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10.1002/prca.201300090 http://scihub22266oqcxt.onion/10.1002/prca.201300090 C4062080!4062080 !24470285     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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24470285 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proteomics+Clin+Appl 2014 ; 8 (5-6 ): 327-37 Nephropedia Template TP {{tp|p=24470285 |t=2014. Carboxypeptidases in disease: insights from peptidomic studies |pdf=|usr=}}{{24470285 }} gab.com Text Carboxypeptidases in disease: insights from peptidomic studies JO: Proteomics Clin Appl http://www.kidney.de/pget.php?&tw=1&pmid=24470285 #FOAvip Carboxypeptidases (CPs) perform many diverse physiological functions by removing C-terminal amino acids from proteins and peptides. Some CPs function in the degradation of proteins in the digestive tract while other enzymes play biosynthetic roles in the formation of neuropeptides and peptide hormones. Another set of CPs modify tubulin by removing amino acids from the C-terminus and from polyglutamyl side chains, thereby altering the properties of microtubules. This review focuses on three CPs: carboxypeptidase E, carboxypeptidase A6, and cytosolic carboxypeptidase 1. Naturally occurring mutations in all three of these enzymes are associated with disease phenotypes, ranging from obesity to epilepsy to neurodegeneration. Peptidomics is a useful tool to investigate the relationship between these mutations and alterations in peptide levels. This technique has also been used to define the function and characteristics of CPs. Results from peptidomics studies have helped to elucidate the function of CPs and clarify the biological underpinnings of pathologies by identifying peptides altered in disease states. This review describes the use of peptidomic techniques to gain insights into the normal function of CPs and the molecular defects caused by mutations in the enzymes. Twit Text FOAVip Carboxypeptidases in disease: insights from peptidomic studies ????Proteomics Clin Appl http://www.kidney.de/pget.php?&tw=1&pmid=24470285 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24470285 #FOAvip English Wikipedia <ref>{{Cite pmid|24470285 }}</ref> Carboxypeptidases in disease: insights from peptidomic studies #MMPMID24470285 Sapio MR ; Fricker LD Proteomics Clin Appl 2014[Jun]; 8 (5-6 ): 327-37 PMID24470285 show ga Carboxypeptidases (CPs) perform many diverse physiological functions by removing C-terminal amino acids from proteins and peptides. Some CPs function in the degradation of proteins in the digestive tract while other enzymes play biosynthetic roles in the formation of neuropeptides and peptide hormones. Another set of CPs modify tubulin by removing amino acids from the C-terminus and from polyglutamyl side chains, thereby altering the properties of microtubules. This review focuses on three CPs: carboxypeptidase E, carboxypeptidase A6, and cytosolic carboxypeptidase 1. Naturally occurring mutations in all three of these enzymes are associated with disease phenotypes, ranging from obesity to epilepsy to neurodegeneration. Peptidomics is a useful tool to investigate the relationship between these mutations and alterations in peptide levels. This technique has also been used to define the function and characteristics of CPs. Results from peptidomics studies have helped to elucidate the function of CPs and clarify the biological underpinnings of pathologies by identifying peptides altered in disease states. This review describes the use of peptidomic techniques to gain insights into the normal function of CPs and the molecular defects caused by mutations in the enzymes. |*Disease [MESH] |Animals [MESH] |Carboxypeptidases/*metabolism [MESH] |Humans [MESH] |Peptides/*metabolism [MESH]Carboxypeptidases in disease: insights from peptidomic studies (epmc).pdf DeepDyve Pubget Overpricing