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10.1083/jcb.201512016 http://scihub22266oqcxt.onion/10.1083/jcb.201512016 C5021092!5021092 !27597756     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 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 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\27597756 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Biol 2016 ; 214 (6 ): 705-18 Nephropedia Template TP {{tp|p=27597756 |t=2016. Munc18-1 is a molecular chaperone for ?-synuclein, controlling its self-replicating aggregation |pdf=|usr=}}{{27597756 }} gab.com Text Munc18-1 is a molecular chaperone for -synuclein, controlling its self-replicating aggregation JO: J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27597756 #FOAvip Munc18-1 is a key component of the exocytic machinery that controls neurotransmitter release. Munc18-1 heterozygous mutations cause developmental defects and epileptic phenotypes, including infantile epileptic encephalopathy (EIEE), suggestive of a gain of pathological function. Here, we used single-molecule analysis, gene-edited cells, and neurons to demonstrate that Munc18-1 EIEE-causing mutants form large polymers that coaggregate wild-type Munc18-1 in vitro and in cells. Surprisingly, Munc18-1 EIEE mutants also form Lewy body-like structures that contain ?-synuclein (?-Syn). We reveal that Munc18-1 binds ?-Syn, and its EIEE mutants coaggregate ?-Syn. Likewise, removal of endogenous Munc18-1 increases the aggregative propensity of ?-Syn(WT) and that of the Parkinson's disease-causing ?-Syn(A30P) mutant, an effect rescued by Munc18-1(WT) expression, indicative of chaperone activity. Coexpression of the ?-Syn(A30P) mutant with Munc18-1 reduced the number of ?-Syn(A30P) aggregates. Munc18-1 mutations and haploinsufficiency may therefore trigger a pathogenic gain of function through both the corruption of native Munc18-1 and a perturbed chaperone activity for ?-Syn leading to aggregation-induced neurodegeneration. Twit Text FOAVip Munc18-1 is a molecular chaperone for -synuclein, controlling its self-replicating aggregation ????J Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=27597756 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27597756 #FOAvip English Wikipedia <ref>{{Cite pmid|27597756 }}</ref> Munc18-1 is a molecular chaperone for ?-synuclein, controlling its self-replicating aggregation #MMPMID27597756 Chai YJ ; Sierecki E ; Tomatis VM ; Gormal RS ; Giles N ; Morrow IC ; Xia D ; Götz J ; Parton RG ; Collins BM ; Gambin Y ; Meunier FA J Cell Biol 2016[Sep]; 214 (6 ): 705-18 PMID27597756 show ga Munc18-1 is a key component of the exocytic machinery that controls neurotransmitter release. Munc18-1 heterozygous mutations cause developmental defects and epileptic phenotypes, including infantile epileptic encephalopathy (EIEE), suggestive of a gain of pathological function. Here, we used single-molecule analysis, gene-edited cells, and neurons to demonstrate that Munc18-1 EIEE-causing mutants form large polymers that coaggregate wild-type Munc18-1 in vitro and in cells. Surprisingly, Munc18-1 EIEE mutants also form Lewy body-like structures that contain ?-synuclein (?-Syn). We reveal that Munc18-1 binds ?-Syn, and its EIEE mutants coaggregate ?-Syn. Likewise, removal of endogenous Munc18-1 increases the aggregative propensity of ?-Syn(WT) and that of the Parkinson's disease-causing ?-Syn(A30P) mutant, an effect rescued by Munc18-1(WT) expression, indicative of chaperone activity. Coexpression of the ?-Syn(A30P) mutant with Munc18-1 reduced the number of ?-Syn(A30P) aggregates. Munc18-1 mutations and haploinsufficiency may therefore trigger a pathogenic gain of function through both the corruption of native Munc18-1 and a perturbed chaperone activity for ?-Syn leading to aggregation-induced neurodegeneration. |*Nerve Degeneration [MESH] |*Protein Aggregates [MESH] |Animals [MESH] |Animals, Newborn [MESH] |Genotype [MESH] |Haploinsufficiency [MESH] |Lewy Bodies/metabolism/pathology [MESH] |Microscopy, Fluorescence [MESH] |Models, Molecular [MESH] |Molecular Chaperones/chemistry/genetics/*metabolism [MESH] |Munc18 Proteins/chemistry/genetics/*metabolism [MESH] |Mutation [MESH] |Neurons/*metabolism/pathology [MESH] |PC12 Cells [MESH] |Parkinson Disease/genetics/metabolism/pathology [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |RNA Interference [MESH] |Rats [MESH] |Rats, Sprague-Dawley [MESH] |Recombinant Fusion Proteins/genetics/metabolism [MESH] |Time Factors [MESH] |Transfection [MESH]Munc18-1 is a molecular chaperone for ?-synuclein, controlling its s(epmc).pdf DeepDyve Pubget Overpricing