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10.1371/journal.pone.0136362 http://scihub22266oqcxt.onion/10.1371/journal.pone.0136362 C4552826!4552826 !26317359     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 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\26317359 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       PLoS+One 2015 ; 10 (8 ): e0136362 Nephropedia Template TP {{tp|p=26317359 |t=2015. Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates |pdf=|usr=}}{{26317359 }} gab.com Text Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26317359 #FOAvip Intracellular protein aggregation is the hallmark of several neurodegenerative diseases. Aggregates formed by polyglutamine (polyQ)-expanded proteins, such as Huntingtin, adopt amyloid-like structures that are resistant to denaturation. We used a novel purification strategy to isolate aggregates formed by human Huntingtin N-terminal fragments with expanded polyQ tracts from both yeast and mammalian (PC-12) cells. Using mass spectrometry we identified the protein species that are trapped within these polyQ aggregates. We found that proteins with very long intrinsically-disordered (ID) domains (? 100 amino acids) and RNA-binding proteins were disproportionately recruited into aggregates. The removal of the ID domains from selected proteins was sufficient to eliminate their recruitment into polyQ aggregates. We also observed that several neurodegenerative disease-linked proteins were reproducibly trapped within the polyQ aggregates purified from mammalian cells. Many of these proteins have large ID domains and are found in neuronal inclusions in their respective diseases. Our study indicates that neurodegenerative disease-associated proteins are particularly vulnerable to recruitment into polyQ aggregates via their ID domains. Also, the high frequency of ID domains in RNA-binding proteins may explain why RNA-binding proteins are frequently found in pathological inclusions in various neurodegenerative diseases. Twit Text FOAVip Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26317359 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26317359 #FOAvip English Wikipedia <ref>{{Cite pmid|26317359 }}</ref> Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates #MMPMID26317359 Wear MP ; Kryndushkin D ; O'Meally R ; Sonnenberg JL ; Cole RN ; Shewmaker FP PLoS One 2015[]; 10 (8 ): e0136362 PMID26317359 show ga Intracellular protein aggregation is the hallmark of several neurodegenerative diseases. Aggregates formed by polyglutamine (polyQ)-expanded proteins, such as Huntingtin, adopt amyloid-like structures that are resistant to denaturation. We used a novel purification strategy to isolate aggregates formed by human Huntingtin N-terminal fragments with expanded polyQ tracts from both yeast and mammalian (PC-12) cells. Using mass spectrometry we identified the protein species that are trapped within these polyQ aggregates. We found that proteins with very long intrinsically-disordered (ID) domains (? 100 amino acids) and RNA-binding proteins were disproportionately recruited into aggregates. The removal of the ID domains from selected proteins was sufficient to eliminate their recruitment into polyQ aggregates. We also observed that several neurodegenerative disease-linked proteins were reproducibly trapped within the polyQ aggregates purified from mammalian cells. Many of these proteins have large ID domains and are found in neuronal inclusions in their respective diseases. Our study indicates that neurodegenerative disease-associated proteins are particularly vulnerable to recruitment into polyQ aggregates via their ID domains. Also, the high frequency of ID domains in RNA-binding proteins may explain why RNA-binding proteins are frequently found in pathological inclusions in various neurodegenerative diseases. |*Protein Aggregates [MESH] |Animals [MESH] |Humans [MESH] |Huntingtin Protein [MESH] |Nerve Tissue Proteins/genetics/*metabolism [MESH] |PC12 Cells [MESH] |Peptides/genetics/*metabolism [MESH] |RNA-Binding Proteins/genetics/*metabolism [MESH] |Rats [MESH]Proteins with Intrinsically Disordered Domains Are Preferentially Recr(epmc).pdf DeepDyve Pubget Overpricing