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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
Mutation of Tyr138 disrupts the structural coupling between the opposing domains in vertebrate calmodulin.
TL;DR: Results indicate that alterations in either the hydrogen bond between Tyr138 and Glu82 or contact interactions between aromatic amino acid side chains have the potential to initiate the structural collapse of CaM normally associated with target protein binding and activation.
Journal ArticleDOI
Basic interdomain boundary residues in calmodulin decrease calcium affinity of sites I and II by stabilizing helix-helix interactions
TL;DR: It is concluded that the 3 basic residues in the sequence from 74 to 77 (RKMK) are critical to the increased stability and decreased calcium affinity of the longer N‐domain fragments of Calmodulin.
Journal ArticleDOI
Bohr effects of the partially-ligated (CN-met) intermediates of hemoglobin as probed by quaternary assembly.
TL;DR: The present results show that the "tertiary BohR effect" within quaternary T exceeds the Bohr effect of dissociated dimers, as suggested by Lee and Karplus (1983).
Journal ArticleDOI
Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel Na V 1.2.
Liam Hovey,C. Andrew Fowler,Ryan Mahling,Zesen Lin,Mark S. Miller,Dagan C. Marx,Jesse B. Yoder,Elaine H. Kim,Kristin M. Tefft,Brett C. Waite,Michael D. Feldkamp,Liping Yu,Madeline A. Shea +12 more
TL;DR: Several members of the voltage-gated sodium channel family are regulated by calmodulin (CaM) and ionic calcium, and to understand how calcium triggers conformational change at the CaM-IQ interface, a solution structure of (Ca2+)2-CaMC bound to NaV1.2IQp (2KXW) is determined.
Book ChapterDOI
Proteolytic footprinting titrations for estimating ligand-binding constants and detecting pathways of conformational switching of calmodulin
TL;DR: The unexpected finding that the isolated domains are nearly equivalent in their calcium-binding properties leaves us with many of the questions the authors had at the start: How does the sum of two nearly equivalent domains result in a molecule that switches sequentially rather than simultaneously?