Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Christoph Patzelt"'
Publikováno v:
Organic Letters. 18:3466-3469
In the presented method, a one-pot metal-free access to β-lactams is provided. The developed strategy employs a hypervalent iodine(III)-triggered bromination/rearrangement/cyclization cascade reaction that allows the straightforward synthesis of a b
Autor:
Christoph Patzelt, Tanja Gulder, Alexander Pöthig, Wolfgang Bettray, Anna Ulmer, Maciej Stodulski, Stefanie V. Kohlhepp
Publikováno v:
Chemistry - A European Journal. 21:1444-1448
A tertiary hydroxy group α to a carboxyl moiety comprises a key structural motif in many bioactive substances. With the herein presented metal-free rearrangement of imides triggered by hypervalent λ(3)-iodane, an easy and selective way to gain acce
Publikováno v:
ChemInform. 47
Autor:
Maciej Stodulski, Wolfgang Bettray, Christoph Patzelt, Stefanie V. Kohlhepp, Tanja Gulder, Anna Ulmer, Alexander Poethig
Publikováno v:
ChemInform. 46
The metal-free rearrangement of imides, catalyzed by in-situ formed trivalent iodine catalysts furnishes brominated α-hydroxycarboxylamides in high yields.
Autor:
Christoph Patzelt, Françoise Assimacopoulos-Jeannet, Bernard Jeanrenaud, Yannick Le Marchand, E. G. Loten
Publikováno v:
Journal of Clinical Investigation. 53:1512-1517
Livers of normal mice were prefused in situ and the secretion of newly synthesized (i.e. labeled) proteins into the perfusate were measured. In control livers, the secretion of newly synthesized proteins was found to be linear with time. In marked co
Autor:
Christoph Patzelt, Gudrun Schug
Publikováno v:
FEBS Letters. (1):127-130
Publikováno v:
European journal of biochemistry. 33(1)
Active form and total activity of pyruvate dehydrogenase were measured in homogenates prepared from tissue samples obtained from the isolated rat liver during perfusion. In the absence of substrate, the active portion accounted for about 20% of total
Publikováno v:
European journal of biochemistry. 26(3)
Active form and total activity of pyruvate dehydrogenase were measured in rat liver homogenates. The activity obtained immediately after homogenization was considered to represent the active form, i.e. dephospho pyruvate dehydrogenase, originally pre
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