Cover Picture: Effect of Substituents on the Complexation of Aromatic and Quinoid Substrates with Molecular Tweezers and Clips (Eur. J. Org. Chem. 7/2004)

2004 ◽  
Vol 2004 (7) ◽  
pp. 1367-1367
Author(s):  
Frank-Gerrit Klärner ◽  
Jolanta Polkowska ◽  
Jens Panitzky ◽  
Uta P. Seelbach ◽  
Ulrich Burkert ◽  
...  
2004 ◽  
Vol 2004 (7) ◽  
pp. 1405-1423 ◽  
Author(s):  
Frank-Gerrit Klärner ◽  
Jolanta Polkowska ◽  
Jens Panitzky ◽  
Uta P. Seelbach ◽  
Ulrich Burkert ◽  
...  

1979 ◽  
Vol 44 (3) ◽  
pp. 750-755 ◽  
Author(s):  
Josef Pola ◽  
Marie Jakoubková ◽  
Václav Chvalovský

Relative basicity of the oxygen in alkoxysilanes (RO)nSi(CH3)3-n having n = 1-4 and various electrondonating and electronwithdrawing groups R measured as Δν(OH) of phenol due to its interaction with these compounds in CCl4 is shown to be chiefly controlled by the electronic effect of substituents R. Linear regression analysis of the Δν(OH) vs n relatioship for individual series (RO)nSi(CH3)4-n suggests the operation of the polarizability effect of RO groups becoming more important with increasing electronwithdrawing nature of R.


2007 ◽  
Vol 54 (4) ◽  
pp. 853-860 ◽  
Author(s):  
Liang Ding ◽  
Yu-Qi Ding ◽  
Qi-Wen Teng ◽  
Ke Wang

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Annika Meiners ◽  
Sandra Bäcker ◽  
Inesa Hadrović ◽  
Christian Heid ◽  
Christine Beuck ◽  
...  

AbstractSurvivin’s dual function as apoptosis inhibitor and regulator of cell proliferation is mediated via its interaction with the export receptor CRM1. This protein–protein interaction represents an attractive target in cancer research and therapy. Here, we report a sophisticated strategy addressing Survivin’s nuclear export signal (NES), the binding site of CRM1, with advanced supramolecular tweezers for lysine and arginine. These were covalently connected to small peptides resembling the natural, self-complementary dimer interface which largely overlaps with the NES. Several biochemical methods demonstrated sequence-selective NES recognition and interference with the critical receptor interaction. These data were strongly supported by molecular dynamics simulations and multiscale computational studies. Rational design of lysine tweezers equipped with a peptidic recognition element thus allowed to address a previously unapproachable protein surface area. As an experimental proof-of-principle for specific transport signal interference, this concept should be transferable to any protein epitope with a flanking well-accessible lysine.


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