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10.1177/1087057114525853 http://scihub22266oqcxt.onion/10.1177/1087057114525853 C4570879!4570879 !24598103     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24598103 &cmd=llinks): Failed to open stream: HTTP request failed! 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Enzymatic Characterization of ER Stress-Dependent Kinase, PERK, and Development of a High-Throughput Assay for Identification of PERK Inhibitors |pdf=|usr=}}{{24598103 }} gab.com Text Enzymatic Characterization of ER Stress-Dependent Kinase, PERK, and Development of a High-Throughput Assay for Identification of PERK Inhibitors JO: J Biomol Screen http://www.kidney.de/pget.php?&tw=1&pmid=24598103 #FOAvip PERK is serine/threonine kinase localized to the endoplasmic reticulum (ER) membrane. PERK is activated and contributes to cell survival in response to a variety of physiological stresses that affect protein quality control in the ER, such as hypoxia, glucose depravation, increased lipid biosynthesis, and increased protein translation. Pro-survival functions of PERK are triggered by such stresses, suggesting that development of small-molecule inhibitors of PERK may be efficacious in a variety of disease scenarios. Hence, we have conducted a detailed enzymatic characterization of the PERK kinase to develop a high-throughput-screening assay (HTS) that will permit the identification of small-molecule PERK inhibitors. In addition to establishing the K(m) of PERK for both its primary substrate, eIF2?, and for adenosine triphosphate, further mechanistic studies revealed that PERK targets its substrate via either a random/steady-state ordered mechanism. For HTS, we developed a time-resolved fluorescence resonance energy transfer-based assay that yielded a robust Z' factor and percent coefficient of variation value, enabling the successful screening of 79,552 compounds. This approach yielded one compound that exhibited good in vitro and cellular activity. These results demonstrate the validity of this screen and represent starting points for drug discovery efforts. Twit Text FOAVip Enzymatic Characterization of ER Stress-Dependent Kinase, PERK, and Development of a High-Throughput Assay for Identification of PERK Inhibitors ????J Biomol Screen http://www.kidney.de/pget.php?&tw=1&pmid=24598103 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24598103 #FOAvip English Wikipedia <ref>{{Cite pmid|24598103 }}</ref> Enzymatic Characterization of ER Stress-Dependent Kinase, PERK, and Development of a High-Throughput Assay for Identification of PERK Inhibitors #MMPMID24598103 Pytel D ; Seyb K ; Liu M ; Ray SS ; Concannon J ; Huang M ; Cuny GD ; Diehl JA ; Glicksman MA J Biomol Screen 2014[Aug]; 19 (7 ): 1024-34 PMID24598103 show ga PERK is serine/threonine kinase localized to the endoplasmic reticulum (ER) membrane. PERK is activated and contributes to cell survival in response to a variety of physiological stresses that affect protein quality control in the ER, such as hypoxia, glucose depravation, increased lipid biosynthesis, and increased protein translation. Pro-survival functions of PERK are triggered by such stresses, suggesting that development of small-molecule inhibitors of PERK may be efficacious in a variety of disease scenarios. Hence, we have conducted a detailed enzymatic characterization of the PERK kinase to develop a high-throughput-screening assay (HTS) that will permit the identification of small-molecule PERK inhibitors. In addition to establishing the K(m) of PERK for both its primary substrate, eIF2?, and for adenosine triphosphate, further mechanistic studies revealed that PERK targets its substrate via either a random/steady-state ordered mechanism. For HTS, we developed a time-resolved fluorescence resonance energy transfer-based assay that yielded a robust Z' factor and percent coefficient of variation value, enabling the successful screening of 79,552 compounds. This approach yielded one compound that exhibited good in vitro and cellular activity. These results demonstrate the validity of this screen and represent starting points for drug discovery efforts. |Animals [MESH] |Computer Simulation [MESH] |Drug Design [MESH] |Drug Discovery/*methods [MESH] |Endoplasmic Reticulum Stress [MESH] |Endoplasmic Reticulum/metabolism [MESH] |Enzyme Inhibitors/*chemistry [MESH] |Eukaryotic Initiation Factor-2/chemistry [MESH] |Fibroblasts/metabolism [MESH] |Fluorescence Resonance Energy Transfer [MESH] |High-Throughput Screening Assays/*methods [MESH] |Humans [MESH] |Mice [MESH] |Phenotype [MESH] |Phosphorylation [MESH] |Signal Transduction [MESH]Enzymatic Characterization of ER Stress-Dependent Kinase, PERK, and De(epmc).pdf DeepDyve Pubget Overpricing