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10.3390/biom4010252 http://scihub22266oqcxt.onion/10.3390/biom4010252 C4030994!4030994!24970215     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       Biomolecules 2014 ; 4 (1): 252-67 Nephropedia Template TP {{tp|p=24970215|t=2014. Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation |pdf=|usr=}}{{24970215}} gab.com Text Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation JO: Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970215 #FOAvip While the toxicity of metals and metalloids, like arsenic, cadmium, mercury, lead and chromium, is undisputed, the underlying molecular mechanisms are not entirely clear. General consensus holds that proteins are the prime targets; heavy metals interfere with the physiological activity of specific, particularly susceptible proteins, either by forming a complex with functional side chain groups or by displacing essential metal ions in metalloproteins. Recent studies have revealed an additional mode of metal action targeted at proteins in a non-native state; certain heavy metals and metalloids have been found to inhibit the in vitro refolding of chemically denatured proteins, to interfere with protein folding in vivo and to cause aggregation of nascent proteins in living cells. Apparently, unfolded proteins with motile backbone and side chains are considerably more prone to engage in stable, pluridentate metal complexes than native proteins with their well-defined 3D structure. By interfering with the folding process, heavy metal ions and metalloids profoundly affect protein homeostasis and cell viability. This review describes how heavy metals impede protein folding and promote protein aggregation, how cells regulate quality control systems to protect themselves from metal toxicity and how metals might contribute to protein misfolding disorders. Twit Text FOAVip Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation ????Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=24970215 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24970215 #FOAvip English Wikipedia <ref>{{Cite pmid|24970215}}</ref> Heavy Metals and Metalloids As a Cause for Protein Misfolding and Aggregation #MMPMID24970215 Tamás MJ; Sharma SK; Ibstedt S; Jacobson T; Christen P Biomolecules 2014[Mar]; 4 (1): 252-67 PMID24970215show ga While the toxicity of metals and metalloids, like arsenic, cadmium, mercury, lead and chromium, is undisputed, the underlying molecular mechanisms are not entirely clear. General consensus holds that proteins are the prime targets; heavy metals interfere with the physiological activity of specific, particularly susceptible proteins, either by forming a complex with functional side chain groups or by displacing essential metal ions in metalloproteins. Recent studies have revealed an additional mode of metal action targeted at proteins in a non-native state; certain heavy metals and metalloids have been found to inhibit the in vitro refolding of chemically denatured proteins, to interfere with protein folding in vivo and to cause aggregation of nascent proteins in living cells. Apparently, unfolded proteins with motile backbone and side chains are considerably more prone to engage in stable, pluridentate metal complexes than native proteins with their well-defined 3D structure. By interfering with the folding process, heavy metal ions and metalloids profoundly affect protein homeostasis and cell viability. This review describes how heavy metals impede protein folding and promote protein aggregation, how cells regulate quality control systems to protect themselves from metal toxicity and how metals might contribute to protein misfolding disorders. äHeavy Metals and Metalloids As a Cause for Protein Misfolding and Aggr(epmc).pdf DeepDyve Pubget Overpricing