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10.1371/journal.pone.0151547 http://scihub22266oqcxt.onion/10.1371/journal.pone.0151547 C4798761!4798761!26991433     free     free     free       PLoS+One 2016 ; 11 (3): ä Nephropedia Template TP {{tp|p=26991433|t=2016. Ca-Dependent Folding of Human Calumenin |pdf=|usr=}}{{26991433}} gab.com Text Ca-Dependent Folding of Human Calumenin JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26991433 #FOAvip Human calumenin (hCALU) is a six EF-hand protein belonging to the CREC family. As other members of the family, it is localized in the secretory pathway and regulates the activity of SERCA2a and of the ryanodine receptor in the endoplasmic reticulum (ER). We have studied the effects of Ca2+ binding to the protein and found it to attain a more compact structure upon ion binding. Circular Dichroism (CD) measurements suggest a major rearrangement of the protein secondary structure, which reversibly switches from disordered at low Ca2+ concentrations to predominantly alpha-helical when Ca2+ is added. SAXS experiments confirm the transition from an unfolded to a compact structure, which matches the structural prediction of a trilobal fold. Overall our experiments suggest that calumenin is a Ca2+ sensor, which folds into a compact structure, capable of interacting with its molecular partners, when Ca2+ concentration within the ER reaches the millimolar range. Twit Text FOAVip Ca-Dependent Folding of Human Calumenin ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26991433 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26991433 #FOAvip English Wikipedia <ref>{{Cite pmid|26991433}}</ref> Ca-Dependent Folding of Human Calumenin #MMPMID26991433 Mazzorana M; Hussain R; Sorensen T PLoS One 2016[]; 11 (3): ä PMID26991433show ga Human calumenin (hCALU) is a six EF-hand protein belonging to the CREC family. As other members of the family, it is localized in the secretory pathway and regulates the activity of SERCA2a and of the ryanodine receptor in the endoplasmic reticulum (ER). We have studied the effects of Ca2+ binding to the protein and found it to attain a more compact structure upon ion binding. Circular Dichroism (CD) measurements suggest a major rearrangement of the protein secondary structure, which reversibly switches from disordered at low Ca2+ concentrations to predominantly alpha-helical when Ca2+ is added. SAXS experiments confirm the transition from an unfolded to a compact structure, which matches the structural prediction of a trilobal fold. Overall our experiments suggest that calumenin is a Ca2+ sensor, which folds into a compact structure, capable of interacting with its molecular partners, when Ca2+ concentration within the ER reaches the millimolar range. äCa-Dependent Folding of Human Calumenin (epmc).pdf DeepDyve Pubget Overpricing