Zobrazeno 1 - 10
of 85
pro vyhledávání: '"Madeline A. Shea"'
Autor:
Koichi, Kato, Holly M, Isbell, Véronique, Fressart, Isabelle, Denjoy, Amal, Debbiche, Hideki, Itoh, Jacques, Poinsot, Alfred L, George, Alain, Coulombe, Madeline A, Shea, Pascale, Guicheney
Publikováno v:
Circulation. Arrhythmia and electrophysiology. 15(3)
CaM (calmodulin), encoded by 3 separate genes (We performed whole exome sequencing for a large, 4-generation family affected by LQTS. To assess the effect of the detectedWe identified 14 p.N138K-CaM carriers in a family where 2 sudden deaths occurred
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f9a10bce85e46aeda707877fa51f38e6
https://pubmed.ncbi.nlm.nih.gov/35225649
https://pubmed.ncbi.nlm.nih.gov/35225649
Autor:
Koichi Kato, Holly M. Isbell, Véronique Fressart, Isabelle Denjoy, Amal Debbiche, Hideki Itoh, Jacques Poinsot, Alfred L. George, Alain Coulombe, Madeline A. Shea, Pascale Guicheney
Publikováno v:
Circulation: Arrhythmia and Electrophysiology. 15
Background:CaM (calmodulin), encoded by 3 separate genes (CALM1, CALM2, and CALM3), is a multifunctional Ca2+-binding protein involved in many signal transduction events including ion channel regulation. CaM variants may present with early-onset long
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a47cb91233f5c43c21b5b0b8d73b39b
https://doi.org/10.1161/circep.121.010572
https://doi.org/10.1161/circep.121.010572
Autor:
Kevin R. Murphy, Vadim N. Gladyshev, Anthony Cammarato, Holly M. Isbell, Bruno Manta, Klitos Konstantinidis, Mario A. Bianchet, Fujian Lu, Meera C. Viswanathan, Lo Lai, Elizabeth D. Luczak, Donghui Zhang, Vassilios J. Bezzerides, Jonathan M. Granger, Rodney L. Levine, Thomas J. Hund, Qiang Wang, Mark N. Wu, William T. Pu, Madeline A. Shea, Alex L. Kolodkin, Daniel Gratz, Ian D. Blum, Danielle A. Heims-Waldron, An-Chi Wei, Mark E. Anderson, Qinchuan Wang, Yuejin Wu
Publikováno v:
J Clin Invest
Oxidant stress can contribute to health and disease. Here we show that invertebrates and vertebrates share a common stereospecific redox pathway that protects against pathological responses to stress, at the cost of reduced physiological performance,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90a80e0f446ebb142a4cde4b056e2bd9
https://doi.org/10.1172/jci133181
https://doi.org/10.1172/jci133181
Publikováno v:
The Journal of Biological Chemistry
Voltage-gated sodium channels (Navs) are tightly regulated by multiple conserved auxiliary proteins, including the four fibroblast growth factor homologous factors (FGFs), which bind the Nav EF-hand like domain (EFL), and calmodulin (CaM), a multifun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b930dde359327245b32bdf269984067b
https://pubmed.ncbi.nlm.nih.gov/33639159
https://pubmed.ncbi.nlm.nih.gov/33639159
Publikováno v:
Biophysical Journal. 121:340a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::084a6b22037f2bd4c9c86f5bb345d359
https://doi.org/10.1016/j.bpj.2021.11.1087
https://doi.org/10.1016/j.bpj.2021.11.1087
Publikováno v:
Biomolecular NMR Assignments. 12:283-289
Human voltage-gated sodium (NaV) channels are critical for initiating and propagating action potentials in excitable cells. Nine isoforms have different roles but similar topologies, with a pore-forming α-subunit and auxiliary transmembrane β-subun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::648406eb3f8ef2707bf1d2bd59faa4c8
https://doi.org/10.1007/s12104-018-9824-5
https://doi.org/10.1007/s12104-018-9824-5
Autor:
Dagan C. Marx, Mark S. Miller, Lisa D. Weaver, Corinne N.J. Andresen, Ryan Mahling, Liam Hovey, Elaine H. Kim, Adina M. Kilpatrick, Shuxiang Li, Jesse B. Yoder, Holly M. Isbell, Madeline A. Shea
Publikováno v:
Structure
Neuronal voltage-gated sodium channel Na(V)1.2 C-terminal domain (CTD) binds calmodulin (CaM) constitu-tively at its IQ motif. A solution structure (6BUT) and other NMR evidence showed that the CaM N domain (CaM(N)) is structurally independent of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e6a04ef868725ae46015ae05a08d2da
https://doi.org/10.1016/j.str.2021.03.002
https://doi.org/10.1016/j.str.2021.03.002
Publikováno v:
Biomolecular NMR Assignments. 11:297-303
Human voltage-gated sodium channel NaV1.2 has a single pore-forming α-subunit and two transmembrane β-subunits. Expressed primarily in the brain, NaV1.2 is critical for initiation and propagation of action potentials. Milliseconds after the pore op
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d53d244adcfb723807e9a99fa212ffc
https://doi.org/10.1007/s12104-017-9767-2
https://doi.org/10.1007/s12104-017-9767-2
Publikováno v:
Biomolecular NMR Assignments. 11:275-280
Calcineurin (CaN) is a heterodimeric and highly conserved serine/threonine phosphatase (PP2B) that plays a critical role in coupling calcium signals to physiological processes including embryonic cardiac development, NF-AT-regulated gene expression i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75e3e211f69ee7f8baed1a3ce3716405
https://doi.org/10.1007/s12104-017-9762-7
https://doi.org/10.1007/s12104-017-9762-7
Autor:
Dagan C. Marx, Ryan Mahling, Jesse B. Yoder, Madeline A. Shea, C. Andrew Fowler, Kristin M. Tefft, Liping Yu, Michael D. Feldkamp, Mark S. Miller, Brett C. Waite, Zesen Lin, Liam Hovey, Elaine H. Kim
Publikováno v:
Biophysical Chemistry. 224:1-19
Several members of the voltage-gated sodium channel family are regulated by calmodulin (CaM) and ionic calcium. The neuronal voltage-gated sodium channel NaV1.2 contains binding sites for both apo (calcium-depleted) and calcium-saturated CaM. We have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ded627771a11a9fc18daa89c0154d011
https://doi.org/10.1016/j.bpc.2017.02.006
https://doi.org/10.1016/j.bpc.2017.02.006