The crystal structure of <scp>TRPM2 MHR1</scp> /2 domain reveals a conserved Zn <sup>2+</sup> ‐binding domain essential for structural integrity and channel activity-Reference-Cited by-同舟云学术

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The crystal structure of TRPM2 MHR1 /2 domain reveals a conserved Zn ²⁺ ‐binding domain essential for structural integrity and channel activity

Published:2022-05-17 Issue:6 Volume:31 Page:
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Sander Simon¹^ORCID,Pick Jelena²^ORCID,Gattkowski Ellen¹,Fliegert Ralf²,Tidow Henning¹^ORCID

Affiliation:

1. Hamburg Advanced Research Centre for Bioorganic Chemistry (HARBOR) & Department of Chemistry Institute for Biochemistry and Molecular Biology, University of Hamburg Hamburg Germany

2. The Calcium Signaling Group, Department of Biochemistry and Molecular Cell Biology University Medical Center Hamburg‐Eppendorf Hamburg Germany

Funder

Deutsche Forschungsgemeinschaft

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4320

Reference50 articles.

1. Identification of a cold receptor reveals a general role for TRP channels in thermosensation

2. The TRPM2 ion channel is required for sensitivity to warmth

3. The TRPM2 channel is a hypothalamic heat sensor that limits fever and can drive hypothermia;Siemens J;Science (80‐).,2016

4. The TRPM Cation Channels in the Immune Context

5. Mg2+ Homeostasis: The Mg2+nificent TRPM Chanzymes

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1. Calcium’s Role and Signaling in Aging Muscle, Cellular Senescence, and Mineral Interactions;International Journal of Molecular Sciences;2023-12-01

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