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10.1038/ncomms15035 http://scihub22266oqcxt.onion/10.1038/ncomms15035 C5418579!5418579 !28462916     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 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\28462916 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2017 ; 8 (ä): 15035 Nephropedia Template TP {{tp|p=28462916 |t=2017. Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins |pdf=|usr=}}{{28462916 }} gab.com Text Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28462916 #FOAvip Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign ?- and ?-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule. Twit Text FOAVip Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28462916 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28462916 #FOAvip English Wikipedia <ref>{{Cite pmid|28462916 }}</ref> Subnanometre-resolution structure of the doublet microtubule reveals new classes of microtubule-associated proteins #MMPMID28462916 Ichikawa M ; Liu D ; Kastritis PL ; Basu K ; Hsu TC ; Yang S ; Bui KH Nat Commun 2017[May]; 8 (ä): 15035 PMID28462916 show ga Cilia are ubiquitous, hair-like appendages found in eukaryotic cells that carry out functions of cell motility and sensory reception. Cilia contain an intriguing cytoskeletal structure, termed the axoneme that consists of nine doublet microtubules radially interlinked and longitudinally organized in multiple specific repeat units. Little is known, however, about how the axoneme allows cilia to be both actively bendable and sturdy or how it is assembled. To answer these questions, we used cryo-electron microscopy to structurally analyse several of the repeating units of the doublet at sub-nanometre resolution. This structural detail enables us to unambiguously assign ?- and ?-tubulins in the doublet microtubule lattice. Our study demonstrates the existence of an inner sheath composed of different kinds of microtubule inner proteins inside the doublet that likely stabilizes the structure and facilitates the specific building of the B-tubule. |Amino Acid Sequence [MESH] |Axoneme/*chemistry/ultrastructure [MESH] |Binding Sites [MESH] |Cilia/*chemistry/ultrastructure [MESH] |Cryoelectron Microscopy [MESH] |Cytoskeleton/chemistry/ultrastructure [MESH] |Flagella/chemistry/ultrastructure [MESH] |Microtubule-Associated Proteins/chemistry/genetics/metabolism [MESH] |Microtubules/*chemistry/ultrastructure [MESH] |Models, Molecular [MESH] |Protein Binding [MESH] |Protein Conformation, alpha-Helical [MESH] |Protein Conformation, beta-Strand [MESH] |Protein Interaction Domains and Motifs [MESH] |Protein Isoforms/chemistry/genetics/metabolism [MESH] |Protozoan Proteins/*chemistry/genetics/metabolism [MESH] |Sequence Alignment [MESH] |Sequence Homology, Amino Acid [MESH] |Tetrahymena thermophila/*chemistry/ultrastructure [MESH] |Thermodynamics [MESH]Subnanometre-resolution structure of the doublet microtubule reveals n(epmc).pdf DeepDyve Pubget Overpricing