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Moreover, this process can be reversibly controlled by addition or sequestration of copper II cations, which capture the ligand in a non-DNA-binding, dinuclear metal complex. This mechanism allows implementation of reversible DNA switches and machines.
Recognition of abasic sites and inhibition of DNA repair: Small-molecule recognition of another type of DNA pairing defects, namely abasic sites , can be harnessed to induce modulation of enzymatic DNA repair pathways. Thus, substrate masking by non-covalent abasic-site ligands represents an attractive strategy for inhibition of APE1.
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Thus, these ligands can be considered as promising modulators of cellular DNA repair pathways and represent a potential for anti-cancer therapy in a combination with DNA-targeting drugs. Development of fluorescent probes for G-quadruplex G4 DNA and RNA structures remains an active research area due to the high biological importance of these non-canonical nucleic acid structures, which is still far from being fully understood.
Along these lines, we demonstrated that 2,4-distyrylpyridinium dyes e.
Additionally, we established a novel bimodal colorimetric and fluorimetric probe BCVP , useful for robust in vitro detection of G4-DNA structures irrespective of their topology and their discrimination from other DNA forms. This involves recognition of the substrate protein and the actions of a succession of proteins on it. Current evidence points to a role for p97 in the identification and possible subsequent partial unfolding or disassembly of a given protein or protein complex.
In the UPS, for example, this could be the disassembly of ubiquitinated proteins from unmodified proteins, prior to capture by the following interacting protein. It appears that this functionality possibly extends to other cellular processes that p97 participates in, such as post-mitotic membrane fusion.
Progress in Nucleic Acid Research and Molecular Biology, Volume 69 - 1st Edition
In this chapter we will give an overview of these p97 interacting proteins and detail how p97 targets ubiquitin-modified proteins in cellular processes such as ERAD. This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.