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10.1530/JME-15-0266 http://scihub22266oqcxt.onion/10.1530/JME-15-0266 C4899100!4899100!26667899     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Mol+Endocrinol 2016 ; 56 (4): T63-76 Nephropedia Template TP {{tp|p=26667899|t=2016. 60 YEARS OF POMC: From POMC and ?MSH to PAM, molecular oxygen, copper and vitamin C |pdf=|usr=}}{{26667899}} gab.com Text 60 YEARS OF POMC: From POMC and MSH to PAM, molecular oxygen, copper and vitamin C JO: J Mol Endocrinol http://www.kidney.de/pget.php?&tw=1&pmid=26667899 #FOAvip A critical role for peptide C-terminal amidation was apparent when the first bioactive peptides were identified. The conversion of POMC into ACTH and then into ?MSH, an amidated peptide, provided a model system for identifying the amidating enzyme. Peptidylglycine ?-amidating monooxygenase (PAM), the only enzyme that catalyzes this modification, is essential; mice lacking PAM survive only until mid-gestation. Purification and cloning led to the discovery that the amidation of peptidylglycine substrates proceeds in two steps: peptidylglycine ?-hydroxylating monooxygenase (PHM) catalyzes the copper and ascorbate-dependent ?-hydroxylation of the peptidylglycine substrate; peptidyl-?-hydroxyglycine ?-amidating lyase (PAL) cleaves the N-C bond, producing amidated product plus glyoxylate. Both enzymes are contained in the luminal domain of PAM, a type 1 integral membrane protein. The structures of both catalytic cores have been determined, revealing how they interact with metals, molecular oxygen and substrate to catalyze both reactions. Although not essential for activity, the intrinsically disordered cytosolic domain is essential for PAM trafficking. A phylogenetic survey led to identification of bifunctional membrane PAM in Chlamydomonas, a unicellular eukaryote. Accumulating evidence points to a role for PAM in copper homeostasis and in retrograde signaling from the lumen of the secretory pathway to the nucleus. The discovery of PAM in cilia, cellular antennae that sense and respond to environmental stimuli, suggests that much remains to be learned about this ancient protein. Twit Text FOAVip 60 YEARS OF POMC: From POMC and MSH to PAM, molecular oxygen, copper and vitamin C ????J Mol Endocrinol http://www.kidney.de/pget.php?&tw=1&pmid=26667899 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26667899 #FOAvip English Wikipedia <ref>{{Cite pmid|26667899}}</ref> 60 YEARS OF POMC: From POMC and ?MSH to PAM, molecular oxygen, copper and vitamin C #MMPMID26667899 Kumar D; Mains RE; Eipper BA J Mol Endocrinol 2016[May]; 56 (4): T63-76 PMID26667899show ga A critical role for peptide C-terminal amidation was apparent when the first bioactive peptides were identified. The conversion of POMC into ACTH and then into ?MSH, an amidated peptide, provided a model system for identifying the amidating enzyme. Peptidylglycine ?-amidating monooxygenase (PAM), the only enzyme that catalyzes this modification, is essential; mice lacking PAM survive only until mid-gestation. Purification and cloning led to the discovery that the amidation of peptidylglycine substrates proceeds in two steps: peptidylglycine ?-hydroxylating monooxygenase (PHM) catalyzes the copper and ascorbate-dependent ?-hydroxylation of the peptidylglycine substrate; peptidyl-?-hydroxyglycine ?-amidating lyase (PAL) cleaves the N-C bond, producing amidated product plus glyoxylate. Both enzymes are contained in the luminal domain of PAM, a type 1 integral membrane protein. The structures of both catalytic cores have been determined, revealing how they interact with metals, molecular oxygen and substrate to catalyze both reactions. Although not essential for activity, the intrinsically disordered cytosolic domain is essential for PAM trafficking. A phylogenetic survey led to identification of bifunctional membrane PAM in Chlamydomonas, a unicellular eukaryote. Accumulating evidence points to a role for PAM in copper homeostasis and in retrograde signaling from the lumen of the secretory pathway to the nucleus. The discovery of PAM in cilia, cellular antennae that sense and respond to environmental stimuli, suggests that much remains to be learned about this ancient protein. ä60 YEARS OF POMC: From POMC and ?MSH to PAM, molecular oxygen, copper (epmc).pdf DeepDyve Pubget Overpricing