Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Aldo Meizoso-Huesca"'
Autor:
Rocío Alcántara-Hernández, Aurelio Hernández-Méndez, Gisselle A Campos-Martínez, Aldo Meizoso-Huesca, J Adolfo García-Sáinz
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0140583 (2015)
The lysophosphatidic acid receptors LPA1, LPA2, and LPA3 were individually expressed in C9 cells and their signaling and regulation were studied. Agonist-activation increases intracellular calcium concentration in a concentration-dependent fashion. P
Externí odkaz:
https://doaj.org/article/225ff1ace72d457cb5485e3689921364
Autor:
Crystal Seng, Luke Pearce, Aldo Meizoso-Huesca, Daniel P. Singh, Robyn M. Murphy, Cedric R. Lamboley, Bradley S. Launikonis
Publikováno v:
American Journal of Physiology-Cell Physiology. 323:C1285-C1289
Ca2+ is an integral component of the functional and developmental regulation of the mitochondria. In skeletal muscle, Ca2+ is reported to modulate the rate of ATP resynthesis, regulate the expression of peroxisome proliferator-activated receptor-gamm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d390e02ddb7831983faacc5a7e86b494
https://doi.org/10.1152/ajpcell.00092.2022
https://doi.org/10.1152/ajpcell.00092.2022
Autor:
Daniel P. Singh, Luke Pearce, Rocky H. Choi, Aldo Meizoso-Huesca, Stefan G. Wette, John W. Scott, Cedric R. Lamboley, Robyn M. Murphy, Bradley S. Launikonis
Publikováno v:
Proceedings of the National Academy of Sciences. 120
Resting skeletal muscle generates heat for endothermy in mammals but not amphibians, while both use the same Ca 2+ -handling proteins and membrane structures to conduct excitation–contraction coupling apart from having different ryanodine receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01dcd7dcca02bd3aba3e5270488ae9f3
https://doi.org/10.1073/pnas.2117503120
https://doi.org/10.1073/pnas.2117503120
Autor:
Luke Pearce, Aldo Meizoso‐Huesca, Crystal Seng, Cedric R. Lamboley, Daniel P. Singh, Bradley S. Launikonis
Publikováno v:
The Journal of Physiology.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a498616a02ab29a2ea34d5847e1571be
https://doi.org/10.1113/jp279512
https://doi.org/10.1113/jp279512
Autor:
Jack U. Flanagan, Ryan E. Yoast, Gregory R. Monteith, Bradley S. Launikonis, Irina Vetter, Iman Azimi, Ping Xin, Mohamed Trebak, Jeevak Sopanrao Kapure, Martin Johnson, Mark R. Ashton, Aldo Meizoso-Huesca, Benjamin P. Ross, Xuexin Zhang, Silke B. Chalmers, Ralph J. Stevenson, William A. Denny
Publikováno v:
ACS Pharmacology & Translational Science. 3:135-147
Store-operated calcium (Ca2+) entry is an important homeostatic mechanism in cells, whereby the release of Ca2+ from intracellular endoplasmic reticulum stores triggers the activation of a Ca2+ influx pathway. Mediated by Orai1, this Ca2+ influx has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b28ef4e60f28fbdda21f83956ca5309e
https://doi.org/10.1021/acsptsci.9b00081
https://doi.org/10.1021/acsptsci.9b00081
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance The evolution of mammals to use skeletal muscle as a source of heat allowed them to spread to all parts of the globe. The generation of heat requires increased adenosine triphosphate (ATP) hydrolysis in the resting muscle in a regulated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe4aa994ba9ad31e4e7c66c815219d50
https://doi.org/10.1073/pnas.2119203119
https://doi.org/10.1073/pnas.2119203119
Autor:
Luke, Pearce, Aldo, Meizoso-Huesca, Crystal, Seng, Cedric R, Lamboley, Daniel P, Singh, Bradley S, Launikonis
Publikováno v:
The Journal of physiologyReferences.
Store-operated Ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::839a5b30cf70fe78eb5a9001f01e993c
https://pubmed.ncbi.nlm.nih.gov/35218018
https://pubmed.ncbi.nlm.nih.gov/35218018
Autor:
Iman, Azimi, Ralph J, Stevenson, Xuexin, Zhang, Aldo, Meizoso-Huesca, Ping, Xin, Martin, Johnson, Jack U, Flanagan, Silke B, Chalmers, Ryan E, Yoast, Jeevak S, Kapure, Benjamin P, Ross, Irina, Vetter, Mark R, Ashton, Bradley S, Launikonis, William A, Denny, Mohamed, Trebak, Gregory R, Monteith
Publikováno v:
ACS pharmacologytranslational science. 3(1)
Store operated calcium (Ca(2+)) entry is an important homeostatic mechanism in cells, whereby the release of Ca(2+) from intracellular endoplasmic reticulum stores triggers the activation of a Ca(2+) influx pathway. Mediated by Orai1, this Ca(2+) inf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::334f50c1ea210ae9f96369fe5f0bb3d8
https://pubmed.ncbi.nlm.nih.gov/32190822
https://pubmed.ncbi.nlm.nih.gov/32190822
Autor:
Robyn M. Murphy, Barnaby P. Frankish, Bradley S. Launikonis, Harriet P. Lo, Paul D. Allen, Aldo Meizoso-Huesca, Luke Pearce, Cedric R. Lamboley, Chris van der Poel, Charles Ferguson, Robert G. Parton, Crystal Seng, Christopher John Barclay, Vikas Kaura, Daniel P. Singh, Philip M. Hopkins
Publikováno v:
Science Advances
Description
RyR1 Ca2+ leak causes a cascade of events that shifts Ca2+ to the cytoplasm and mitochondria, supporting force generation.
Muscle contraction depends on tightly regulated Ca2+ release. Aberrant Ca2+ leak through ryanodine recept
RyR1 Ca2+ leak causes a cascade of events that shifts Ca2+ to the cytoplasm and mitochondria, supporting force generation.
Muscle contraction depends on tightly regulated Ca2+ release. Aberrant Ca2+ leak through ryanodine recept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f23394ad8035d2256dda06c6eae76be
Publikováno v:
The Journal of General Physiology
Meizoso-Huesca and Launikonis describe multiple effects of BTP2, an inhibitor of the Ca2+ channel Orai1, on Ca2+ handling in skeletal muscle, which include impairment of Ca2+ release from the sarcoplasmic reticulum and indirect effects on the activit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8388019f9e0dfcbc7d4a4c775cace01
https://pubmed.ncbi.nlm.nih.gov/33316029
https://pubmed.ncbi.nlm.nih.gov/33316029