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10.1074/jbc.M115.689539 http://scihub22266oqcxt.onion/10.1074/jbc.M115.689539 C4807280!4807280 !26884339     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 265.2 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\26884339 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2016 ; 291 (13 ): 6958-66 Nephropedia Template TP {{tp|p=26884339 |t=2016. Clusterin Binds to A?1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation |pdf=|usr=}}{{26884339 }} gab.com Text Clusterin Binds to A 1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26884339 #FOAvip The aggregation of amyloid ? protein (A?) is a fundamental pathogenic mechanism leading to the neuronal damage present in Alzheimer disease, and soluble A? oligomers are thought to be a major toxic culprit. Thus, better knowledge and specific targeting of the pathways that lead to these noxious species may result in valuable therapeutic strategies. We characterized some effects of the molecular chaperone clusterin, providing new and more detailed evidence of its potential neuroprotective effects. Using a classical thioflavin T assay, we observed a dose-dependent inhibition of the aggregation process. The global analysis of time courses under different conditions demonstrated that clusterin has no effect on the elongation rate but mainly interferes with the nucleation processes (both primary and secondary), reducing the number of nuclei available for further fibril growth. Then, using a recently developed immunoassay based on surface plasmon resonance, we obtained direct evidence of a high-affinity (KD= 1 nm) interaction of clusterin with biologically relevant A?1-42oligomers, selectively captured on the sensor chip. Moreover, with the same technology, we observed that substoichiometric concentrations of clusterin prevent oligomer interaction with the antibody 4G8, suggesting that the chaperone shields hydrophobic residues exposed on the oligomeric assemblies. Finally, we found that preincubation with clusterin antagonizes the toxic effects of A?1-42oligomers, as evaluated in a recently developedin vivomodel inCaenorhabditis elegans.These data substantiate the interaction of clusterin with biologically active regions exposed on nuclei/oligomers of A?1-42, providing a molecular basis for the neuroprotective effects of the chaperone. Twit Text FOAVip Clusterin Binds to A 1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26884339 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26884339 #FOAvip English Wikipedia <ref>{{Cite pmid|26884339 }}</ref> Clusterin Binds to A?1-42 Oligomers with High Affinity and Interferes with Peptide Aggregation by Inhibiting Primary and Secondary Nucleation #MMPMID26884339 Beeg M ; Stravalaci M ; Romeo M ; Carrá AD ; Cagnotto A ; Rossi A ; Diomede L ; Salmona M ; Gobbi M J Biol Chem 2016[Mar]; 291 (13 ): 6958-66 PMID26884339 show ga The aggregation of amyloid ? protein (A?) is a fundamental pathogenic mechanism leading to the neuronal damage present in Alzheimer disease, and soluble A? oligomers are thought to be a major toxic culprit. Thus, better knowledge and specific targeting of the pathways that lead to these noxious species may result in valuable therapeutic strategies. We characterized some effects of the molecular chaperone clusterin, providing new and more detailed evidence of its potential neuroprotective effects. Using a classical thioflavin T assay, we observed a dose-dependent inhibition of the aggregation process. The global analysis of time courses under different conditions demonstrated that clusterin has no effect on the elongation rate but mainly interferes with the nucleation processes (both primary and secondary), reducing the number of nuclei available for further fibril growth. Then, using a recently developed immunoassay based on surface plasmon resonance, we obtained direct evidence of a high-affinity (KD= 1 nm) interaction of clusterin with biologically relevant A?1-42oligomers, selectively captured on the sensor chip. Moreover, with the same technology, we observed that substoichiometric concentrations of clusterin prevent oligomer interaction with the antibody 4G8, suggesting that the chaperone shields hydrophobic residues exposed on the oligomeric assemblies. Finally, we found that preincubation with clusterin antagonizes the toxic effects of A?1-42oligomers, as evaluated in a recently developedin vivomodel inCaenorhabditis elegans.These data substantiate the interaction of clusterin with biologically active regions exposed on nuclei/oligomers of A?1-42, providing a molecular basis for the neuroprotective effects of the chaperone. |Alzheimer Disease/metabolism/pathology [MESH] |Amyloid beta-Peptides/*antagonists & inhibitors/chemical synthesis/toxicity [MESH] |Animals [MESH] |Biological Assay [MESH] |Caenorhabditis elegans/*drug effects/physiology [MESH] |Clusterin/isolation & purification/*pharmacology [MESH] |Humans [MESH] |Kinetics [MESH] |Larva/drug effects/physiology [MESH] |Neuroprotective Agents/isolation & purification/*pharmacology [MESH] |Peptide Fragments/*antagonists & inhibitors/chemical synthesis/toxicity [MESH] |Pharynx/*drug effects/physiology [MESH] |Protein Aggregates/drug effects [MESH] |Protein Aggregation, Pathological/pathology/*prevention & control [MESH]Clusterin Binds to A?1-42 Oligomers with High Affinity and Interferes (epmc).pdf DeepDyve Pubget Overpricing