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10.1371/journal.pone.0178381 http://scihub22266oqcxt.onion/10.1371/journal.pone.0178381 C5453487!5453487 !28570566     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28570566 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       PLoS+One 2017 ; 12 (6 ): e0178381 Nephropedia Template TP {{tp|p=28570566 |t=2017. Targeting YAP/TAZ-TEAD protein-protein interactions using fragment-based and computational modeling approaches |pdf=|usr=}}{{28570566 }} gab.com Text Targeting YAP/TAZ-TEAD protein-protein interactions using fragment-based and computational modeling approaches JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=28570566 #FOAvip The Hippo signaling pathway, which is implicated in the regulation of organ size, has emerged as a potential target for the development of cancer therapeutics. YAP, TAZ (transcription co-activators) and TEAD (transcription factor) are the downstream transcriptional machinery and effectors of the pathway. Formation of the YAP/TAZ-TEAD complex leads to transcription of growth-promoting genes. Conversely, disrupting the interactions of the complex decreases cell proliferation. Herein, we screened a 1000-member fragment library using Thermal Shift Assay and identified a hit fragment. We confirmed its binding at the YAP/TAZ-TEAD interface by X-ray crystallography, and showed that it occupies the same hydrophobic pocket as a conserved phenylalanine of YAP/TAZ. This hit fragment serves as a scaffold for the development of compounds that have the potential to disrupt YAP/TAZ-TEAD interactions. Structure-activity relationship studies and computational modeling were also carried out to identify more potent compounds that may bind at this validated druggable binding site. Twit Text FOAVip Targeting YAP/TAZ-TEAD protein-protein interactions using fragment-based and computational modeling approaches ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=28570566 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28570566 #FOAvip English Wikipedia <ref>{{Cite pmid|28570566 }}</ref> Targeting YAP/TAZ-TEAD protein-protein interactions using fragment-based and computational modeling approaches #MMPMID28570566 Kaan HYK ; Sim AYL ; Tan SKJ ; Verma C ; Song H PLoS One 2017[]; 12 (6 ): e0178381 PMID28570566 show ga The Hippo signaling pathway, which is implicated in the regulation of organ size, has emerged as a potential target for the development of cancer therapeutics. YAP, TAZ (transcription co-activators) and TEAD (transcription factor) are the downstream transcriptional machinery and effectors of the pathway. Formation of the YAP/TAZ-TEAD complex leads to transcription of growth-promoting genes. Conversely, disrupting the interactions of the complex decreases cell proliferation. Herein, we screened a 1000-member fragment library using Thermal Shift Assay and identified a hit fragment. We confirmed its binding at the YAP/TAZ-TEAD interface by X-ray crystallography, and showed that it occupies the same hydrophobic pocket as a conserved phenylalanine of YAP/TAZ. This hit fragment serves as a scaffold for the development of compounds that have the potential to disrupt YAP/TAZ-TEAD interactions. Structure-activity relationship studies and computational modeling were also carried out to identify more potent compounds that may bind at this validated druggable binding site. |*Computer Simulation [MESH] |Animals [MESH] |Calorimetry [MESH] |Crystallography, X-Ray [MESH] |Humans [MESH] |Ligands [MESH] |Mice [MESH] |Protein Binding [MESH] |Structure-Activity Relationship [MESH]Targeting YAP/TAZ-TEAD protein-protein interactions using fragment-bas(epmc).pdf DeepDyve Pubget Overpricing