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10.2147/IJN.S114705 http://scihub22266oqcxt.onion/10.2147/IJN.S114705 C5012629!5012629!27621617     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Int+J+Nanomedicine 2016 ; 11 (ä): 4221-9 Nephropedia Template TP {{tp|p=27621617|t=2016. MDM2?MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance |pdf=|usr=}}{{27621617}} gab.com Text MDM2 MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance JO: Int J Nanomedicine http://www.kidney.de/pget.php?&tw=1&pmid=27621617 #FOAvip Murine double minute 2 (MDM2) and 4 (MDM4) are known as the main negative regulators of p53, a tumor suppressor. They are able to form heterodimers that are much more effective in the downregulation of p53. Therefore, the MDM2?MDM4 complex could be a target for promising therapeutic restoration of p53 function. To this aim, a deeper understanding of the molecular mechanisms underlining the heterodimerization is needed. The kinetic and thermodynamic characterization of the MDM2?MDM4 complex was performed with two complementary approaches: atomic force spectroscopy and surface plasmon resonance. Both techniques revealed an equilibrium dissociation constant (KD) in the micromolar range for the MDM2?MDM4 heterodimer, similar to related complexes involved in the p53 network. Furthermore, the MDM2?MDM4 complex is characterized by a relatively high free energy, through a single energy barrier, and by a lifetime in the order of tens of seconds. New insights into the MDM2?MDM4 interaction could be highly important for developing innovative anticancer drugs focused on p53 reactivation. Twit Text FOAVip MDM2 MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance ????Int J Nanomedicine http://www.kidney.de/pget.php?&tw=1&pmid=27621617 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27621617 #FOAvip English Wikipedia <ref>{{Cite pmid|27621617}}</ref> MDM2?MDM4 molecular interaction investigated by atomic force spectroscopy and surface plasmon resonance #MMPMID27621617 Moscetti I; Teveroni E; Moretti F; Bizzarri AR; Cannistraro S Int J Nanomedicine 2016[]; 11 (ä): 4221-9 PMID27621617show ga Murine double minute 2 (MDM2) and 4 (MDM4) are known as the main negative regulators of p53, a tumor suppressor. They are able to form heterodimers that are much more effective in the downregulation of p53. Therefore, the MDM2?MDM4 complex could be a target for promising therapeutic restoration of p53 function. To this aim, a deeper understanding of the molecular mechanisms underlining the heterodimerization is needed. The kinetic and thermodynamic characterization of the MDM2?MDM4 complex was performed with two complementary approaches: atomic force spectroscopy and surface plasmon resonance. Both techniques revealed an equilibrium dissociation constant (KD) in the micromolar range for the MDM2?MDM4 heterodimer, similar to related complexes involved in the p53 network. Furthermore, the MDM2?MDM4 complex is characterized by a relatively high free energy, through a single energy barrier, and by a lifetime in the order of tens of seconds. New insights into the MDM2?MDM4 interaction could be highly important for developing innovative anticancer drugs focused on p53 reactivation. äMDM2?MDM4 molecular interaction investigated by atomic force spectrosc(epmc).pdf DeepDyve Pubget Overpricing