Donald K. Blumenthal

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Title:

Office: 102A Skaggs Hall
Email: Don.Blumenthal@pharm.utah.edu
Phone: (801) 585-3094
Fax: (801) 585-5111

Education:

  • B.A., 1975, University of California, San Diego
  • Ph.D., 1980, University of California, San Diego, Physiology and Pharmacology

Research Interests

My laboratory is broadly interested in the enzymes known as protein kinases and their roles in cell function and disease. Protein kinases catalyze the phosphorylation of proteins on serine, threonine, and tyrosine residues, which is the most common mechanism for the reversible covalent modification of protein structure and function. Protein kinases are the largest enzyme superfamily in eukaryotes, with more than 500 genes in the human genome. Many protein kinases are directly or indirectly involved in a variety of disease processes including cancer, diabetes, and heart disease, and there are now many drugs that target protein kinases and provide therapies for these diseases.

The protein kinases studied by my laboratory include the cAMP-dependent protein kinase (also known as protein kinase A or PKA), cGMP-dependent protein kinase (PKG), myosin light chain kinase (MLCK), phosphorylase kinase, and the platelet-derived growth factor (PDGF) receptor tyrosine kinase. These protein kinases have very different subunit structures and are regulated in very different ways, even though their catalytic domains are homologous. Our research ranges from biochemical and biophysical studies of protein kinase structure and function, to studies of protein kinase activity in different disease states.

Much of our current basic research efforts are directed towards biophysical studies of protein kinases using fluorescence, circular dichroism (CD), small-angle x-ray (SAXS) and neutron scattering (SANS), and molecular dynamics (MD). We are using these methods to better understand the large-scale dynamic properties of protein kinases and their role in protein kinase function.

We have also recently begun to study a different enzyme, human acetylcholinesterase, the enzyme that hydrolyzes the neurotransmitter acetylcholine. This enzyme is the target of nerve gas agents and several drugs that have therapeutic application in treating glaucoma and Alzheimer's disease. We are interested in developing better antidotes to inhibitors of this enzyme by studying the conformational dynamics of the protein using techniques such as SAXS, MD simulations, and neutron and X-ray diffraction.

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Figure: SAXS/SANS-based Models of PKA RIIbeta Holoenzyme (Blumenthal et al., J Biol Chem 2014)

 

Selected Publications

Web Publications:

  • "Goodman & Gilman Online (GGOL)" L.L. Brunton, D.K. Blumenthal, N. Murri, R. Hilal-Dandan, B.C. Knollmann (eds.) On-line version of the 12th edition of Goodman & Gilman's The Pharmacological Basis of Therapeutics (www.accessmedicine.com, www.accesspharmacy.com, and others)

Full PubMed bibliography

Book Chapters:

  • Goodman & Gilman's The Pharmacological Basis of Therapeutics Blumenthal DK. 13th ed. Brunton LL, R. Hilal-Dandan, and Knollmann BC, editors. United States: McGraw-Hill Medical; 2017. Chapter 3, Pharmacodynamics: Molecular Mechanisms of Drug Action (in press)
  • Goodman & Gilman's The Pharmacological Basis of Therapeutics Gurgel, H. and Blumenthal DK. 13th ed. Brunton LL, R. Hilal-Dandan, and Knollmann BC, editors. United States: McGraw-Hill Medical; 2017. Chapter 33, Drug Therapy for Dyslipidemias (in press)
  • Goodman & Gilman's The Pharmacological Basis of Therapeutics Blumenthal DK, Garrison JC. 12th ed. Brunton LL, Chabner BA, Knollmann BC, editors. United States: McGraw-Hill Medical; 2011. Chapter 3, Pharmacodynamics: Molecular Mechanisms of Drug Action; p.41-72.

Books Edited:

  • Workbook and Casebook for Goodman & Gilman's The Pharmacological Basis of Therapeutics (Editors: D.A. Rollins, D.K. Blumenthal; 2016)
  • Goodman & Gilman's Manual of Pharmacology & Therapeutics (Editors: L.L. Brunton, K.L. Parker, D.K. Blumenthal, I.L.O. Buxton; 2008)

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