scholarly journals Inside Cover: Rational Design of Ruthenium Complexes Containing 2,6-Bis(benzimidazolyl)pyridine Derivatives with Radiosensitization Activity by Enhancing p53 Activation (ChemMedChem 6/2015)

ChemMedChem ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. 934-934
Author(s):  
Zhiqin Deng ◽  
Lianling Yu ◽  
Wenqiang Cao ◽  
Wenjie Zheng ◽  
Tianfeng Chen

ChemMedChem ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. 991-998 ◽  
Author(s):  
Zhiqin Deng ◽  
Lianling Yu ◽  
Wenqiang Cao ◽  
Wenjie Zheng ◽  
Tianfeng Chen


2015 ◽  
Vol 51 (13) ◽  
pp. 2637-2640 ◽  
Author(s):  
Zhiqin Deng ◽  
Lianling Yu ◽  
Wenqiang Cao ◽  
Wenjie Zheng ◽  
Tianfeng Chen

We have described the rational design of selenium-containing ruthenium complexes and their use as cancer radiosensitizers through regulating ROS-mediated pathways.



Synthesis ◽  
2018 ◽  
Vol 50 (23) ◽  
pp. 4555-4568 ◽  
Author(s):  
Janusz Jurczak ◽  
Agnieszka Cholewiak ◽  
Pawel Stepniak

A selective digest of linear anion receptors based on different aromatic skeletons is presented. Since the structures of anions vary from one to another, different strategies have been developed over recent years in order to bind anions efficiently and selectively. Rigidity, number of hydrogen bond donors, steric hindrance, and special preorganization of linear receptors are analyzed to shed light on the rational design of anion receptors.1 Introduction2 1,3- and 1,2-Benzene Derivatives3 1,3- and 5,7-Azulene Derivatives4 1,8-Naphthalene Derivatives5 1,8-Anthracene Derivatives6 2,6-Pyridine Derivatives7 2,5-Pyrrole Derivatives8 Diamidoarenodipyrrole Derivatives9 Carbazole Derivatives10 DITIPIRAM Derivatives11 Conclusion



2011 ◽  
Vol 95 (1) ◽  
pp. 310-314 ◽  
Author(s):  
Nobuko Onozawa-Komatsuzaki ◽  
Masatoshi Yanagida ◽  
Takashi Funaki ◽  
Kazuyuki Kasuga ◽  
Kazuhiro Sayama ◽  
...  


2019 ◽  
Author(s):  
BL Allen ◽  
K Quach ◽  
CB Levandowski ◽  
JD Rubin ◽  
T Read ◽  
...  

AbstractDNA-binding transcription factors (TFs) remain challenging to target with molecular probes. Many TFs function in part through interaction with Mediator; we sought to block p53 function by disrupting the p53-Mediator interaction. Through rational design and activity-based screening, we characterized a stapled peptide, with functional mimics of both p53 activation domains, that selectively inhibited p53- and Mediator-dependent transcription in vitro. This “bivalent peptide” also suppressed p53 transcriptional response in human cancer cells. Our strategy circumvents the TF and instead targets the TF-Mediator interface, with desired transcriptional outcomes. Different TFs target Mediator through different subunits, suggesting this strategy could be broadly applied.



2021 ◽  
pp. 105075
Author(s):  
Ya-Sheng Li ◽  
Shen Mao ◽  
Dong-Sheng Zhao ◽  
Can-Can Wang ◽  
Dan Zu ◽  
...  




ChemInform ◽  
2006 ◽  
Vol 37 (39) ◽  
Author(s):  
Renate Drozdzak ◽  
Nele Ledoux ◽  
Bart Allaert ◽  
Ileana Dragutan ◽  
Valerian Dragutan ◽  
...  


2010 ◽  
Vol 29 (2) ◽  
pp. 417-427 ◽  
Author(s):  
Andrew D. Phillips ◽  
Olivier Zava ◽  
Rosario Scopelitti ◽  
Alexey A. Nazarov ◽  
Paul J. Dyson


2021 ◽  
Vol 23 (1) ◽  
pp. 219-228
Author(s):  
Nabanita Saikia ◽  
Mohamed Taha ◽  
Ravindra Pandey

The rational design of self-assembled nanobio-molecular hybrids of peptide nucleic acids with single-wall nanotubes rely on understanding how biomolecules recognize and mediate intermolecular interactions with the nanomaterial's surface.



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