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10.1016/j.ceca.2018.11.004

http://scihub22266oqcxt.onion/10.1016/j.ceca.2018.11.004
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30470536!ä!30470536

suck abstract from ncbi

pmid30470536      Cell+Calcium 2018 ; 76 (ä): 129-131
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  • 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]


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