2009
DOI: 10.1016/j.canlet.2009.04.043
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Peroxiredoxins, a novel target in cancer radiotherapy

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Cited by 108 publications
(73 citation statements)
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“…In addition, PRDX1 crystallized as toroid‐shaped complexes consisting of a pentameric arrangement of dimers [an (a 2 ) 5 decamer], consistent with observations that PRDX1 dimers can form discrete higher‐order oligomers 8. Compared with other antioxidant enzymes, PRDX1 employs a particular mechanism to detoxify peroxide with reducing equivalents provided through the thioredoxin (Trx) system but not from glutaredoxin 19.…”
Section: Structure Functions Of Prdx1 and Its Role In Ros‐dependent supporting
confidence: 72%
“…In addition, PRDX1 crystallized as toroid‐shaped complexes consisting of a pentameric arrangement of dimers [an (a 2 ) 5 decamer], consistent with observations that PRDX1 dimers can form discrete higher‐order oligomers 8. Compared with other antioxidant enzymes, PRDX1 employs a particular mechanism to detoxify peroxide with reducing equivalents provided through the thioredoxin (Trx) system but not from glutaredoxin 19.…”
Section: Structure Functions Of Prdx1 and Its Role In Ros‐dependent supporting
confidence: 72%
“…Literature data report an over-expression of PRDXs in several human cancers (mesothelioma, bladder, breast, and brain cancers) during tumorigenesis [Kinnula et al, 2002;Chang et al, 2007;Zhang et al, 2009], tumor recurrence or progression [Quan et al, 2006], and cancer therapies [An and Seong, 2006;Pak et al, 2011].…”
Section: Discussionmentioning
confidence: 99%
“…It is a member of the Prdxs family of antioxidant proteins which is known to be overexpressed in several different carcinomas [18,19]. Many studies indicated that aberrant expression of Prdxs was found in various kinds of cancers.…”
Section: Discussionmentioning
confidence: 99%