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10.1039/c6mb00175k http://scihub22266oqcxt.onion/10.1039/c6mb00175k C4955733!4955733 !27216279     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27216279 &cmd=llinks): Failed to open stream: HTTP request failed! 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A clickable glutathione approach for identification of protein glutathionylation in response to glucose metabolism |pdf=|usr=}}{{27216279 }} gab.com Text A clickable glutathione approach for identification of protein glutathionylation in response to glucose metabolism JO: Mol Biosyst http://www.kidney.de/pget.php?&tw=1&pmid=27216279 #FOAvip Glucose metabolism and mitochondrial function are closely interconnected with cellular redox-homeostasis. Although glucose starvation, which mimics ischemic conditions or insufficient vascularization, is known to perturb redox-homeostasis, global and individual protein glutathionylation in response to glucose metabolism or mitochondrial activity remains largely unknown. In this report, we use our clickable glutathione approach, which forms clickable glutathione (azido-glutathione) by using a mutant of glutathione synthetase (GS M4), for detection and identification of protein glutathionylation in response to glucose starvation. We found that protein glutathionylation is readily induced in HEK293 cells in response to low glucose concentrations when mitochondrial reactive oxygen species (ROS) are elevated in cells, and glucose is the major determinant for inducing reversible glutathionylation. Proteomic and biochemical analysis identified over 1300 proteins, including SMYD2, PP2C?, and catalase. We further showed that PP2C? is glutathionylated at C314 in a C-terminal domain, and PP2C? C314 glutathionylation disrupts the interaction with mGluR3, an important glutamate receptor associated with synaptic plasticity. Twit Text FOAVip A clickable glutathione approach for identification of protein glutathionylation in response to glucose metabolism ????Mol Biosyst http://www.kidney.de/pget.php?&tw=1&pmid=27216279 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27216279 #FOAvip English Wikipedia <ref>{{Cite pmid|27216279 }}</ref> A clickable glutathione approach for identification of protein glutathionylation in response to glucose metabolism #MMPMID27216279 Samarasinghe KT ; Munkanatta Godage DN ; Zhou Y ; Ndombera FT ; Weerapana E ; Ahn YH Mol Biosyst 2016[Jul]; 12 (8 ): 2471-80 PMID27216279 show ga Glucose metabolism and mitochondrial function are closely interconnected with cellular redox-homeostasis. Although glucose starvation, which mimics ischemic conditions or insufficient vascularization, is known to perturb redox-homeostasis, global and individual protein glutathionylation in response to glucose metabolism or mitochondrial activity remains largely unknown. In this report, we use our clickable glutathione approach, which forms clickable glutathione (azido-glutathione) by using a mutant of glutathione synthetase (GS M4), for detection and identification of protein glutathionylation in response to glucose starvation. We found that protein glutathionylation is readily induced in HEK293 cells in response to low glucose concentrations when mitochondrial reactive oxygen species (ROS) are elevated in cells, and glucose is the major determinant for inducing reversible glutathionylation. Proteomic and biochemical analysis identified over 1300 proteins, including SMYD2, PP2C?, and catalase. We further showed that PP2C? is glutathionylated at C314 in a C-terminal domain, and PP2C? C314 glutathionylation disrupts the interaction with mGluR3, an important glutamate receptor associated with synaptic plasticity. |*Protein Processing, Post-Translational [MESH] |*Proteomics/methods [MESH] |Catalysis [MESH] |Catalytic Domain [MESH] |Gene Expression [MESH] |Glucose/*metabolism [MESH] |Glutathione Synthase/chemistry/genetics/metabolism [MESH] |Glutathione/*metabolism [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Models, Molecular [MESH] |Mutation [MESH] |Oxidation-Reduction [MESH] |Protein Conformation [MESH] |Protein Interaction Domains and Motifs [MESH] |Protein Phosphatase 2C/chemistry/metabolism [MESH]A clickable glutathione approach for identification of protein glutath(epmc).pdf DeepDyve Pubget Overpricing