Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Klaus Kis"'
Autor:
Sebastian Bertram, Arturo Blazquez-Navarro, Maximilian Seidel, Bodo Hölzer, Felix S. Seibert, Adrian Doevelaar, Benjamin Rohn, Panagiota Zgoura, Alexandra Witte-Lack, Sarah Skrzypczyk, David Scholten, Klaus Kisters, Nina Babel, Timm H. Westhoff
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-5 (2022)
Abstract Healthcare workers are at substantially increased risk for infection with SARS-CoV-2. Successful vaccination constitutes a crucial prerequisite to protect this group during the pandemic. Since post vaccination antibody monitoring is not stan
Externí odkaz:
https://doaj.org/article/c6be70520d8047f1ad3dd231cdbe7ddf
Autor:
Felix Rohdich, Meinhart H. Zenk, Stefan Hecht, Monika Fellermeier, Adelbert Bacher, Christoph A. Schuhr, Juraithip Wungsintaweekul, Sylvia Sagner, Klaus Kis
Publikováno v:
Acta Horticulturae. :115-122
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::307064e91cf97fdbd62c0ba84273af6d
https://doi.org/10.17660/actahortic.2005.677.15
https://doi.org/10.17660/actahortic.2005.677.15
Autor:
Rudolf Ladenstein, Nicholas Schramek, Markus Fischer, Robert Huber, Winfried Meining, Ilka Haase, Klaus Kis, Adelbert Bacher, Mark Cushman
Publikováno v:
Journal of Molecular Biology. 326:783-793
6,7-Dimethyl-8-ribityllumazine synthase (lumazine synthase) catalyses the penultimate step in the biosynthesis of riboflavin. In Bacillus subtilis, 60 lumazine synthase subunits form an icosahedral capsid enclosing a homotrimeric riboflavin synthase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccc442a632e7dc0fd408c8d636d6ef22
https://doi.org/10.1016/s0022-2836(02)01473-0
https://doi.org/10.1016/s0022-2836(02)01473-0
Autor:
Stefan Hecht, Klaus Kis, Felix Rohdich, Viola Trentinaglia, Sabine Amslinger, Petra Adam, Johann Jauch, Adelbert Bacher, Wolfgang Eisenreich
Publikováno v:
Tetrahedron Letters. 43:8929-8933
(E)-1-Hydroxy-2-methylbut-2-enyl 4-diphosphate (6) has been recently detected as an intermediate of isoprenoid biosynthesis via 1-deoxy-D-xylulose 5-phosphate. The compound was synthesized in two steps from 2-methyl-2-vinyloxirane with an overall yie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9e0ddbfd1b3091c352376905909ad23d
https://doi.org/10.1016/s0040-4039(02)02195-0
https://doi.org/10.1016/s0040-4039(02)02195-0
Autor:
Sabine Amslinger, Stefan Hecht, Petra Adam, Felix Rohdich, Duilio Arigoni, Adelbert Bacher, Wolfgang Eisenreich, Klaus Kis
Publikováno v:
Proceedings of the National Academy of Sciences. 98:14837-14842
Recombinant Escherichia coli cells engineered for the expression of the xylB gene in conjunction with genes of the nonmevalonate pathway were supplied with 13 C-labeled 1-deoxy- d -xylulose. Cell extracts were analyzed directly by NMR spectroscopy. 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9480aa2ca70c4feaaf034f1845970746
https://doi.org/10.1073/pnas.201399298
https://doi.org/10.1073/pnas.201399298
Autor:
Wolfgang Eisenreich, Stefan Hecht, Duilio Arigoni, Meinhart H. Zenk, Petra Adam, Felix Rohdich, Maja Raschke, Adelbert Bacher, Monika Fellermeier, Silvia Sagner, Christoph A. Schuhr, Klaus Kis, Juraithip Wungsintaweekul, Tanja Radykewicz
Publikováno v:
European Journal of Biochemistry. 268:6302-6310
2C-methyl-D-erythritol 2,4-cyclodiphosphate was recently shown to be formed from 2C-methyl-D-erythritol 4-phosphate by the consecutive action of IspD, IspE, and IspF proteins in the nonmevalonate pathway of terpenoid biosynthesis. To complement previ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98bec13cc624b60c9d9a86f36a8ae947
https://doi.org/10.1046/j.0014-2956.2001.02585.x
https://doi.org/10.1046/j.0014-2956.2001.02585.x
Autor:
Stefan Hecht, Christoph A. Schuhr, Tanja Radykewicz, Wolfgang Eisenreich, Adelbert Bacher, Gerald Richter, Felix Rohdich, Juraithip Wungsintaweekul, Klaus Kis
Publikováno v:
The Journal of Organic Chemistry. 66:7770-7775
This paper describes the recombinant expression of the ispC gene of Escherichia coli specifying 2C-methyl-D-erythritol 4-phosphate synthase in a modified form that can be purified efficiently by metal-chelating chromatography. The enzyme was used for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b67c2ef54f5fc8b6806cb890d0512c4
https://doi.org/10.1021/jo015890v
https://doi.org/10.1021/jo015890v
Autor:
Juraithip Wungsintaweekul, Meinhart H. Zenk, Klaus Kis, Wolfgang Eisenreich, Felix Rohdich, Tanja Radykewicz, Adelbert Bacher, Duilio Arigoni, Stefan Herz
Publikováno v:
FEBS Letters. 465:157-160
1-Deoxy-D-xylulose-5-phosphate is converted into 2-C-methyl-D-erythritol-4-phosphate by the catalytic action of 1-deoxy-D-xylulose-5-phosphate reductoisomerase (Dxr protein) using NADPH as cofactor. The stereochemical features of this reaction were i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc216d2f27edaee9cea76588d6d64d5f
https://doi.org/10.1016/s0014-5793(99)01743-3
https://doi.org/10.1016/s0014-5793(99)01743-3
Publikováno v:
The Journal of Organic Chemistry. 64:4635-4642
The reaction catalyzed by riboflavin synthase utilizes two identical 6,7-dimethyl-8-D-ribityllumazine substrate molecules. Three bis(6,7-dimethyl-8-D-ribityllumazines) were, therefore, synthesized in which the two lumazine moieties were connected thr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb802aa1e278ac38ddebbe23bf931fb7
https://doi.org/10.1021/jo9821731
https://doi.org/10.1021/jo9821731
Publikováno v:
The Journal of Organic Chemistry. 64:3838-3845
Three phosphonic acid inhibitors of lumazine synthase were synthesized in which the phosphorus atom was separated from the pyrimidinedione ring by polymethylene linker chains containing four, five, and six carbon atoms. Three analogous sulfonic acids
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d1138e661bb1e7c80db285d9a1df66b
https://doi.org/10.1021/jo9821729
https://doi.org/10.1021/jo9821729