Literature DB >> 30470536

TRPM7 reflected in Cryo-EMirror.

Vladimir Chubanov1, Lorenz Mittermeier2, Thomas Gudermann3.   

Abstract

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.
Copyright © 2018 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  Magnesium; TRP channels; TRPM2; TRPM6; TRPM7

Mesh:

Substances:

Year:  2018        PMID: 30470536     DOI: 10.1016/j.ceca.2018.11.004

Source DB:  PubMed          Journal:  Cell Calcium        ISSN: 0143-4160            Impact factor:   6.817


  3 in total

1.  TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1.

Authors:  Kristyna Bousova; Monika Zouharova; Petr Herman; Veronika Vetyskova; Katerina Jiraskova; Jiri Vondrasek
Journal:  Heliyon       Date:  2021-11-27

2.  TRPM6 N-Terminal CaM- and S100A1-Binding Domains.

Authors:  Monika Zouharova; Petr Herman; Kateřina Hofbauerová; Jiri Vondrasek; Kristyna Bousova
Journal:  Int J Mol Sci       Date:  2019-09-09       Impact factor: 5.923

Review 3.  Mapping TRPM7 Function by NS8593.

Authors:  Vladimir Chubanov; Thomas Gudermann
Journal:  Int J Mol Sci       Date:  2020-09-23       Impact factor: 5.923

  3 in total

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