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By Stefano Mangani

Disruption of Protein-Protein Interfaces studies the newest advancements and destiny views in drug discovery at protein-protein interfaces. The authors aspect experimental and computational instruments to take on the topic and spotlight the contribution of the Italian examine group to the sector. proof indicates that blocking off or modulating protein-protein interactions may perhaps result in the improvement of valuable new medicines. hence, in recent times nice attempt has been devoted to unveiling the molecular info of protein-protein interfaces by way of structural ideas e.g. X-ray diffraction, NMR spectroscopy. This publication, written and edited via leaders within the box, presents examples from the literature of successes and screw ups to increase drug-like molecules powerful in interacting at protein-protein interfaces

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Popowicz GM, Dömling A, Holak TA (2011) The structure-based design of Mdm2/MDMX– p53 inhibitors gets serious. Angew Chem Int Ed 50:2680–2688 34. Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP (1996) Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274(5289):948–953 35. Popowicz GM, Czarna A, Rothweiler U, Szwagierczak A, Krajewski M, Weber L, Holak TA (2007) Molecular basis for the inhibition of p53 by Mdmx. Cell Cycle 6:2386–2392 36.

Finally, it remains unclear whether the effects of antisense therapies are related to the knockdown of their target or non-specific effects resulting from altered gene regulation. Given these concerns, XIAP antisense therapy may also be hampered in clinical trials. Therefore, there is great interest in developing small-molecule inhibitors of XIAP to overcome the limitations of antisense oligonucleotides [44]. The natural inhibitor of XIAP, SMAC/DIABLO (second mitochondrial activator of caspases/direct IAP-binding protein with Low PI), is a protein that is released from the mitochondria into the cytosol in response to apoptotic stimuli.

Upon the recruitment to a multiprotein structure called the apoptosome, procaspase-9 dimerizes into a catalytically active form that cleaves and activates procaspase-3 and procaspase-7 (Fig. 6) [42]. Apoptosis plays a crucial role in the homeostasis and development of living organisms. Deregulation of this mechanism is associated with many diseases, including several types of cancer. In the apoptosis pathway, the inhibitors of apoptosis proteins (IAPs) are exploited by tumor cells to evade programmed cell death.

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