Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1098/rsob.160255 http://scihub22266oqcxt.onion/10.1098/rsob.160255 C5090066!5090066!27784791     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Open+Biol 2016 ; 6 (10): ä Nephropedia Template TP {{tp|p=27784791|t=2016. An affinity-directed protein missile system for targeted proteolysis |pdf=|usr=}}{{27784791}} gab.com Text An affinity-directed protein missile system for targeted proteolysis JO: Open Biol http://www.kidney.de/pget.php?&tw=1&pmid=27784791 #FOAvip The von Hippel?Lindau (VHL) protein serves to recruit the hypoxia-inducible factor alpha (HIF1?) protein under normoxia to the CUL2 E3 ubiquitin ligase for its ubiquitylation and degradation through the proteasome. In this report, we modify VHL to engineer an affinity-directed protein missile (AdPROM) system to direct specific endogenous target proteins for proteolysis in mammalian cells. The proteolytic AdPROM construct harbours a cameloid anti-green fluorescence protein (aGFP) nanobody that is fused to VHL for either constitutive or tetracycline-inducible expression. For target proteins, we exploit CRISPR/Cas9 to rapidly generate human kidney HEK293 and U2OS osteosarcoma homozygous knock-in cells harbouring GFP tags at the VPS34 (vacuolar protein sorting 34) and protein associated with SMAD1 (PAWS1, aka FAM83G) loci, respectively. Using these cells, we demonstrate that the expression of the VHL-aGFP AdPROM system results in near-complete degradation of the endogenous GFP-VPS34 and PAWS1-GFP proteins through the proteasome. Additionally, we show that Tet-inducible destruction of GFP-VPS34 results in the degradation of its associated partner, UVRAG, and reduction in levels of cellular phosphatidylinositol 3-phosphate. Twit Text FOAVip An affinity-directed protein missile system for targeted proteolysis ????Open Biol http://www.kidney.de/pget.php?&tw=1&pmid=27784791 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27784791 #FOAvip English Wikipedia <ref>{{Cite pmid|27784791}}</ref> An affinity-directed protein missile system for targeted proteolysis #MMPMID27784791 Fulcher LJ; Macartney T; Bozatzi P; Hornberger A; Rojas-Fernandez A; Sapkota GP Open Biol 2016[Oct]; 6 (10): ä PMID27784791show ga The von Hippel?Lindau (VHL) protein serves to recruit the hypoxia-inducible factor alpha (HIF1?) protein under normoxia to the CUL2 E3 ubiquitin ligase for its ubiquitylation and degradation through the proteasome. In this report, we modify VHL to engineer an affinity-directed protein missile (AdPROM) system to direct specific endogenous target proteins for proteolysis in mammalian cells. The proteolytic AdPROM construct harbours a cameloid anti-green fluorescence protein (aGFP) nanobody that is fused to VHL for either constitutive or tetracycline-inducible expression. For target proteins, we exploit CRISPR/Cas9 to rapidly generate human kidney HEK293 and U2OS osteosarcoma homozygous knock-in cells harbouring GFP tags at the VPS34 (vacuolar protein sorting 34) and protein associated with SMAD1 (PAWS1, aka FAM83G) loci, respectively. Using these cells, we demonstrate that the expression of the VHL-aGFP AdPROM system results in near-complete degradation of the endogenous GFP-VPS34 and PAWS1-GFP proteins through the proteasome. Additionally, we show that Tet-inducible destruction of GFP-VPS34 results in the degradation of its associated partner, UVRAG, and reduction in levels of cellular phosphatidylinositol 3-phosphate. äAn affinity-directed protein missile system for targeted proteolysis (epmc).pdf DeepDyve Pubget Overpricing