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10.1016/j.ceca.2018.11.004 http://scihub22266oqcxt.onion/10.1016/j.ceca.2018.11.004 30470536!ä!30470536 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=30470536&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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\30470536.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Calcium 2018 ; 76 (ä): 129-131 Nephropedia Template TP {{tp|p=30470536|t=2018. TRPM7 reflected in Cryo-EMirror |pdf=|usr=}}{{30470536}} gab.com Text TRPM7 reflected in Cryo-EMirror JO: Cell Calcium http://www.kidney.de/pget.php?&tw=1&pmid=30470536 #FOAvip TRPM7 is an atypical type of ion channel because its pore-forming moiety is covalently linked to a protein kinase domain. The channel-kinase TRPM7 controls a wide range of biological processes such as mineral homeostasis, immune responses, cell motility, proliferation and differentiation. Earlier this year, Duan J & co-workers [1] published three TRPM7 structures resolved by cryo-electron microscopy (cryo-EM). This study tremendously advances our mechanistic understanding of TRPM7 channel function and forms the basis for informed structure-function assessment of this extraordinary protein. Twit Text FOAVip TRPM7 reflected in Cryo-EMirror ????Cell Calcium http://www.kidney.de/pget.php?&tw=1&pmid=30470536 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30470536 #FOAvip English Wikipedia <ref>{{Cite pmid|30470536}}</ref> TRPM7 reflected in Cryo-EMirror #MMPMID30470536 Chubanov V; Mittermeier L; Gudermann T Cell Calcium 2018[Dec]; 76 (ä): 129-131 PMID30470536show ga TRPM7 is an atypical type of ion channel because its pore-forming moiety is covalently linked to a protein kinase domain. The channel-kinase TRPM7 controls a wide range of biological processes such as mineral homeostasis, immune responses, cell motility, proliferation and differentiation. Earlier this year, Duan J & co-workers [1] published three TRPM7 structures resolved by cryo-electron microscopy (cryo-EM). This study tremendously advances our mechanistic understanding of TRPM7 channel function and forms the basis for informed structure-function assessment of this extraordinary protein. |*TRPM Cation Channels[MESH] |Animals[MESH] |Calcium[MESH] |Cryoelectron Microscopy[MESH] |Homeostasis[MESH] |Humans[MESH] |Magnesium[MESH]TRPM7 reflected in Cryo-EMirror (epmc).pdf DeepDyve Pubget Overpricing