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University of Vermont |
Wolfgang Dostmann |
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Wolfgang Dostmann, Ph.D |
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Academic History: |
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| INSTITUTION AND LOCATION | DEGREE | YEAR | FIELD OF STUDY | |
| University of Bremen, Germany | Dipl.Chem. (M.S.) | 1983 | Chemistry | |
| University of Bremen, Germany | Dr.rer.nat. (Ph.D.) | 1987 | Bio-Organic Chemistry | |
| University of California at San Diego | Post-Doc | 1987-1991 | Biochemistry & Biophysics | |
| University of Technology Munich, Germany | Dr.med.habil (M.D.) | 1996 | Pharmacology & Toxicology | |
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Full Curriculum Vitae |
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BackgroundMy research interests focus on the topic of ‘second messenger signaling’ since graduate school in 1982 in Bremen, Germany. First as a chemist, I was involved in the synthesis, rational design, mapping studies, and theoretical aspects of cyclic nucleotides. During graduate school, I also conducted research at Sandoz, Inc (Novartis), New Jersey.As a post-doc at the University of California at San Diego, I concentrated on a wide variety of techniques in molecular biology, protein-biochemistry, and biophysics/crystallography to study the major cyclic nucleotide receptor proteins, namely the cAMP-dependent protein kinase (PKA). After establishing my own laboratory in Munich, Germany, I have expanded my studies to the cGMP-dependent protein kinase (PKG) and its role in disease. At the Technical University of Munich, the pharmacology of cGMP and PKG has become an increasing part of my research interests. Since I have joined the faculty of the Department of Pharmacology at the University of Vermont, my research has continued to develop methods and tools that allow us to study the cGMP-PKG pathway in vitro and in vivo in ever-increasing detail. My research has also allowed me to collaborate with the Pharmaceutical Industry in the development of novel drug targets involving cGMP signaling. Although my research interests are highly focused, my research projects have been and will continue to be stimulated and integrated through the use of a large variety of methods and techniques ranging from organic chemistry, biochemistry, molecular biology, cell biology, biophysics, physiology and pharmacology. |
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Selected publications: |
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Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine cyclic-3',5' phosphorothioates
Dostmann WRG, Taylor SS, Genieser HG, Jastorff B, Døskeland S and Øgreid D |
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Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains
Su Y, Dostmann WRG, Herberg FW, Durick K, Xuong NH, Ten Eyck L, Taylor SS and Varughese KI |
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Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase
Herberg FW, Taylor SS and Dostmann WRG |
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Highly specific, membrane permeant peptide blockers of cGMP-dependent protein kinase Ia inhibit NO-induced cerebral dilation
Dostmann WRG, Nickl CK, Taylor MS, Brayden JE, Frank R and Tegge WJ |
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Spatiotemporal dynamics of guanosine 3',5'-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator
Honda A, Adams SR Sawyer CL, Lev-Ram V, Tsien RY and Dostmann WRG |
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A new class of cGMP-dependent protein kinase peptide inhibitors and their role in elucidating vasomotor mechanisms
Dostmann WRG, Nickl, CK, Taylor MS, Brayden JE, Frank R and Tegge WJ |
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Unique inhibitory properties of the cell-permeable cGMP-dependent protein kinase inhibitor DT-2 reveal a novel mechanism of vasoregulation
Taylor, MS, Okwuchukwuasanya, C, Nickl, CK, Brayden, JE and Dostmann, WRG |
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Cygnets: Rapid cellular internalization of fluorescent cGMP-indicators
Honda A, Moosmeier M, and Dostmann WR |
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Culture conditions influence uptake and intracellular localization of the membrane permeable cGMP-dependent protein kinase peptide inhibitor DT-2
Foley KF, De Frutos S, Laskovski KE, Tegge W and Dostmann WR |
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Inhibition of cGMP-dependent protein kinase-I attenuates contractile protein expression and contractile morphology in cultured rat aortic smooth muscle cells
Dey N, Foley KF, Lincoln TM and Dostmann WR |
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Compartmentalized phosphodiesterase-2 activity blunts beta-adrenergic cardiac inotropy via an NO/cGMP-dependent pathway
Mongillo M, Tocchetti CG, Terrin A, Lissandron V, Cheung YF, Dostmann WR, Pozzan T,
Kass DA, Paolocci N, Houslay MD, Zaccolo M |
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Dostmann WR. Nitric oxide-evoked transient kinetics of cyclic GMP in vascular smooth muscle cells
Cawley SM, Sawyer CL, Brunelle KF, van der Vliet A |
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The hinge region operates as a stability switch in cGMP dependent protein kinase I
Scholten A, Fuss H, Heck AJ, Dostmann WR |
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Differential patterning of cGMP in vascular smooth muscle cells revealed by single GFP-linked biosensors
Nausch L, Ledoux J, Bonev A, Nelson MT, Dostmann WR |
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(D)-amino acid analogues of DT-2 as highly selective and superior inhibitors of cGMP-dependent protein kinase I
Nickl CK, Raidas SK, Zhao H, Sausbier M, Ruth P, Tegge W, Brayden JE, and Dostmann WR |
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Adenosine analogue-oligo-arginine conjugates (ARCs) serve as high-affinity inhibitors and fluorescence probes of type I cGMP-dependent protein kinase (PKGIalpha)
Lavogina D, Nickl CK, Enkvist E, Raidaru G, Lust M, Vaasa A, Uri A, Dostmann WR |
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Exquisite sensitivity to subsecond, picomolar nitric oxide transients conferred on cells byguanylyl cyclase-coupled receptors
Batchelor AM, Bartus K, Reynell C, Constantinou S, Halvey EJ, Held KF, Dostmann WR, Vernon J,
Garthwaite J |
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Crystal structure of cGMP-dependent protein kinase reveals novel site of interchain communication.
Osborne BW, Wu J, McFarland CJ, Nickl CK, Sankaran B, Casteel DE, Woods VL Jr, Kornev AP, Taylor SS, Dostmann WR. |
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