Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases
Baier M, Dietz K-J (1996)
Plant Mol. Biol. 31(3): 553-564.
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Autor*in
Baier, Margarete;
Dietz, Karl-JosefUniBi
Erscheinungsjahr
1996
Zeitschriftentitel
Plant Mol. Biol.
Band
31
Ausgabe
3
Seite(n)
553-564
ISSN
0167-4412
eISSN
1573-5028
Page URI
https://pub.uni-bielefeld.de/record/1866567
Zitieren
Baier M, Dietz K-J. Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol. 1996;31(3):553-564.
Baier, M., & Dietz, K. - J. (1996). Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol., 31(3), 553-564. https://doi.org/10.1007/BF00042228
Baier, Margarete, and Dietz, Karl-Josef. 1996. “Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases”. Plant Mol. Biol. 31 (3): 553-564.
Baier, M., and Dietz, K. - J. (1996). Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol. 31, 553-564.
Baier, M., & Dietz, K.-J., 1996. Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol., 31(3), p 553-564.
M. Baier and K.-J. Dietz, “Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases”, Plant Mol. Biol., vol. 31, 1996, pp. 553-564.
Baier, M., Dietz, K.-J.: Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases. Plant Mol. Biol. 31, 553-564 (1996).
Baier, Margarete, and Dietz, Karl-Josef. “Primary structure and expression of plant homologues of animal and fungal thioredoxin-dependent peroxide reductases and bacterial alkyl hydroperoxide reductases”. Plant Mol. Biol. 31.3 (1996): 553-564.
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2-Cys peroxiredoxin BAS1, chloroplastic (UNIPROT: Q96468)
Organism: Hordeum vulgare
Download in FASTA format
Organism: Hordeum vulgare
Download in FASTA format
2-Cys peroxiredoxin BAS1, chloroplastic (UNIPROT: O24364)
Organism: Spinacia oleracea
Download in FASTA format
Organism: Spinacia oleracea
Download in FASTA format
55 Zitationen in Europe PMC
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Physiological relevance of plant 2-Cys peroxiredoxin overoxidation level and oligomerization status.
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The redox-sensitive transcription factor Rap2.4a controls nuclear expression of 2-Cys peroxiredoxin A and other chloroplast antioxidant enzymes.
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Identification of a Gs-protein coupling domain to the beta-adrenoceptor using site-specific synthetic peptides. Carboxyl terminus of Gs alpha is involved in coupling to beta-adrenoceptors.
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Perl-Treves R, Galun E., Plant Mol. Biol. 17(4), 1991
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Perl-Treves R, Galun E., Plant Mol. Biol. 17(4), 1991
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A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins.
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Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.
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Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and homology to thioredoxin reductase and other flavoprotein disulfide oxidoreductases.
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Tartaglia LA, Storz G, Brodsky MH, Lai A, Ames BN., J. Biol. Chem. 265(18), 1990
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Cloning of a housekeeping-type gene (MER5) preferentially expressed in murine erythroleukemia cells.
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Yamamoto T, Matsui Y, Natori S, Obinata M., Gene 80(2), 1989
PMID: 2583515
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