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pro vyhledávání: '"Constanze Wilch"'
Autor:
Utta Berchner-Pfannschmidt, Peter Talbiersky, Thomas Schrader, Frank-Gerrit Klärner, Michael Kirsch, Torsten Schaller, Constanze Wilch
Publikováno v:
European Journal of Organic Chemistry. 2017:2223-2229
Inhibition of the key enzyme for DNA quality control, i.e. PARP-1, by synthetic molecular tweezers is demonstrated via a non-competitive mechanism with an IC50 value of 3 µM. Electrophoretic mobility shift assays and molecular docking experiments po
Autor:
Thomas Schrader, Frank-Gerrit Klärner, Christoph Wölper, Andrea Sowislok, Som Dutt, Constanze Wilch, Thomas Gersthagen
Publikováno v:
European Journal of Organic Chemistry. 2013:7705-7714
Transition from monotopic symmetrical to ditopic unsymmetrical molecular recognition frequently occurs when a general, powerful, but unspecific receptor molecule is transformed into a specific ditopic host. Especially in water, this endeavor is accom
Autor:
Kenny Bravo-Rodriguez, Elsa Sanchez-Garcia, Christian Ochsenfeld, Thomas Schrader, Som Dutt, Thomas Gersthagen, Constanze Wilch, Peter Talbiersky, Matti Hanni, Frank-Gerrit Klärner
Publikováno v:
The Journal of Organic Chemistry. 78:6721-6734
Selective binding of the phosphate-substituted molecular tweezer 1a to protein lysine residues was suggested to explain the inhibition of certain enzymes and the aberrant aggregation of amyloid petide Aβ42 or α-synuclein, which are assumed to be re
Autor:
Rolf Rose, Kenny Bravo-Rodriguez, Elsa Sanchez-Garcia, Thomas Schrader, Maria Bartel, Som Dutt, David Bier, Constanze Wilch, Juan Manuel Ramírez-Anguita, Christian Ottmann, Frank-Gerrit Klärner
Publikováno v:
Nature Chemistry, 5(3), 234-239. Nature Publishing Group
Supramolecular chemistry has recently emerged as a promising way to modulate protein functions, but devising molecules that will interact with a protein in the desired manner is difficult as many competing interactions exist in a biological environme
Publikováno v:
ChemInform. 42
This article discusses most recent work and progress in the direction of a rational design of small molecule receptors that efficiently interfere with the biological function of a particular receptor or enzyme—some of which are therapeutically rele
This article discusses most recent work and progress in the direction of a rational design of small molecule receptors that efficiently interfere with the biological function of a particular receptor or enzyme-some of which are therapeutically releva
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3604e139ede4da4b2002cd7c2052d91
https://www.ncbi.nlm.nih.gov/pubmed/21394349
https://www.ncbi.nlm.nih.gov/pubmed/21394349
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