Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Peter Steinert"'
Autor:
Volker Schulze, Jürgen Michna, Harald Meier, Rüdiger Pabst, Doug Watts, Heiner Lang, Peter Steinert
Publikováno v:
wt Werkstattstechnik online. 102:52-55
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::77f8ecfebf49cc5cca970d0dc2eb6e97
https://doi.org/10.37544/1436-4980-2012-1-2-52
https://doi.org/10.37544/1436-4980-2012-1-2-52
Autor:
Leopold Flohé, Everson Nogoceke, Hans-Jürgen Hecht, S.A. Guerrero, Henryk M. Kalisz, Marisa Montemartini, Mahavir Singh, Peter Steinert
Publikováno v:
European Journal of Biochemistry. 259:789-794
Tryparedoxin (TXN) has recently been discovered as a constituent of the complex peroxidase system in the trypanosomatid Crithidia fasciculata [Nogoceke et al. (1997) Biol. Chem. 378, 827-836] where it catalyzes the reduction of a peroxiredoxin-type p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f8c2dd6c743990a1b775941dec21da5
https://doi.org/10.1046/j.1432-1327.1999.00087.x
https://doi.org/10.1046/j.1432-1327.1999.00087.x
Autor:
M. J. M. Alves, Mahavir Singh, Peter Steinert, Henryk M. Kalisz, Marisa Montemartini, Jorge Lopez, Leopold Flohé, S.A. Guerrero, Walter Colli
Publikováno v:
Scopus-Elsevier
Tryparedoxin peroxidase has recently been identified as a constituent of the complex peroxidase system in the trypanosomatid Crithidia fasciculata [Nogoceke E, Gommel DU, Kiess M, Kalisz HM, Flohe L (1997) Biol Chem 378: 827-836]. In trypanosomatids,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aad6edf6a1ceb795e7bfc5043bf1d317
https://doi.org/10.1007/s002530051634
https://doi.org/10.1007/s002530051634
Publikováno v:
Free Radical Biology and Medicine. 27:966-984
Thiol-dependent hydroperoxide metabolism in parasites is reviewed in respect to potential therapeutic strategies. The hydroperoxide metabolism of Crithidia fasciculata has been characterized to comprise a cascade of three enzymes, trypanothione reduc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8189f4fe7d990ddf3aafc8b84e57afed
https://doi.org/10.1016/s0891-5849(99)00172-0
https://doi.org/10.1016/s0891-5849(99)00172-0
Autor:
Manfred Rohde, Peter Steinert, Marisa Montemartini, Leopold Flohé, Everson Nogoceke, Henryk M. Kalisz, Kurt E.J. Dittmar, Mahavir Singh
Publikováno v:
Free Radical Biology and Medicine. 26:844-849
Tryparedoxin I (TXNI) and tryparedoxin peroxidase (TXNPx), novel proteins isolated from Crithidia fasciculata, have been reported to reconstitute a trypanothione peroxidase activity in vitro (Nogoceke, E.; Gommel, D. U.; Kiess, M.; Kalisz, H. M.; Flo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3384876f007095205b1e7dfbdd28cdb4
https://doi.org/10.1016/s0891-5849(98)00263-9
https://doi.org/10.1016/s0891-5849(98)00263-9
Autor:
Antonella Roveri, Peter Steinert, Leopold Flohé, Josef Wissing, Matilde Maiorino, Fulvio Ursini
Publikováno v:
BioFactors. 10:251-256
Selenium deficiency has long been known to be associated with decreased male and female fertility in live stock. The underlying mechanisms may be numerous. As far as female fertility is concerned, impairment of fertilization of ova of selenium-defici
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b34d1127683df6702d5e0c738e0e243
https://doi.org/10.1002/biof.5520100224
https://doi.org/10.1002/biof.5520100224
Autor:
Andrea Hoffmann, Nicole Betat, Gerhard Gross, Marion Ahrens, Dietmar Bächner, Jörg Lauber, Dietmar Schröder, Leopold Flohé, Peter Steinert
Publikováno v:
Developmental Dynamics. 213:398-411
ABmp-dependent in vitro model was used to identify cDNAs during the manifestation of mesenchymal lineages. This model involves the recombinant expression of Bmps (Bmp-2, Bmp-4-7) in murine mesenchymal C3H10T1/2 progenitors, which leads to the differe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8dd3dd15c6f130b9374e38a84862df1a
https://doi.org/10.1002/(sici)1097-0177(199812)213:4<398::aid-aja5>3.0.co
https://doi.org/10.1002/(sici)1097-0177(199812)213:4<398::aid-aja5>3.0.co
Autor:
Michael Kiess, Mahavir Singh, Marisa Montemartini, Everson Nogoceke, Henryk M. Kalisz, Peter Steinert, Leopold Flohé
Publikováno v:
bchm. 379:1137-1142
Tryparedoxin has recently been discovered as a constituent of the trypanosomal peroxidase system catalysing the reduction of a peroxiredoxin-type peroxidase by trypanothione [Nogoceke et al. (1997) Biol. Chem. 378, 827-836] and has attracted interest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::543c1b13c4d7ff6b6d0785362fb850bd
https://doi.org/10.1515/bchm.1998.379.8-9.1137
https://doi.org/10.1515/bchm.1998.379.8-9.1137
Publikováno v:
Phosphorus, Sulfur, and Silicon and the Related Elements. 136:25-42
Selenium-mediated catalysis in the enzymatic reduction of hydroperoxides is reviewed. Out of the growing number of mammalian selenoproteins four are peroxidases. Their common catalytic mechanism involves redox shuttling of a selenocysteine residue in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a121f1c756492498ece332a7e81690e
https://doi.org/10.1080/10426509808545933
https://doi.org/10.1080/10426509808545933
Publikováno v:
BioFactors. 6:311-319
An 11-day embryonic Swiss Webster/NIH mouse cDNA library was screened with a partial murine selenoprotein P cDNA probe and a murine selenoprotein-P-type cDNA 1 clone of 2075 bp lenght was obtained. The clone contained a 5 0 -leader sequence of 132 bp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04f9be963772051cef57854b2f60a284
https://doi.org/10.1002/biof.5520060302
https://doi.org/10.1002/biof.5520060302