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Madeline A. Shea
Researcher at Roy J. and Lucille A. Carver College of Medicine
Publications - 62
Citations - 4637
Madeline A. Shea is an academic researcher from Roy J. and Lucille A. Carver College of Medicine. The author has contributed to research in topics: Calmodulin & Calcium. The author has an hindex of 31, co-authored 60 publications receiving 4399 citations. Previous affiliations of Madeline A. Shea include Johns Hopkins University & University of Kansas.
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Journal ArticleDOI
Backbone resonance assignments of complexes of human voltage-dependent sodium channel Na V 1.2 IQ motif peptide bound to apo calmodulin and to the C-domain fragment of apo calmodulin.
TL;DR: Human voltage-gated sodium channel NaV1.2 has a single pore-forming α-subunit and two transmembrane β-subunits, and the chemical shifts of residues in NaV 1.2IQp and in the C-domain of CaM were nearly identical regardless of whether CaMN was covalently linked to CaMC, suggesting that CaMN does not influence apo CaM binding to NaV2.2 IQp.
Journal ArticleDOI
Novel CALM3 Variant Causing Calmodulinopathy With Variable Expressivity in a 4-Generation Family
Koichi Kato,Holly M. Isbell,Véronique Fressart,Isabelle Denjoy,A Debbiche,Hideki Itoh,Jacques Poinsot,Alfred L. George,Alain Coulombe,Madeline A. Shea,Pascale Guicheney +10 more
TL;DR: The variably expressed phenotype of this variant compared with previously published de novo LQTS-CaM variants is likely explained by a milder impairment of ICaL inactivation combined with IKs augmentation.
Journal ArticleDOI
The Nkd EF-hand domain modulates divergent wnt signaling outputs in zebrafish
Autumn N. Marsden,Sarah W. Derry,Sarah W. Derry,Igor Schneider,Igor Schneider,C. Anthony Scott,Trudi A. Westfall,Lindy K. Brastrom,Madeline A. Shea,Deborah V. Dawson,Diane C. Slusarski +10 more
TL;DR: It is revealed that the zebrafish Nkd1 EF-hand is essential to balance Wnt signaling inputs and modulate the appropriate outputs, while the Drosophila-like EF-Hand primarily functions in β-catenin signaling.
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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.
Ryan Mahling,Liam Hovey,Holly M. Isbell,Dagan C. Marx,Mark S. Miller,Adina M. Kilpatrick,Lisa D. Weaver,Jesse B. Yoder,Elaine H. Kim,Corinne N.J. Andresen,Shuxiang Li,Madeline A. Shea +11 more
TL;DR: In this paper, a solution structure (6BUT) and other NMR evidence showed that the CaM N domain (CaMN) is structurally independent of the C-domain (CaMC) whether CaM is bound to the NaV1.2 IQ motif favorably under resting (apo) conditions and bound calcium normally at CaMN sites.
Journal ArticleDOI
Calmodulin Regulation of the Neuronal Voltage-Dependent Sodium Channel
TL;DR: Understanding the interface between CaM and the IQ-motif of the channel will result in a more complete model of how CaM regulates Nav1.2 function at low physiological [Ca2+] in neuronal tissues.