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10.1681/ASN.2013070760 http://scihub22266oqcxt.onion/10.1681/ASN.2013070760 24511133!4073431!24511133     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Am+Soc+Nephrol 2014 ; 25 (7): 1509-22 Nephropedia Template TP {{tp|p=24511133|t=2014. Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier |pdf=|usr=}}{{24511133}} gab.com Text Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier JO: J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=24511133 #FOAvip Diseases of the kidney filtration barrier are a leading cause of ESRD. Most disorders affect the podocytes, polarized cells with a limited capacity for self-renewal that require tightly controlled signaling to maintain their integrity, viability, and function. Here, we provide an atlas of in vivo phosphorylated, glomerulus-expressed proteins, including podocyte-specific gene products, identified in an unbiased tandem mass spectrometry-based approach. We discovered 2449 phosphorylated proteins corresponding to 4079 identified high-confidence phosphorylated residues and performed a systematic bioinformatics analysis of this dataset. We discovered 146 phosphorylation sites on proteins abundantly expressed in podocytes. The prohibitin homology domain of the slit diaphragm protein podocin contained one such site, threonine 234 (T234), located within a phosphorylation motif that is mutated in human genetic forms of proteinuria. The T234 site resides at the interface of podocin dimers. Free energy calculation through molecular dynamic simulations revealed a role for T234 in regulating podocin dimerization. We show that phosphorylation critically regulates formation of high molecular weight complexes and that this may represent a general principle for the assembly of proteins containing prohibitin homology domains. Twit Text FOAVip Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier ????J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=24511133 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24511133 #FOAvip English Wikipedia <ref>{{Cite pmid|24511133}}</ref> Phosphoproteomic analysis reveals regulatory mechanisms at the kidney filtration barrier #MMPMID24511133 Rinschen MM; Wu X; Konig T; Pisitkun T; Hagmann H; Pahmeyer C; Lamkemeyer T; Kohli P; Schnell N; Schermer B; Dryer S; Brooks BR; Beltrao P; Krueger M; Brinkkoetter PT; Benzing T J Am Soc Nephrol 2014[Jul]; 25 (7): 1509-22 PMID24511133show ga Diseases of the kidney filtration barrier are a leading cause of ESRD. Most disorders affect the podocytes, polarized cells with a limited capacity for self-renewal that require tightly controlled signaling to maintain their integrity, viability, and function. Here, we provide an atlas of in vivo phosphorylated, glomerulus-expressed proteins, including podocyte-specific gene products, identified in an unbiased tandem mass spectrometry-based approach. We discovered 2449 phosphorylated proteins corresponding to 4079 identified high-confidence phosphorylated residues and performed a systematic bioinformatics analysis of this dataset. We discovered 146 phosphorylation sites on proteins abundantly expressed in podocytes. The prohibitin homology domain of the slit diaphragm protein podocin contained one such site, threonine 234 (T234), located within a phosphorylation motif that is mutated in human genetic forms of proteinuria. The T234 site resides at the interface of podocin dimers. Free energy calculation through molecular dynamic simulations revealed a role for T234 in regulating podocin dimerization. We show that phosphorylation critically regulates formation of high molecular weight complexes and that this may represent a general principle for the assembly of proteins containing prohibitin homology domains. |*Proteomics[MESH] |Animals[MESH] |Female[MESH] |Glomerular Filtration Barrier/*physiology[MESH] |Intracellular Signaling Peptides and Proteins/physiology[MESH] |Membrane Proteins/physiology[MESH] |Mice[MESH] |Phosphoproteins/*analysis/*physiology[MESH] |Phosphorylation[MESH]Phosphoproteomic analysis reveals regulatory mechanisms at the kidney (epmc).pdf DeepDyve Pubget Overpricing