Zobrazeno 1 - 10
of 42
pro vyhledávání: '"pore helix"'
Autor:
Kunitoshi Uchida, Tomo Kita, Mitsutoki Hatta, Satoru G. Itoh, Hisashi Okumura, Makoto Tominaga, Jun Yamazaki
Publikováno v:
Heliyon, Vol 7, Iss 1, Pp e06102- (2021)
The transient receptor potential melastatin 5 (TRPM5) channel is a monovalent-permeable cation channel that is activated by intracellular Ca2+. Expression of TRPM5 has been shown in taste cells, pancreas, brainstem and olfactory epithelium, and this
Externí odkaz:
https://doaj.org/article/3090c84e1e064359a34cb27f75a072f4
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in Molecular Bioscience
Frontiers in Molecular Biosciences
Frontiers in Molecular Bioscience
Frontiers in Molecular Biosciences
CRAC channel is ubiquitous and its importance in the regulation of the immune system is testified by the severe immunodeficiencies caused by its mutations. In this work we took advantage of the availability of open and closed structures of this chann
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf570d57dec0671284ba250fede5cf1e
https://doi.org/10.3389/fmolb.2021.773388
https://doi.org/10.3389/fmolb.2021.773388
Autor:
Sen-Fang Sui, Wenlong Zhao
Publikováno v:
Chinese Science Bulletin = Kexue Tongbao
The Nobel Prize in Chemistry for 2003 was awarded to two biologists, Peter Agre in Johns Hopkins School of Medicine and Roderick MacKinnon from Howard Hughes Medical Institute in Rockefeller University, who have made fundamental discoveries concernin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0bd4c105ac919589e9b8caae89a1c05
https://pubmed.ncbi.nlm.nih.gov/32214718
https://pubmed.ncbi.nlm.nih.gov/32214718
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Tomo Kita, Makoto Tominaga, Satoru G. Itoh, Hisashi Okumura, Mitsutoki Hatta, Jun Yamazaki, Kunitoshi Uchida
Publikováno v:
Heliyon
Heliyon, Vol 7, Iss 1, Pp e06102-(2021)
Heliyon, Vol 7, Iss 1, Pp e06102-(2021)
The transient receptor potential melastatin 5 (TRPM5) channel is a monovalent-permeable cation channel that is activated by intracellular Ca2+. Expression of TRPM5 has been shown in taste cells, pancreas, brainstem and olfactory epithelium, and this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7576633af55a43c255165a733ca02e53
https://doi.org/10.1016/j.heliyon.2021.e06102
https://doi.org/10.1016/j.heliyon.2021.e06102
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Jian Xiong, Yungang Lu, Min Li, Zhaobing Gao, Xia Wan, Xueqin Chen, Michael X. Zhu, Ping Li, Bingqing Xia, Yuanda Zhou
Publikováno v:
Pflugers Archiv
Transient receptor potential A1 (TRPA1) is implicated in somatosensory processing and pathological pain sensation. Although not strictly voltage-gated, ionic currents of TRPA1 typically rectify outwardly, indicating channel activation at depolarized
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10c58c4aa2af13a9523df97e26b46f2a
http://europepmc.org/articles/PMC4062818
http://europepmc.org/articles/PMC4062818
Autor:
Willem J. Laursen, Elena O. Gracheva, Sviatoslav N. Bagriantsev, Evan O. Anderson, Lydia J. Hoffstaetter
Publikováno v:
Temperature: Multidisciplinary Biomedical Journal
Transient receptor potential ankyrin 1 (TRPA1) is a polymodal ion channel sensitive to temperature and chemical stimuli. The importance of temperature and aversive chemical detection for survival has driven the evolutionary diversity of TRPA1 sensiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e1593da0a7b9db92b9d077d0bde95de
https://pubmed.ncbi.nlm.nih.gov/27227025
https://pubmed.ncbi.nlm.nih.gov/27227025
Publikováno v:
The Journal of General Physiology
The pores of glutamate receptors and K+ channels share sequence homology, suggesting a conserved secondary structure. Scanning mutagenesis with substitution of alanine and tryptophan in GluR6 channels was performed based on the structure of KcsA. Our
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67b8764507c08ee9a30d75609bbf1bf6
https://doi.org/10.1085/jgp.117.4.345
https://doi.org/10.1085/jgp.117.4.345