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10.1042/BST20170506 http://scihub22266oqcxt.onion/10.1042/BST20170506 C6008590!6008590!29802218     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       Biochem+Soc+Trans 2018 ; 46 (3): 721-8 Nephropedia Template TP {{tp|p=29802218|t=2018. Coenzyme A, protein CoAlation and redox regulation in mammalian cells |pdf=|usr=}}{{29802218}} gab.com Text Coenzyme A, protein CoAlation and redox regulation in mammalian cells JO: Biochem Soc Trans http://www.kidney.de/pget.php?&tw=1&pmid=29802218 #FOAvip In a diverse family of cellular cofactors, coenzyme A (CoA) has a unique design to function in various biochemical processes. The presence of a highly reactive thiol group and a nucleotide moiety offers a diversity of chemical reactions and regulatory interactions. CoA employs them to activate carbonyl-containing molecules and to produce various thioester derivatives (e.g. acetyl CoA, malonyl CoA and 3-hydroxy-3-methylglutaryl CoA), which have well-established roles in cellular metabolism, production of neurotransmitters and the regulation of gene expression. A novel unconventional function of CoA in redox regulation, involving covalent attachment of this coenzyme to cellular proteins in response to oxidative and metabolic stress, has been recently discovered and termed protein CoAlation (S-thiolation by CoA or CoAthiolation). A diverse range of proteins was found to be CoAlated in mammalian cells and tissues under various experimental conditions. Protein CoAlation alters the molecular mass, charge and activity of modified proteins, and prevents them from irreversible sulfhydryl overoxidation. This review highlights the role of a key metabolic integrator CoA in redox regulation in mammalian cells and provides a perspective of the current status and future directions of the emerging field of protein CoAlation. Twit Text FOAVip Coenzyme A, protein CoAlation and redox regulation in mammalian cells ????Biochem Soc Trans http://www.kidney.de/pget.php?&tw=1&pmid=29802218 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29802218 #FOAvip English Wikipedia <ref>{{Cite pmid|29802218}}</ref> Coenzyme A, protein CoAlation and redox regulation in mammalian cells #MMPMID29802218 Gout I Biochem Soc Trans 2018[Jun]; 46 (3): 721-8 PMID29802218show ga In a diverse family of cellular cofactors, coenzyme A (CoA) has a unique design to function in various biochemical processes. The presence of a highly reactive thiol group and a nucleotide moiety offers a diversity of chemical reactions and regulatory interactions. CoA employs them to activate carbonyl-containing molecules and to produce various thioester derivatives (e.g. acetyl CoA, malonyl CoA and 3-hydroxy-3-methylglutaryl CoA), which have well-established roles in cellular metabolism, production of neurotransmitters and the regulation of gene expression. A novel unconventional function of CoA in redox regulation, involving covalent attachment of this coenzyme to cellular proteins in response to oxidative and metabolic stress, has been recently discovered and termed protein CoAlation (S-thiolation by CoA or CoAthiolation). A diverse range of proteins was found to be CoAlated in mammalian cells and tissues under various experimental conditions. Protein CoAlation alters the molecular mass, charge and activity of modified proteins, and prevents them from irreversible sulfhydryl overoxidation. This review highlights the role of a key metabolic integrator CoA in redox regulation in mammalian cells and provides a perspective of the current status and future directions of the emerging field of protein CoAlation. äCoenzyme A, protein CoAlation and redox regulation in mammalian cells (epmc).pdf DeepDyve Pubget Overpricing