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J

Jun Zhang

Researcher at University of Louisville

Publications -  20
Citations -  3084

Jun Zhang is an academic researcher from University of Louisville. The author has contributed to research in topics: Protein kinase C & Protein Kinase C-epsilon. The author has an hindex of 16, co-authored 19 publications receiving 3046 citations.

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Ischemic Preconditioning Induces Selective Translocation of Protein Kinase C Isoforms ε and η in the Heart of Conscious Rabbits Without Subcellular Redistribution of Total Protein Kinase C Activity

TL;DR: Quantitative immunoblotting demonstrated that as a subgroup, conventional PKCs are more abundant than novel PKCs (nPKCs) and that PKC alpha is the predominant isoform among the cPKCs (alpha, beta1, beta2, and gamma), representing 51% of this sub group, and PKC epsilon is the most abundant among the nPKCs
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The nitric oxide hypothesis of late preconditioning.

TL;DR: The NO hypothesis of late PC puts forth a comprehensive paradigm that can explain both the initiation and the mediation of this complex phenomenon, and has potential clinical reverberations, since NO donors are widely used clinically and could be used to protect the ischemic myocardium in patients.
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Isoform-Selective Activation of Protein Kinase C by Nitric Oxide in the Heart of Conscious Rabbits A Signaling Mechanism for Both Nitric Oxide–Induced and Ischemia-Induced Preconditioning

TL;DR: The results provide direct evidence that NO donors induce late PC by activating PKC and that among the 10 isozymes of PKC expressed in the rabbit heart, the epsilon isotype is specifically involved in the development of this form of pharmacological PC.
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Functional Proteomic Analysis of Protein Kinase C ε Signaling Complexes in the Normal Heart and During Cardioprotection

TL;DR: Using two-dimensional electrophoresis, mass spectrometry, immunoblotting, and affinity pull-down assays, it is found that myocardial protein kinase C &egr; (PKC&egr) is physically associated with at least 36 known proteins that are organized into structural proteins, signaling molecules, and stress-responsive proteins.