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10.1002/cphc.201000996 http://scihub22266oqcxt.onion/10.1002/cphc.201000996 C5402868!5402868!21308945     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Chemphyschem 2011 ; 12 (3): 673-80 Nephropedia Template TP {{tp|p=21308945|t=2011. A FRET Sensor for Non-Invasive Imaging of Amyloid Formation in Vivo |pdf=|usr=}}{{21308945}} gab.com Text A FRET Sensor for Non-Invasive Imaging of Amyloid Formation in Vivo JO: Chemphyschem http://www.kidney.de/pget.php?&tw=1&pmid=21308945 #FOAvip Misfolding and aggregation of amyloidogenic polypeptides lie at the root of many neurodegenerative diseases. Whilst protein aggregation can be readily studied in vitro by established biophysical techniques, direct observation of the nature and kinetics of aggregation processes taking place in vivo is much more challenging. We describe here, however, a Förster resonance energy transfer sensor that permits the aggregation kinetics of amyloidogenic proteins to be quantified in living systems by exploiting our observation that amyloid assemblies can act as energy acceptors for variants of fluorescent proteins. The observed lifetime reduction can be attributed to fluorescence energy transfer to intrinsic energy states associated with the growing amyloid species. Indeed, for ?-synuclein, a protein whose aggregation is linked to Parkinson?s disease, we have used this sensor to follow the kinetics of the self-association reactions taking place in vitro and in vivo and to reveal the nature of the ensuing aggregated species. Experiments were conducted in vitro, in cells in culture and in living Caenorhabditis elegans. For the latter the readout correlates directly with the appearance of a toxic phenotype. The ability to measure the appearance and development of pathogenic amyloid species in a living animal and the ability to relate such data to similar processes observed in vitro provides a powerful new tool in the study of the pathology of the family of misfolding disorders. Our study confirms the importance of the molecular environment in which aggregation reactions take place, highlighting similarities as well as differences between the processes occurring in vitro and in vivo, and their significance for defining the molecular physiology of the diseases with which they are associated. Twit Text FOAVip A FRET Sensor for Non-Invasive Imaging of Amyloid Formation in Vivo ????Chemphyschem http://www.kidney.de/pget.php?&tw=1&pmid=21308945 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=21308945 #FOAvip English Wikipedia <ref>{{Cite pmid|21308945}}</ref> A FRET Sensor for Non-Invasive Imaging of Amyloid Formation in Vivo #MMPMID21308945 Kaminski Schierle GS; Bertoncini CW; Chan FTS; van der Goot AT; Schwedler S; Skepper J; Schlachter S; van Ham T; Esposito A; Kumita JR; Nollen EAA; Dobson CM; Kaminski CF Chemphyschem 2011[Feb]; 12 (3): 673-80 PMID21308945show ga Misfolding and aggregation of amyloidogenic polypeptides lie at the root of many neurodegenerative diseases. Whilst protein aggregation can be readily studied in vitro by established biophysical techniques, direct observation of the nature and kinetics of aggregation processes taking place in vivo is much more challenging. We describe here, however, a Förster resonance energy transfer sensor that permits the aggregation kinetics of amyloidogenic proteins to be quantified in living systems by exploiting our observation that amyloid assemblies can act as energy acceptors for variants of fluorescent proteins. The observed lifetime reduction can be attributed to fluorescence energy transfer to intrinsic energy states associated with the growing amyloid species. Indeed, for ?-synuclein, a protein whose aggregation is linked to Parkinson?s disease, we have used this sensor to follow the kinetics of the self-association reactions taking place in vitro and in vivo and to reveal the nature of the ensuing aggregated species. Experiments were conducted in vitro, in cells in culture and in living Caenorhabditis elegans. For the latter the readout correlates directly with the appearance of a toxic phenotype. The ability to measure the appearance and development of pathogenic amyloid species in a living animal and the ability to relate such data to similar processes observed in vitro provides a powerful new tool in the study of the pathology of the family of misfolding disorders. Our study confirms the importance of the molecular environment in which aggregation reactions take place, highlighting similarities as well as differences between the processes occurring in vitro and in vivo, and their significance for defining the molecular physiology of the diseases with which they are associated. äA FRET Sensor for Non-Invasive Imaging of Amyloid Formation in Vivo (epmc).pdf DeepDyve Pubget Overpricing