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10.3389/fmolb.2017.00018 http://scihub22266oqcxt.onion/10.3389/fmolb.2017.00018 C5378721!5378721!28421184     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Mol+Biosci 2017 ; 4 (ä): ä Nephropedia Template TP {{tp|p=28421184|t=2017. The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins |pdf=|usr=}}{{28421184}} gab.com Text The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins JO: Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=28421184 #FOAvip All domains of life have ATP-dependent compartmentalized proteases that sequester their peptidase sites on their interior. ATPase complexes will often associate with these compartmentalized proteases in order to unfold and inject substrates into the protease for degradation. Significant effort has been put into understanding how ATP hydrolysis is used to apply force to proteins and cause them to unfold. The unfolding kinetics of the bacterial ATPase, ClpX, have been shown to resemble a fast motor that traps unfolded intermediates as a strategy to unfold proteins. In the present study, we sought to determine if the proteasomal ATPases from eukaryotes and archaea exhibit similar unfolding kinetics. We found that the proteasomal ATPases appear to use a different kinetic strategy for protein unfolding, behaving as a slower but more processive and efficient translocation motor, particularly when encountering a folded domain. We expect that these dissimilarities are due to differences in the ATP binding/exchange cycle, the presence of a trans-arginine finger, or the presence of a threading ring (i.e., the OB domain), which may be used as a rigid platform to pull folded domains against. We speculate that these differences may have evolved due to the differing client pools these machines are expected to encounter. Twit Text FOAVip The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins ????Front Mol Biosci http://www.kidney.de/pget.php?&tw=1&pmid=28421184 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28421184 #FOAvip English Wikipedia <ref>{{Cite pmid|28421184}}</ref> The Proteasomal ATPases Use a Slow but Highly Processive Strategy to Unfold Proteins #MMPMID28421184 Snoberger A; Anderson RT; Smith DM Front Mol Biosci 2017[]; 4 (ä): ä PMID28421184show ga All domains of life have ATP-dependent compartmentalized proteases that sequester their peptidase sites on their interior. ATPase complexes will often associate with these compartmentalized proteases in order to unfold and inject substrates into the protease for degradation. Significant effort has been put into understanding how ATP hydrolysis is used to apply force to proteins and cause them to unfold. The unfolding kinetics of the bacterial ATPase, ClpX, have been shown to resemble a fast motor that traps unfolded intermediates as a strategy to unfold proteins. In the present study, we sought to determine if the proteasomal ATPases from eukaryotes and archaea exhibit similar unfolding kinetics. We found that the proteasomal ATPases appear to use a different kinetic strategy for protein unfolding, behaving as a slower but more processive and efficient translocation motor, particularly when encountering a folded domain. We expect that these dissimilarities are due to differences in the ATP binding/exchange cycle, the presence of a trans-arginine finger, or the presence of a threading ring (i.e., the OB domain), which may be used as a rigid platform to pull folded domains against. We speculate that these differences may have evolved due to the differing client pools these machines are expected to encounter. äThe Proteasomal ATPases Use a Slow but Highly Processive Strategy to U(epmc).pdf DeepDyve Pubget Overpricing