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10.1002/bip.22856 http://scihub22266oqcxt.onion/10.1002/bip.22856 C4879348!4879348!27062277     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       Biopolymers 2016 ; 105 (8): 557-67 Nephropedia Template TP {{tp|p=27062277|t=2016. Review: Structure and mechanism of the dynein motor ATPase |pdf=|usr=}}{{27062277}} gab.com Text Review: Structure and mechanism of the dynein motor ATPase JO: Biopolymers http://www.kidney.de/pget.php?&tw=1&pmid=27062277 #FOAvip Dyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest individual component of the dynein complex is the heavy chain. Its C?terminal 3500 amino?acid residues form the motor domain, which hydrolyses ATP in its ring of AAA+ (ATPases associated with diverse cellular activities) domains to generate the force for movement. The production of force is synchronized with cycles of microtubule binding and release, another important prerequisite for efficient motility along the microtubule. Although the large scale conformational changes that lead to force production and microtubule affinity regulation are well established, it has been largely enigmatic how ATP?hydrolysis in the AAA+ ring causes these rearrangements. The past five years have seen a surge of high resolution information on the dynein motor domain that finally allowed unprecedented insights into this important open question. This review, part of the ?ATP and GTP hydrolysis in Biology? special issue, will summarize our current understanding of the dynein motor mechanism with a special emphasis on the recently obtained crystal and EM structures. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 557?567, 2016. Twit Text FOAVip Review: Structure and mechanism of the dynein motor ATPase ????Biopolymers http://www.kidney.de/pget.php?&tw=1&pmid=27062277 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27062277 #FOAvip English Wikipedia <ref>{{Cite pmid|27062277}}</ref> Review: Structure and mechanism of the dynein motor ATPase #MMPMID27062277 Schmidt H; Carter AP Biopolymers 2016[Aug]; 105 (8): 557-67 PMID27062277show ga Dyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest individual component of the dynein complex is the heavy chain. Its C?terminal 3500 amino?acid residues form the motor domain, which hydrolyses ATP in its ring of AAA+ (ATPases associated with diverse cellular activities) domains to generate the force for movement. The production of force is synchronized with cycles of microtubule binding and release, another important prerequisite for efficient motility along the microtubule. Although the large scale conformational changes that lead to force production and microtubule affinity regulation are well established, it has been largely enigmatic how ATP?hydrolysis in the AAA+ ring causes these rearrangements. The past five years have seen a surge of high resolution information on the dynein motor domain that finally allowed unprecedented insights into this important open question. This review, part of the ?ATP and GTP hydrolysis in Biology? special issue, will summarize our current understanding of the dynein motor mechanism with a special emphasis on the recently obtained crystal and EM structures. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 557?567, 2016. äReview: Structure and mechanism of the dynein motor ATPase (epmc).pdf DeepDyve Pubget Overpricing