M
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.
Papers
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Journal ArticleDOI
A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
Jeffrey R. Erickson,Mei Ling A. Joiner,Xiaoqun Guan,William Kutschke,Jinying Yang,Carmine V. Oddis,Ryan K. Bartlett,John S. Lowe,Susan E. O'Donnell,Nukhet Aykin-Burns,Matthew C. Zimmerman,Kathy Zimmerman,Amy-Joan L. Ham,Robert M. Weiss,Douglas R. Spitz,Madeline A. Shea,Roger J. Colbran,Peter J. Mohler,Mark E. Anderson +18 more
TL;DR: It is shown that oxidation of paired regulatory domain methionine residues sustains CaMKII activity in the absence of Ca2+/CaM and highlights the critical importance of oxidation-dependent CaMK II activation to AngII and ischemic myocardial apoptosis.
Journal ArticleDOI
Quantitative model for gene regulation by lambda phage repressor
TL;DR: The model predicts repression curves at the divergent promoters PR and PRM that control transcription of genes coding for the regulatory proteins cro and repressor, respectively, and demonstrates the importance of cooperative interactions between repressor dimers bound to the adjacent operator sites OR1 and OR2 in maintaining a stable lysogenic state.
Journal ArticleDOI
The OR control system of bacteriophage lambda. A physical-chemical model for gene regulation.
Madeline A. Shea,Gary K. Ackers +1 more
TL;DR: A quantitative model for processes in the bacteriophage lambda that control the switchover from lysogenic to lytic modes of growth was found capable of predicting essential physiological characteristics of the system over an extended time.
Book ChapterDOI
Quantitative DNase footprint titration: a method for studying protein-DNA interactions.
TL;DR: It is discussed that individual-site binding isotherms are uniquely suited to permit the resolution of interaction parameters for systems exhibiting cooperative interactions between multiple sites.
Journal ArticleDOI
Regulation of Calcium/Calmodulin-dependent Protein Kinase II Docking toN-Methyl-d-aspartate Receptors by Calcium/Calmodulin and α-Actinin
A. Soren Leonard,A. Soren Leonard,K. Ulrich Bayer,Michelle A. Merrill,Michelle A. Merrill,Indra A. Lim,Indra A. Lim,Madeline A. Shea,Howard Schulman,Johannes W. Hell,Johannes W. Hell +10 more
TL;DR: The NR1 C0 region is a key site for recruiting CaMKII to the postsynaptic site, where it may act in concert with calmodulin to modulate the stimulatory role of α-actinin interaction with the NMDA receptor.