E
Emanuel E. Strehler
Researcher at Mayo Clinic
Publications - 133
Citations - 6533
Emanuel E. Strehler is an academic researcher from Mayo Clinic. The author has contributed to research in topics: Plasma membrane Ca2+ ATPase & Calmodulin. The author has an hindex of 44, co-authored 133 publications receiving 6250 citations. Previous affiliations of Emanuel E. Strehler include École Polytechnique Fédérale de Lausanne & ETH Zurich.
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Journal ArticleDOI
Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps.
TL;DR: The identification of mice carrying PMCA mutations that lead to diseases such as hearing loss and ataxia, as well as the corresponding phenotypes of genetically engineered PMCA "knockout" mice further support the concept of specific, nonredundant roles for each Ca( 2+) pump isoform in cellular Ca(2+) regulation.
Journal ArticleDOI
Complete primary structure of a human plasma membrane Ca2+ pump.
Anil K. Verma,Adelaida G. Filoteo,David R. Stanford,Eric D. Wieben,John T. Penniston,Emanuel E. Strehler,R. Fischer,R. Heim,G. Vogel,S Mathews +9 more
TL;DR: Comparison of the cloned sequence with peptide sequences from the erythrocyte Ca2+ pump showed that the two proteins have a very high proportion of identical residues but are not 100% identical, indicating that they represent different isozymes.
Journal ArticleDOI
Multiple divergent mRNAs code for a single human calmodulin.
R Fischer,M Koller,M Flura,S Mathews,M A Strehler-Page,Joachim Krebs,J T Penniston,Ernesto Carafoli,Emanuel E. Strehler +8 more
TL;DR: The results indicate that the human genome contains at least three divergent CaM genes that are under selective pressure to encode an identical protein while maintaining maximally divergent nucleotide sequences.
Journal ArticleDOI
Calcium pumps of plasma membrane and cell interior.
TL;DR: Understanding the involvement of different Ca2+ pump isoforms in the pathogenesis of disease allows their identification as therapeutic targets for the development of selective strategies to prevent or combat the progression of these disorders.
Journal ArticleDOI
Plasma Membrane Ca2+ ATPase Isoform 4b Binds to Membrane-associated Guanylate Kinase (MAGUK) Proteins via Their PDZ (PSD-95/Dlg/ZO-1) Domains
Eunjoon Kim,Steven J. DeMarco,Shirin M. Marfatia,Athar H. Chishti,Morgan Sheng,Emanuel E. Strehler +5 more
TL;DR: Yeast two-hybrid assays demonstrate a direct physical binding of Ca2+ pump isoform 4b to MAGUKs via their PDZ domains and reveal a novel role of alternative splicing within the family of plasma membrane Ca 2+ pumps.