peroxidases that have conserved …
[HTML][HTML] Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity∗
…, HA Woo, KS Kwon, YS Kim, SG Rhee, K Kim… - Journal of Biological …, 2008 - ASBMB
The thiol (–SH) of the active cysteine residue in peroxiredoxin (Prx) is known to be reversibly
hyperoxidized to cysteine sulfinic acid (–SO 2 H), which can be reduced back to thiol by …
hyperoxidized to cysteine sulfinic acid (–SO 2 H), which can be reduced back to thiol by …
Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron.
K Kim, SG Rhee, ER Stadtman - Journal of Biological Chemistry, 1985 - ASBMB
Many enzymes, represented by yeast glutamine synthetase, are inactivated and degraded in
the presence of dithiothreitol (DTT), oxygen, and catalytic amounts of iron salts. The roles of …
the presence of dithiothreitol (DTT), oxygen, and catalytic amounts of iron salts. The roles of …
Regulation of thioredoxin peroxidase activity by C-terminal truncation
…, S Lee, SY Jeong, ET Kim, HJ Kim, K Kim… - Archives of biochemistry …, 2002 - Elsevier
Thioredoxin peroxidase is a member of peroxiredoxin (Prx) family, which uses a thioredoxin
(Trx) as an immediate electron donor for the reduction of peroxide. We have identified C-…
(Trx) as an immediate electron donor for the reduction of peroxide. We have identified C-…