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10.1371/journal.pone.0161445 http://scihub22266oqcxt.onion/10.1371/journal.pone.0161445 C5077117!5077117 !27776132     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27776132 &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       PLoS+One 2016 ; 11 (10 ): e0161445 Nephropedia Template TP {{tp|p=27776132 |t=2016. Tyrosine Binding Protein Sites Regulate the Intracellular Trafficking and Processing of Amyloid Precursor Protein through a Novel Lysosome-Directed Pathway |pdf=|usr=}}{{27776132 }} gab.com Text Tyrosine Binding Protein Sites Regulate the Intracellular Trafficking and Processing of Amyloid Precursor Protein through a Novel Lysosome-Directed Pathway JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=27776132 #FOAvip The amyloid hypothesis posits that the production of ?-amyloid (A?) aggregates leads to neurodegeneration and cognitive decline associated with AD. A? is produced by sequential cleavage of the amyloid precursor protein (APP) by ?- and ?-secretase. While nascent APP is well known to transit to the endosomal/ lysosomal system via the cell surface, we have recently shown that APP can also traffic to lysosomes intracellularly via its interaction with AP-3. Because AP-3 interacts with cargo protein via interaction with tyrosine motifs, we mutated the three tyrosines motif in the cytoplasmic tail of APP. Here, we show that the YTSI motif interacts with AP-3, and phosphorylation of the serine in this motif disrupts the interaction and decreases APP trafficking to lysosomes. Furthermore, we show that phosphorylation at this motif can decrease the production of neurotoxic A? 42. This demonstrates that reducing APP trafficking to lysosomes may be a strategy to reduce A? 42 in Alzheimer's disease. Twit Text FOAVip Tyrosine Binding Protein Sites Regulate the Intracellular Trafficking and Processing of Amyloid Precursor Protein through a Novel Lysosome-Directed Pathway ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=27776132 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27776132 #FOAvip English Wikipedia <ref>{{Cite pmid|27776132 }}</ref> Tyrosine Binding Protein Sites Regulate the Intracellular Trafficking and Processing of Amyloid Precursor Protein through a Novel Lysosome-Directed Pathway #MMPMID27776132 Tam JH ; Cobb MR ; Seah C ; Pasternak SH PLoS One 2016[]; 11 (10 ): e0161445 PMID27776132 show ga The amyloid hypothesis posits that the production of ?-amyloid (A?) aggregates leads to neurodegeneration and cognitive decline associated with AD. A? is produced by sequential cleavage of the amyloid precursor protein (APP) by ?- and ?-secretase. While nascent APP is well known to transit to the endosomal/ lysosomal system via the cell surface, we have recently shown that APP can also traffic to lysosomes intracellularly via its interaction with AP-3. Because AP-3 interacts with cargo protein via interaction with tyrosine motifs, we mutated the three tyrosines motif in the cytoplasmic tail of APP. Here, we show that the YTSI motif interacts with AP-3, and phosphorylation of the serine in this motif disrupts the interaction and decreases APP trafficking to lysosomes. Furthermore, we show that phosphorylation at this motif can decrease the production of neurotoxic A? 42. This demonstrates that reducing APP trafficking to lysosomes may be a strategy to reduce A? 42 in Alzheimer's disease. |Amyloid beta-Protein Precursor/*metabolism [MESH] |Animals [MESH] |Carrier Proteins/*metabolism [MESH] |Cell Line [MESH] |Endocytosis [MESH] |Enzyme Activation [MESH] |Humans [MESH] |Lysosomes/*metabolism [MESH] |Phosphorylation [MESH] |Protein Kinase C-epsilon/metabolism [MESH] |Protein Transport [MESH]Tyrosine Binding Protein Sites Regulate the Intracellular Trafficking (epmc).pdf DeepDyve Pubget Overpricing