Zobrazeno 1 - 10
of 76
pro vyhledávání: '"TASK-2"'
Publikováno v:
Journal of Animal Reproduction and Biotechnology, Vol 30, Iss 4, Pp 277-282 (2015)
Cryopreservation affects osmotic tolerance and intracellular ion concentration through changes in expression levels of water and ion channels. Control of these changes is important for cell survival after cryopreservation. Relatively little is known
Externí odkaz:
https://doaj.org/article/a3235c2997924700ad3c069946e8c3ea
Publikováno v:
Cellular Physiology and Biochemistry, Vol 32, Iss 5, Pp 1238-1246 (2013)
Background/Aims: Regulatory volume decrease (RVD) in response to acute cell swelling is well described and KCNK5 (also known as TASK-2 or K2P5.1) has been shown to be the volume sensitive K+ channel in Ehrlich cells. Very little is, on the other hand
Externí odkaz:
https://doaj.org/article/603e1d992c734c29b7ea698aeac1ef41
Autor:
Mariangela Centrone, Maria Penelope De Santo, Isabella Nicotera, Cristina Labate, Marianna Ranieri, Annarita Di Mise, Maria Grazia Mola, Maria Mastrodonato, Rosangela Elliani, Riccardo Barberi, Vincenzo Formoso, Grazia Tamma, Giovanna Valenti
Publikováno v:
Cells, Vol 7, Iss 12, p 276 (2018)
Vesicle fusion is a fundamental cell biological process similar from yeasts to humans. For secretory vesicles, swelling is considered a step required for the expulsion of intravesicular content. Here this concept is revisited providing evidence that
Externí odkaz:
https://doaj.org/article/cc7483a4520f4148a6802ec6b80ad4a7
Autor:
Niemeyer, Maria Isabel, González-Nilo, Fernando D., Zúñiga, Leandro, González, Wendy, Cid, L. Pablo, Sepúlveda, Francisco V.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2007 Jan 01. 104(2), 666-671.
Externí odkaz:
https://www.jstor.org/stable/25426159
Autor:
Luis Pablo Cid, Hugo A Roa-Rojas, Maria Isabel eNiemeyer, Wendy eGonzalez, Masatake eAraki, Kimi eAraki, Francisco eSepulveda
Publikováno v:
Frontiers in Physiology, Vol 4 (2013)
TASK-2 (K2P5.1) is a two-pore domain K+ channel belonging to the TALK subgroup of the K2P family of proteins. TASK-2 has been shown to be activated by extra- and intracellular alkalinisation. Extra- and intracellular pH-sensors reside at arginine 224
Externí odkaz:
https://doaj.org/article/786a7be601864207a1b219da415db3bd
Akademický článek
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Autor:
Syeda, Fahima, Holmes, Andrew P., Yu, Ting Y., Tull, Samantha, Kuhlmann, Stefan Michael, Pavlovic, Davor, Betney, Daniel, Riley, Genna, Kucera, Jan P., Jousset, Florian, de Groot, Joris R., Rohr, Stephan, Brown, Nigel A., Fabritz, Larissa, Kirchhof, Paulus
Publikováno v:
Journal of the American College of Cardiology
Background Antiarrhythmic drugs are widely used to treat patients with atrial fibrillation (AF), but the mechanisms conveying their variable effectiveness are not known. Recent data suggested that paired like homeodomain-2 transcription factor (PITX2
Akademický článek
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Autor:
Koudrina, Natalia
Fish naturally experience fluctuating levels of O2 and CO2 in their environment. To cope with the deleterious effects of lowered O2 (hypoxia) or elevated CO2 (hypercapnia), fish exhibit an array of cardiorespiratory adjustments aimed at preserving ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::470f487803d8e11a88e9a90a60d4cd71
Autor:
Erix W. Hernández-Rodríguez, Guierdy Concha, Mauricio Bedoya, David Ramírez, Leandro Zúñiga, Daniel Bustos, Niels Decher, Francisco V. Sepúlveda, Leandro Martínez, Wendy González
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 2
International Journal of Molecular Sciences, Vol 21, Iss 2, p 532 (2020)
Volume 21
Issue 2
International Journal of Molecular Sciences, Vol 21, Iss 2, p 532 (2020)
Two-pore domain potassium (K2P) channels maintain the cell&rsquo
s background conductance by stabilizing the resting membrane potential. They assemble as dimers possessing four transmembrane helices in each subunit. K2P channels were crystallize
s background conductance by stabilizing the resting membrane potential. They assemble as dimers possessing four transmembrane helices in each subunit. K2P channels were crystallize