Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Katrin Fischer‐Schrader"'
Publikováno v:
Plants, Vol 8, Iss 3, p 67 (2019)
Nitrate reductase (NR) is important for higher land plants, as it catalyzes the rate-limiting step in the nitrate assimilation pathway, the two-electron reduction of nitrate to nitrite. Furthermore, it is considered to be a major enzymatic source of
Externí odkaz:
https://doaj.org/article/bd3a876220f542f093ec76aadcf8d04d
Publikováno v:
PLoS ONE, Vol 9, Iss 1, p e86030 (2014)
Molybdenum and tungsten cofactors share a similar pterin-based scaffold, which hosts an ene-dithiolate function being essential for the coordination of either molybdenum or tungsten. The biosynthesis of both cofactors involves a multistep pathway, wh
Externí odkaz:
https://doaj.org/article/099532fd6ff640b39ebd34ff9adc3b07
Five molybdenum-dependent enzymes are known in eukaryotes. While four of them are under investigation since decades, the most recently discovered, (mitochondrial) amidoxime reducing component ((m)ARC), has only been characterized in mammals and the g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fe8343c361e083618dabd0add412cf8
Autor:
Markus Schwarzländer, Regina Wehler, Andrew E Maclean, Peter Dörmann, Luca Pedroletti, Janneke Balk, Markus Wirtz, Rüdiger Hell, Stephan Wagner, Andreas J. Meyer, Marina Franceschetti, Anna Moseler, Inga Kruse, Tatjana M. Hildebrandt, Katrin Fischer-Schrader, Gernot Poschet
Publikováno v:
Plant Physiol
Iron–sulfur (Fe–S) clusters are ubiquitous cofactors in all life and are used in a wide array of diverse biological processes, including electron transfer chains and several metabolic pathways. Biosynthesis machineries for Fe–S clusters exist i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc366bad09de06a2812be090b32cee18
https://pubmed.ncbi.nlm.nih.gov/33856472
https://pubmed.ncbi.nlm.nih.gov/33856472
Autor:
Andrew E Maclean, Ruediger Hell, Markus Schwarzländer, Luca Pedroletti, Tatjana M. Hildebrandt, Andreas J. Meyer, Stephan Wagner, Gernot Poschet, Janneke Balk, Regina Wehler, Markus Wirtz, Anna Moseler, Katrin Fischer-Schrader, Peter Dörmann, Inga Kruse
Iron-sulfur (Fe-S) clusters are ubiquitous cofactors in all life and are used in a wide array of diverse biological processes, including electron transfer chains and several metabolic pathways. Biosynthesis machineries for Fe-S clusters exist in plas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feff27b57f51625aa008dc724acd3d58
https://doi.org/10.1101/2020.02.13.947697
https://doi.org/10.1101/2020.02.13.947697
Autor:
Ella Nukarinen, Markus Teige, Wolfram Weckwerth, Bernhard Wurzinger, Katrin Fischer-Schrader, Andrea Mair, Valentin Roustan
Publikováno v:
Febs Letters
The evolutionarily highly conserved SNF1-related protein kinase (SnRK1) protein kinase is a metabolic master regulator in plants, balancing the critical energy consumption between growth- and stress response-related metabolic pathways. While the regu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92520c96f5827a0d3c76d1bde179aa9f
http://europepmc.org/articles/PMC5698759
http://europepmc.org/articles/PMC5698759
Autor:
Jennifer M McGarry, Joseph Sallmen, Joseph R. McCormick, Partha Basu, Breeanna Mintmier, Günter Schwarz, John F. Stolz, Daniel J. Bain, Courtney Sparacino-Watkins, Axel Magalon, Katrin Fischer-Schrader
Publikováno v:
FEMS Microbiology Letters
FEMS Microbiology Letters, Wiley-Blackwell, 2018, 365 (16), ⟨10.1093/femsle/fny151⟩
FEMS Microbiology Letters, 2018, 365 (16), ⟨10.1093/femsle/fny151⟩
FEMS Microbiology Letters, Wiley-Blackwell, 2018, 365 (16), ⟨10.1093/femsle/fny151⟩
FEMS Microbiology Letters, 2018, 365 (16), ⟨10.1093/femsle/fny151⟩
Campylobacter jejuni, a human gastrointestinal pathogen, uses nitrate for growth under microaerophilic conditions using periplasmic nitrate reductase (Nap). The catalytic subunit, NapA, contains two prosthetic groups, an iron sulfur cluster and a mol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d8372ac5f1fedbb92c3ecc337d6310e
https://hal-amu.archives-ouvertes.fr/hal-01919478
https://hal-amu.archives-ouvertes.fr/hal-01919478
Publikováno v:
Plants
Volume 8
Issue 3
Plants, Vol 8, Iss 3, p 67 (2019)
Volume 8
Issue 3
Plants, Vol 8, Iss 3, p 67 (2019)
Nitrate reductase (NR) is important for higher land plants, as it catalyzes the rate-limiting step in the nitrate assimilation pathway, the two-electron reduction of nitrate to nitrite. Furthermore, it is considered to be a major enzymatic source of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4e7883055462bb33ab3af7e38931cc1
https://doi.org/10.3390/plants8030067
https://doi.org/10.3390/plants8030067
Autor:
Juliane Roeper, Guenter Schwarz, Jen-Chih Chi, Dimitri Niks, Iris C. Lambeck, Russ Hille, Katrin Fischer-Schrader
Publikováno v:
Journal of Biological Chemistry. 287:4562-4571
14-3-3 proteins regulate key processes in eukaryotic cells including nitrogen assimilation in plants by tuning the activity of nitrate reductase (NR), the first and rate-limiting enzyme in this pathway. The homodimeric NR harbors three cofactors, eac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9462cb87c4f899b00c15f7dc506c3566
https://doi.org/10.1074/jbc.m111.323113
https://doi.org/10.1074/jbc.m111.323113
Autor:
Eric E. Kelley, Venkata Ragireddy, Sheila Frizzell, Ling Wang, Yingze Zhang, Mark T. Gladwin, Guenter Schwarz, Dimitri Niks, Courtney Sparacino-Watkins, Sabina Krizowski, Partha Basu, Jesús Tejero, Katrin Fischer-Schrader, Jun Wang, Russ Hille
Publikováno v:
Antioxidants & redox signaling, vol 23, iss 4
Aims: Recent studies suggest that the molybdenum enzymes xanthine oxidase, aldehyde oxidase, and mARC exhibit nitrite reductase activity at low oxygen pressures. However, inhibition studies of xanthine oxidase in humans have failed to block nitrite-d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ad9351bcb6a2fbd7f0007574edd27c7
https://europepmc.org/articles/PMC4523048/
https://europepmc.org/articles/PMC4523048/