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10.1007/s12551-013-0132-0 http://scihub22266oqcxt.onion/10.1007/s12551-013-0132-0 C5425713!5425713!28509960     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 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\28509960.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biophys+Rev 2014 ; 6 (1): 97-110 Nephropedia Template TP {{tp|p=28509960|t=2014. Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases |pdf=|usr=}}{{28509960}} gab.com Text Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases JO: Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28509960 #FOAvip Protein misfolding disorders (PMDs) refer to a group of diseases related to the misfolding of particular proteins that aggregate and deposit in the cells and tissues of humans and other mammals. The mechanisms that trigger protein misfolding and aggregation are still not fully understood. Increasing experimental evidence indicates that abnormal interactions between PMD-related proteins and nucleic acids (NAs) can induce conformational changes. Here, we discuss these protein?NA interactions and address the role of deoxyribonucleic (DNA) and ribonucleic (RNA) acid molecules in the conformational conversion of different proteins that aggregate in PMDs, such as Alzheimer?s, Parkinson?s, and prion diseases. Studies on the affinity, stability, and specificity of proteins involved in neurodegenerative diseases and NAs are specifically addressed. A landscape of reciprocal effects resulting from the binding of prion proteins, amyloid-? peptides, tau proteins, huntingtin, and ?-synuclein are presented here to clarify the possible role of NAs, not only as encoders of genetic information but also in triggering PMDs. Twit Text FOAVip Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases ????Biophys Rev http://www.kidney.de/pget.php?&tw=1&pmid=28509960 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28509960 #FOAvip English Wikipedia <ref>{{Cite pmid|28509960}}</ref> Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases #MMPMID28509960 Cordeiro Y; Macedo B; Silva JL; Gomes MPB Biophys Rev 2014[Mar]; 6 (1): 97-110 PMID28509960show ga Protein misfolding disorders (PMDs) refer to a group of diseases related to the misfolding of particular proteins that aggregate and deposit in the cells and tissues of humans and other mammals. The mechanisms that trigger protein misfolding and aggregation are still not fully understood. Increasing experimental evidence indicates that abnormal interactions between PMD-related proteins and nucleic acids (NAs) can induce conformational changes. Here, we discuss these protein?NA interactions and address the role of deoxyribonucleic (DNA) and ribonucleic (RNA) acid molecules in the conformational conversion of different proteins that aggregate in PMDs, such as Alzheimer?s, Parkinson?s, and prion diseases. Studies on the affinity, stability, and specificity of proteins involved in neurodegenerative diseases and NAs are specifically addressed. A landscape of reciprocal effects resulting from the binding of prion proteins, amyloid-? peptides, tau proteins, huntingtin, and ?-synuclein are presented here to clarify the possible role of NAs, not only as encoders of genetic information but also in triggering PMDs. äPathological implications of nucleic acid interactions with proteins a(epmc).pdf DeepDyve Pubget Overpricing