Výsledky vyhledávání - "Holly M, Isbell"

Novel

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

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Novel CALM3 Variant Causing Calmodulinopathy With Variable Expressivity in a 4-Generation Family

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

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Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7

Autor: Holly M. Isbell, Adina M. Kilpatrick, Zesen Lin, Ryan Mahling, Madeline A. Shea

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

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NaV1.2 EFL domain allosterically enhances Ca2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD

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

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Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels Na

Autor: Holly M, Isbell, Adina M, Kilpatrick, Zesen, Lin, Ryan, Mahling, Madeline A, Shea

Publikováno v: Biomolecular NMR assignments. 12(2)

Human voltage-gated sodium (Na(V)) 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-sub

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::076f31749ce6a8dbbfe0eddbb4b3f5c9
https://pubmed.ncbi.nlm.nih.gov/29728980

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