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Crystal structure of a dimeric oxidized form of human peroxiredoxin 5
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title
Crystal structure of a dimeric oxidized form of human peroxiredoxin 5
(English)
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main subject
crystal structure
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author name string
Christine Evrard
series ordinal
1
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Arnaud Capron
series ordinal
2
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Cécile Marchand
series ordinal
3
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André Clippe
series ordinal
4
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Ruddy Wattiez
series ordinal
5
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Patrice Soumillion
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6
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Bernard Knoops
series ordinal
7
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Jean-Paul Declercq
series ordinal
8
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language of work or name
English
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publication date
9 April 2004
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published in
Journal of Molecular Biology
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volume
337
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issue
5
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page(s)
1079-90
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cites work
Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis
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The structure of reduced tryparedoxin peroxidase reveals a decamer and insight into reactivity of 2Cys-peroxiredoxins
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Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution
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Solvent content of protein crystals
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Glutathione and trypanothione in parasitic hydroperoxide metabolism
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Structure, mechanism and regulation of peroxiredoxins
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Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution
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Thioredoxin--a fold for all reasons
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Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.
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Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase.
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Automated protein model building combined with iterative structure refinement
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Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
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Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution
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A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro
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Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
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Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro
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Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family
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Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate
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An antisense oligonucleotide to 1-cys peroxiredoxin causes lipid peroxidation and apoptosis in lung epithelial cells
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Identifiers
DOI
10.1016/J.JMB.2004.02.017
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PubMed ID
15046979
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ResearchGate publication ID
8653834
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