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Distribution and Features of the Six Classes of Peroxiredoxins
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  • Journal title : Molecules and Cells
  • Volume 39, Issue 1,  2016, pp.53-59
  • Publisher : Korea Society for Molecular and Cellular Biology
  • DOI : 10.14348/molcells.2016.2330
 Title & Authors
Distribution and Features of the Six Classes of Peroxiredoxins
Poole, Leslie B.; Nelson, Kimberly J.;
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 Abstract
Peroxiredoxins are cysteine-dependent peroxide reductases that group into 6 different, structurally discernable classes. In 2011, our research team reported the application of a bioinformatic approach called active site profiling to extract active site-proximal sequence segments from the 29 distinct, structurally-characterized peroxiredoxins available at the time. These extracted sequences were then used to create unique profiles for the six groups which were subsequently used to search GenBank(nr), allowing identification of ~3500 peroxiredoxin sequences and their respective subgroups. Summarized in this minireview are the features and phylogenetic distributions of each of these peroxiredoxin subgroups; an example is also provided illustrating the use of the web accessible, searchable database known as PREX to identify subfamily-specific peroxiredoxin sequences for the organism Vitis vinifera (grape).
 Keywords
active site profiling;bioinformatics;disulfide reductase;peroxide reductase;thiol peroxidase;
 Language
English
 Cited by
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Overview on Peroxiredoxin, Molecules and Cells, 2016, 39, 1, 1  crossref(new windwow)
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An Atlas of Peroxiredoxins Created Using an Active Site Profile-Based Approach to Functionally Relevant Clustering of Proteins, PLOS Computational Biology, 2017, 13, 2, e1005284  crossref(new windwow)
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LokiarchaeotaMarks the Transition between the Archaeal and Eukaryotic Selenocysteine Encoding Systems, Molecular Biology and Evolution, 2016, 33, 9, 2441  crossref(new windwow)
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The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE, Chem. Commun., 2016, 52, 67, 10293  crossref(new windwow)
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Evolution and function of the Mycoplasma hyopneumoniae peroxiredoxin, a 2-Cys-like enzyme with a single Cys residue, Molecular Genetics and Genomics, 2017, 292, 2, 297  crossref(new windwow)
6.
Peroxiredoxin 6 in the repair of peroxidized cell membranes and cell signaling, Archives of Biochemistry and Biophysics, 2017, 617, 68  crossref(new windwow)
7.
The Architecture of Thiol Antioxidant Systems among Invertebrate Parasites, Molecules, 2017, 22, 2, 259  crossref(new windwow)
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Crystal structures of human peroxiredoxin 6 in different oxidation states, Biochemical and Biophysical Research Communications, 2016, 477, 4, 717  crossref(new windwow)
9.
Hyperoxidation of Peroxiredoxins: Gain or Loss of Function?, Antioxidants & Redox Signaling, 2017  crossref(new windwow)
10.
Experimentally Dissecting the Origins of Peroxiredoxin Catalysis, Antioxidants & Redox Signaling, 2017  crossref(new windwow)
11.
Alteration of molecular assembly of peroxiredoxins from hyperthermophilic archaea, The Journal of Biochemistry, 2017  crossref(new windwow)
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