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.

10.1038/nchem.2129 http://scihub22266oqcxt.onion/10.1038/nchem.2129 C4280571!4280571!25515893     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 263.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Chem 2015 ; 7 (1): 73-81 Nephropedia Template TP {{tp|p=25515893|t=2015. Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry |pdf=|usr=}}{{25515893}} gab.com Text Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry JO: Nat Chem http://www.kidney.de/pget.php?&tw=1&pmid=25515893 #FOAvip The search for therapeutic agents which bind specifically to precursor protein conformations and inhibit amyloid assembly is an important challenge. Identifying such inhibitors is difficult since many protein precursors of aggregation are partially folded or intrinsically disordered, ruling out structure-based design. Furthermore, inhibitors can act by a variety of mechanisms, including specific or non-specific binding, as well as colloidal inhibition. Here we report a high throughput method based on ion mobility spectrometry-mass spectrometry (IMS-MS) that is capable of rapidly detecting small molecules that bind to amyloid precursors, identifying the interacting protein species, and defining the mode of inhibition. Using this method we have classified a variety of small molecules that are potential inhibitors of human islet amyloid polypeptide (hIAPP) aggregation or amyloid-beta 1-40 (A?40) aggregation as either specific, non-specific, colloidal or non-interacting. We also demonstrate the ability of IMS-MS to screen for inhibitory small molecules in a 96-well plate format and use this to discover a new inhibitor of hIAPP amyloid assembly. Twit Text FOAVip Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry ????Nat Chem http://www.kidney.de/pget.php?&tw=1&pmid=25515893 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25515893 #FOAvip English Wikipedia <ref>{{Cite pmid|25515893}}</ref> Screening and classifying small molecule inhibitors of amyloid formation using ion mobility spectrometry-mass spectrometry #MMPMID25515893 Young LM; Saunders JC; Mahood RA; Revill CH; Foster RJ; Tu LH; Raleigh DP; Radford SE; Ashcroft AE Nat Chem 2015[Jan]; 7 (1): 73-81 PMID25515893show ga The search for therapeutic agents which bind specifically to precursor protein conformations and inhibit amyloid assembly is an important challenge. Identifying such inhibitors is difficult since many protein precursors of aggregation are partially folded or intrinsically disordered, ruling out structure-based design. Furthermore, inhibitors can act by a variety of mechanisms, including specific or non-specific binding, as well as colloidal inhibition. Here we report a high throughput method based on ion mobility spectrometry-mass spectrometry (IMS-MS) that is capable of rapidly detecting small molecules that bind to amyloid precursors, identifying the interacting protein species, and defining the mode of inhibition. Using this method we have classified a variety of small molecules that are potential inhibitors of human islet amyloid polypeptide (hIAPP) aggregation or amyloid-beta 1-40 (A?40) aggregation as either specific, non-specific, colloidal or non-interacting. We also demonstrate the ability of IMS-MS to screen for inhibitory small molecules in a 96-well plate format and use this to discover a new inhibitor of hIAPP amyloid assembly. äScreening and classifying small molecule inhibitors of amyloid formati(epmc).pdf DeepDyve Pubget Overpricing