Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1186/s12934-015-0361-y http://scihub22266oqcxt.onion/10.1186/s12934-015-0361-y C4634817!4634817 !26536866     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 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\26536866 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Microb+Cell+Fact 2015 ; 14 (ä): 174 Nephropedia Template TP {{tp|p=26536866 |t=2015. Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria |pdf=|usr=}}{{26536866 }} gab.com Text Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria JO: Microb Cell Fact http://www.kidney.de/pget.php?&tw=1&pmid=26536866 #FOAvip BACKGROUND: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. The structural conversion of the cellular prion protein (PrP(C)), into its misfolded pathogenic form (PrP(Sc)) is the central event of prion-driven pathologies. The study of the structural properties of intracellular amyloid aggregates in general and of prion-like ones in particular is a challenging task. In this context, the evidence that the inclusion bodies formed by amyloid proteins in bacteria display amyloid-like structural and functional properties make them a privileged system to model intracellular amyloid aggregation. RESULTS: Here we provide the first demonstration that recombinant murine PrP and its C-terminal domain (90-231) attain amyloid conformations inside bacteria. Moreover, the inclusions formed by these two PrP proteins display conformational diversity, since they differ in fibril morphology, binding affinity to amyloid dyes, stability, resistance to proteinase K digestion and neurotoxicity. CONCLUSIONS: Overall, our results suggest that modelling PrP amyloid formation in microbial cell factories might open an avenue for a better understanding of the structural features modulating the pathogenic impact of this intriguing protein. Twit Text FOAVip Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria ????Microb Cell Fact http://www.kidney.de/pget.php?&tw=1&pmid=26536866 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26536866 #FOAvip English Wikipedia <ref>{{Cite pmid|26536866 }}</ref> Mammalian prion protein (PrP) forms conformationally different amyloid intracellular aggregates in bacteria #MMPMID26536866 Macedo B ; Sant'Anna R ; Navarro S ; Cordeiro Y ; Ventura S Microb Cell Fact 2015[Nov]; 14 (ä): 174 PMID26536866 show ga BACKGROUND: An increasing number of proteins are being shown to assemble into amyloid structures that lead to pathological states. Among them, mammalian prions outstand due to their ability to transmit the pathogenic conformation, becoming thus infectious. The structural conversion of the cellular prion protein (PrP(C)), into its misfolded pathogenic form (PrP(Sc)) is the central event of prion-driven pathologies. The study of the structural properties of intracellular amyloid aggregates in general and of prion-like ones in particular is a challenging task. In this context, the evidence that the inclusion bodies formed by amyloid proteins in bacteria display amyloid-like structural and functional properties make them a privileged system to model intracellular amyloid aggregation. RESULTS: Here we provide the first demonstration that recombinant murine PrP and its C-terminal domain (90-231) attain amyloid conformations inside bacteria. Moreover, the inclusions formed by these two PrP proteins display conformational diversity, since they differ in fibril morphology, binding affinity to amyloid dyes, stability, resistance to proteinase K digestion and neurotoxicity. CONCLUSIONS: Overall, our results suggest that modelling PrP amyloid formation in microbial cell factories might open an avenue for a better understanding of the structural features modulating the pathogenic impact of this intriguing protein. |Amyloid/*chemistry/metabolism [MESH] |Animals [MESH] |Bacteria/*metabolism [MESH] |Benzothiazoles [MESH] |Endopeptidase K/metabolism [MESH] |Escherichia coli/metabolism [MESH] |Inclusion Bodies/metabolism [MESH] |Mice [MESH] |Microscopy, Electron, Transmission [MESH] |Prions/*chemistry/genetics/metabolism [MESH] |Protein Binding [MESH] |Protein Folding [MESH] |Protein Structure, Secondary [MESH] |Protein Structure, Tertiary [MESH] |Recombinant Proteins/biosynthesis/chemistry/isolation & purification [MESH] |Spectroscopy, Fourier Transform Infrared [MESH]Mammalian prion protein (PrP) forms conformationally different amyloid(epmc).pdf DeepDyve Pubget Overpricing