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10.14348/molcells.2016.2320 http://scihub22266oqcxt.onion/10.14348/molcells.2016.2320 C4870188!4870188!27094059     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cells 2016 ; 39 (5): 403-9 Nephropedia Template TP {{tp|p=27094059|t=2016. Characterization of Functional Domains in NME1L Regulation of NF-?B Signaling |pdf=|usr=}}{{27094059}} gab.com Text Characterization of Functional Domains in NME1L Regulation of NF- B Signaling JO: Mol Cells http://www.kidney.de/pget.php?&tw=1&pmid=27094059 #FOAvip NME1 is a well-known metastasis suppressor which has been reported to be downregulated in some highly aggressive cancer cells. Although most studies have focused on NME1, the NME1 gene also encodes the protein (NME1L) containing N-terminal 25 extra amino acids by alternative splicing. According to previous studies, NME1L has potent anti-metastatic activity, in comparison with NME1, by interacting with IKK? and regulating its activity. In the present study, we tried to define the role of the N-terminal 25 amino acids of NME1L in NF-?B activation signaling. Unfortunately, the sequence itself did not interact with IKK?, suggesting that it may be not enough to constitute the functional structure. Further construction of NME1L fragments and biochemical analysis revealed that N-terminal 84 residues constitute minimal structure for homodimerization, IKK? interaction and regulation of NF-?B signaling. The inhibitory effect of the fragment on cancer cell migration and NF-?B-stimulated gene expression was equivalent to that of whole NME1L. The data suggest that the N-terminal 84 residues may be a core region for the anti-metastatic activity of NME1L. Based on this result, further structural analysis of the binding between NME1L and IKK? may help in understanding the anti-metastatic activity of NME1L and provide direction to NME1L and IKK?-related anti-cancer drug design. Twit Text FOAVip Characterization of Functional Domains in NME1L Regulation of NF- B Signaling ????Mol Cells http://www.kidney.de/pget.php?&tw=1&pmid=27094059 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27094059 #FOAvip English Wikipedia <ref>{{Cite pmid|27094059}}</ref> Characterization of Functional Domains in NME1L Regulation of NF-?B Signaling #MMPMID27094059 You DJ; Park CR; Mander S; Ahn C; Seong JY; Hwang JI Mol Cells 2016[May]; 39 (5): 403-9 PMID27094059show ga NME1 is a well-known metastasis suppressor which has been reported to be downregulated in some highly aggressive cancer cells. Although most studies have focused on NME1, the NME1 gene also encodes the protein (NME1L) containing N-terminal 25 extra amino acids by alternative splicing. According to previous studies, NME1L has potent anti-metastatic activity, in comparison with NME1, by interacting with IKK? and regulating its activity. In the present study, we tried to define the role of the N-terminal 25 amino acids of NME1L in NF-?B activation signaling. Unfortunately, the sequence itself did not interact with IKK?, suggesting that it may be not enough to constitute the functional structure. Further construction of NME1L fragments and biochemical analysis revealed that N-terminal 84 residues constitute minimal structure for homodimerization, IKK? interaction and regulation of NF-?B signaling. The inhibitory effect of the fragment on cancer cell migration and NF-?B-stimulated gene expression was equivalent to that of whole NME1L. The data suggest that the N-terminal 84 residues may be a core region for the anti-metastatic activity of NME1L. Based on this result, further structural analysis of the binding between NME1L and IKK? may help in understanding the anti-metastatic activity of NME1L and provide direction to NME1L and IKK?-related anti-cancer drug design. äCharacterization of Functional Domains in NME1L Regulation of NF-?B Si(epmc).pdf DeepDyve Pubget Overpricing