K
Keith K. Schlender
Researcher at University of Toledo Medical Center
Publications - 42
Citations - 1168
Keith K. Schlender is an academic researcher from University of Toledo Medical Center. The author has contributed to research in topics: Phosphatase & Glycogen synthase. The author has an hindex of 18, co-authored 42 publications receiving 1138 citations.
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Journal ArticleDOI
Gap‐junction disassembly and connexin 43 dephosphorylation induced by 18β‐glycyrrhetinic acid
TL;DR: In this article, the authors provided morphological evidence that 18 beta-glycyrrhetinic acid (18 beta-GA), a saponin isolated from licorice root that is an inhibitor of gap junctional communication, caused the disassembly of gap-junction plaques in WB-F344 rat liver epithelial cells.
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The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase.
Zhehui Feng,Susan E. Wilson,Zao-Yuan Peng,Keith K. Schlender,Erwin M. Reimann,Robert J. Trumbly +5 more
TL;DR: The GLC7 mRNA was identified as a 1.4-kilobase RNA that increases 4-fold at the end of exponential growth in wild-type cells, suggesting that activation of glycogen synthase is mediated by increased expression of protein phosphatase 1 as cells reach stationary phase.
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Cardiac myosin-binding protein C (MyBP-C): identification of protein kinase A and protein kinase C phosphorylation sites.
TL;DR: All of the cardiac MyBP-C phosphorylation sites are absent in known sequences of skeletal muscle My BP-C isoforms.
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Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II.
Keith K. Schlender,L J Bean +1 more
TL;DR: Peptide mapping indicated that some of the sites phosphorylated by CaM-kinase II were located on the same phosphopeptides obtained when C-protein was phosphorylation by the cAMP-dependent protein kinase (peptides T1, T2, and T3).
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Activation of Protein Phosphatase 1 FORMATION OF A METALLOENZYME
TL;DR: Zhang et al. as mentioned in this paper investigated the effects of divalent cations on the activity of recombinant catalytic subunit of protein phosphatase 1 and showed that at least two metal binding sites exist on the enzyme and that it may be an iron/zinc metalloprotein in vivo.