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10.1016/j.sbi.2015.12.009 http://scihub22266oqcxt.onion/10.1016/j.sbi.2015.12.009 C4834239!4834239!26803284     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26803284&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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       Curr+Opin+Struct+Biol 2016 ; 37 (ä): 90-6 Nephropedia Template TP {{tp|p=26803284|t=2016. Visualizing Microtubule Structural Transitions and Interactions with Associated Proteins |pdf=|usr=}}{{26803284}} gab.com Text Visualizing Microtubule Structural Transitions and Interactions with Associated Proteins JO: Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=26803284 #FOAvip Microtubules (MTs) have been the subject of cryo-electron microscopy (cryo-EM) studies since the birth of this technique. Although MTs pose some unique challenges, having to do with the presence of a MT seam, lattice variability and disorder, MT cryo-EM reconstructions are steadily improving in resolution and providing exciting new insights into MT structure and function. Recent work has lead to the atomic-detail visualization of lateral contacts between tubulin subunits and the conformational changes that give rise to strain in the MT lattice accompanying GTP hydrolysis. Cryo-EM has also been invaluable in describing the interactions between MTs and MT associated proteins (MAPs), which function to regulate MT dynamic instability, move cargoes, or contribute to other MT cellular processes. Twit Text FOAVip Visualizing Microtubule Structural Transitions and Interactions with Associated Proteins ????Curr Opin Struct Biol http://www.kidney.de/pget.php?&tw=1&pmid=26803284 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26803284 #FOAvip English Wikipedia <ref>{{Cite pmid|26803284}}</ref> Visualizing Microtubule Structural Transitions and Interactions with Associated Proteins #MMPMID26803284 Nogales E; Zhang R Curr Opin Struct Biol 2016[Apr]; 37 (ä): 90-6 PMID26803284show ga Microtubules (MTs) have been the subject of cryo-electron microscopy (cryo-EM) studies since the birth of this technique. Although MTs pose some unique challenges, having to do with the presence of a MT seam, lattice variability and disorder, MT cryo-EM reconstructions are steadily improving in resolution and providing exciting new insights into MT structure and function. Recent work has lead to the atomic-detail visualization of lateral contacts between tubulin subunits and the conformational changes that give rise to strain in the MT lattice accompanying GTP hydrolysis. Cryo-EM has also been invaluable in describing the interactions between MTs and MT associated proteins (MAPs), which function to regulate MT dynamic instability, move cargoes, or contribute to other MT cellular processes. äVisualizing Microtubule Structural Transitions and Interactions with A(epmc).pdf DeepDyve Pubget Overpricing