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10.1016/j.exer.2015.06.029 http://scihub22266oqcxt.onion/10.1016/j.exer.2015.06.029 C4698099!4698099 !26142952     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26142952 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Exp+Eye+Res 2016 ; 144 (?): 73-80 Nephropedia Template TP {{tp|p=26142952 |t=2016. Optineurin: The autophagy connection |pdf=|usr=}}{{26142952 }} gab.com Text Optineurin: The autophagy connection JO: Exp Eye Res http://www.kidney.de/pget.php?&tw=1&pmid=26142952 #FOAvip Optineurin is a cytosolic protein encoded by the OPTN gene. Mutations of OPTN are associated with normal tension glaucoma and amyotrophic lateral sclerosis. Autophagy is an intracellular degradation system that delivers cytoplasmic components to the lysosomes. It plays a wide variety of physiological and pathophysiological roles. The optineurin protein is a selective autophagy receptor (or adaptor), containing an ubiquitin binding domain with the ability to bind polyubiquitinated cargoes and bring them to autophagosomes via its microtubule-associated protein 1 light chain 3-interacting domain. It is involved in xenophagy, mitophagy, aggrephagy, and tumor suppression. Optineurin can also mediate the removal of protein aggregates through an ubiquitin-independent mechanism. This protein in addition can induce autophagy upon overexpression or mutation. When overexpressed or mutated, the optineurin protein also serves as a substrate for autophagic degradation. In the present review, the multiple connections of optineurin to autophagy are highlighted. Twit Text FOAVip Optineurin: The autophagy connection ????Exp Eye Res http://www.kidney.de/pget.php?&tw=1&pmid=26142952 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26142952 #FOAvip English Wikipedia <ref>{{Cite pmid|26142952 }}</ref> Optineurin: The autophagy connection #MMPMID26142952 Ying H ; Yue BY Exp Eye Res 2016[Mar]; 144 (?): 73-80 PMID26142952 show ga Optineurin is a cytosolic protein encoded by the OPTN gene. Mutations of OPTN are associated with normal tension glaucoma and amyotrophic lateral sclerosis. Autophagy is an intracellular degradation system that delivers cytoplasmic components to the lysosomes. It plays a wide variety of physiological and pathophysiological roles. The optineurin protein is a selective autophagy receptor (or adaptor), containing an ubiquitin binding domain with the ability to bind polyubiquitinated cargoes and bring them to autophagosomes via its microtubule-associated protein 1 light chain 3-interacting domain. It is involved in xenophagy, mitophagy, aggrephagy, and tumor suppression. Optineurin can also mediate the removal of protein aggregates through an ubiquitin-independent mechanism. This protein in addition can induce autophagy upon overexpression or mutation. When overexpressed or mutated, the optineurin protein also serves as a substrate for autophagic degradation. In the present review, the multiple connections of optineurin to autophagy are highlighted. |Autophagy/*genetics [MESH] |Cell Cycle Proteins [MESH] |Humans [MESH] |Low Tension Glaucoma/*genetics [MESH] |Membrane Transport Proteins [MESH]Optineurin: The autophagy connection (epmc).pdf DeepDyve Pubget Overpricing