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10.1073/pnas.1606482113 http://scihub22266oqcxt.onion/10.1073/pnas.1606482113 C5018773!5018773 !27559086     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 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\27559086 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (36 ): E5281-7 Nephropedia Template TP {{tp|p=27559086 |t=2016. Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein |pdf=|usr=}}{{27559086 }} gab.com Text Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27559086 #FOAvip Cleavage of the amyloid precursor protein (APP) by ?-secretase is a crucial first step in the evolution of Alzheimer's disease. To discover the cleavage mechanism, it is urgent to predict the structures of APP monomers and dimers in varying membrane environments. We determined the structures of the C9923-55 monomer and homodimer as a function of membrane lipid composition using a multiscale simulation approach that blends atomistic and coarse-grained models. We demonstrate that the C9923-55 homodimer structures form a heterogeneous ensemble with multiple conformational states, each stabilized by characteristic interpeptide interactions. The relative probabilities of each conformational state are sensitive to the membrane environment, leading to substantial variation in homodimer peptide structure as a function of membrane lipid composition or the presence of an anionic lipid environment. In contrast, the helicity of the transmembrane domain of monomeric C991-55 is relatively insensitive to the membrane lipid composition, in agreement with experimental observations. The dimer structures of human EphA2 receptor depend on the lipid environment, which we show is linked to the location of the structural motifs in the dimer interface, thereby establishing that both sequence and membrane composition modulate the complete energy landscape of membrane-bound proteins. As a by-product of our work, we explain the discrepancy in structures predicted for C99 congener homodimers in membrane and micelle environments. Our study provides insight into the observed dependence of C99 protein cleavage by ?-secretase, critical to the formation of amyloid-? protein, on membrane thickness and lipid composition. Twit Text FOAVip Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27559086 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27559086 #FOAvip English Wikipedia <ref>{{Cite pmid|27559086 }}</ref> Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein #MMPMID27559086 Dominguez L ; Foster L ; Straub JE ; Thirumalai D Proc Natl Acad Sci U S A 2016[Sep]; 113 (36 ): E5281-7 PMID27559086 show ga Cleavage of the amyloid precursor protein (APP) by ?-secretase is a crucial first step in the evolution of Alzheimer's disease. To discover the cleavage mechanism, it is urgent to predict the structures of APP monomers and dimers in varying membrane environments. We determined the structures of the C9923-55 monomer and homodimer as a function of membrane lipid composition using a multiscale simulation approach that blends atomistic and coarse-grained models. We demonstrate that the C9923-55 homodimer structures form a heterogeneous ensemble with multiple conformational states, each stabilized by characteristic interpeptide interactions. The relative probabilities of each conformational state are sensitive to the membrane environment, leading to substantial variation in homodimer peptide structure as a function of membrane lipid composition or the presence of an anionic lipid environment. In contrast, the helicity of the transmembrane domain of monomeric C991-55 is relatively insensitive to the membrane lipid composition, in agreement with experimental observations. The dimer structures of human EphA2 receptor depend on the lipid environment, which we show is linked to the location of the structural motifs in the dimer interface, thereby establishing that both sequence and membrane composition modulate the complete energy landscape of membrane-bound proteins. As a by-product of our work, we explain the discrepancy in structures predicted for C99 congener homodimers in membrane and micelle environments. Our study provides insight into the observed dependence of C99 protein cleavage by ?-secretase, critical to the formation of amyloid-? protein, on membrane thickness and lipid composition. |Alzheimer Disease/*genetics/metabolism [MESH] |Amyloid Precursor Protein Secretases/chemistry/genetics [MESH] |Amyloid beta-Protein Precursor/*chemistry/genetics [MESH] |Dimerization [MESH] |Humans [MESH] |Membrane Lipids/*chemistry/genetics [MESH] |Peptide Fragments/chemistry [MESH] |Protein Conformation [MESH] |Protein Domains/genetics [MESH] |Protein Stability [MESH] |Proteolysis [MESH]Impact of membrane lipid composition on the structure and stability of(epmc).pdf DeepDyve Pubget Overpricing