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10.1021/bi300555d http://scihub22266oqcxt.onion/10.1021/bi300555d C5603225!5603225!22631438     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 253.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biochemistry 2012 ; 51 (23): 4633-41 Nephropedia Template TP {{tp|p=22631438|t=2012. Role of Apolipoprotein A-II in the Structure and Remodeling of Human High-Density Lipoprotein (HDL): Protein Conformational Ensemble on HDL |pdf=|usr=}}{{22631438}} gab.com Text Role of Apolipoprotein A-II in the Structure and Remodeling of Human High-Density Lipoprotein (HDL): Protein Conformational Ensemble on HDL JO: Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=22631438 #FOAvip High-density lipoproteins (HDL, or ?good cholesterol?) are heterogeneous nanoparticles that remove excess cell cholesterol and protect against atherosclerosis. The cardioprotective action of HDL and its major protein, apolipoprotein A-I (apoA-I), is well-established, yet the function of the second major protein, apolipoprotein A-II (apoA-II), is less clear. In this review, we postulate an ensemble of apolipoprotein conformations on various HDL. This ensemble is based on the crystal structure of ?(185?243)apoA-I determined by Mei and Atkinson combined with the ?double-hairpin? conformation of apoA-IIdimer proposed in the cross-linking studies by Silva?s team, and is supported by the wide array of low-resolution structural, biophysical, and biochemical data obtained by many teams over decades. The proposed conformational ensemble helps integrate and improve several existing HDL models, including the ?buckle-belt? conformation of apoA-I on the midsize disks and the ?trefoil/tetrafoil? arrangement on spherical HDL. This ensemble prompts us to hypothesize that endogenous apoA-II (i) helps confer lipid surface curvature during conversion of nascent discoidal HDL(A-I) and HDL(A-II) containing either apoA-I or apoA-II to mature spherical HDL(A-I/A-II) containing both proteins, and (ii) hinders remodeling of HDL(A-I/A-II) by hindering the expansion of the apoA-I conformation. Also, we report that, although endogenous apoA-II circulates mainly on the midsize spherical HDL(A-I/A-II), exogenous apoA-II can bind to HDL of any size, thereby slightly increasing this size and stabilizing the HDL assembly. This suggests distinctly different effects of the endogenous and exogenous apoA-II on HDL. Taken together, the existing results and models prompt us to postulate a new structural and functional role of apoA-II on human HDL. Twit Text FOAVip Role of Apolipoprotein A-II in the Structure and Remodeling of Human High-Density Lipoprotein (HDL): Protein Conformational Ensemble on HDL ????Biochemistry http://www.kidney.de/pget.php?&tw=1&pmid=22631438 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=22631438 #FOAvip English Wikipedia <ref>{{Cite pmid|22631438}}</ref> Role of Apolipoprotein A-II in the Structure and Remodeling of Human High-Density Lipoprotein (HDL): Protein Conformational Ensemble on HDL #MMPMID22631438 Gao X; Yuan S; Jayaraman S; Gursky O Biochemistry 2012[Jun]; 51 (23): 4633-41 PMID22631438show ga High-density lipoproteins (HDL, or ?good cholesterol?) are heterogeneous nanoparticles that remove excess cell cholesterol and protect against atherosclerosis. The cardioprotective action of HDL and its major protein, apolipoprotein A-I (apoA-I), is well-established, yet the function of the second major protein, apolipoprotein A-II (apoA-II), is less clear. In this review, we postulate an ensemble of apolipoprotein conformations on various HDL. This ensemble is based on the crystal structure of ?(185?243)apoA-I determined by Mei and Atkinson combined with the ?double-hairpin? conformation of apoA-IIdimer proposed in the cross-linking studies by Silva?s team, and is supported by the wide array of low-resolution structural, biophysical, and biochemical data obtained by many teams over decades. The proposed conformational ensemble helps integrate and improve several existing HDL models, including the ?buckle-belt? conformation of apoA-I on the midsize disks and the ?trefoil/tetrafoil? arrangement on spherical HDL. This ensemble prompts us to hypothesize that endogenous apoA-II (i) helps confer lipid surface curvature during conversion of nascent discoidal HDL(A-I) and HDL(A-II) containing either apoA-I or apoA-II to mature spherical HDL(A-I/A-II) containing both proteins, and (ii) hinders remodeling of HDL(A-I/A-II) by hindering the expansion of the apoA-I conformation. Also, we report that, although endogenous apoA-II circulates mainly on the midsize spherical HDL(A-I/A-II), exogenous apoA-II can bind to HDL of any size, thereby slightly increasing this size and stabilizing the HDL assembly. This suggests distinctly different effects of the endogenous and exogenous apoA-II on HDL. Taken together, the existing results and models prompt us to postulate a new structural and functional role of apoA-II on human HDL. äRole of Apolipoprotein A-II in the Structure and Remodeling of Human H(epmc).pdf DeepDyve Pubget Overpricing