Paul R. Rosevear , PhD

My area of expertise is Structural Biology with emphasis in Biological NMR Spectroscopy. Our general area of interest involves disorder to order conformational transitions in proteins induced by post-translational modifications. We are currently studying structure/function relationships in cardiac thin filament proteins with particular emphasis on the role of phosphorylation in health and disease. The rational and efficient design of effective pharmaceuticals to treat heart failure and genetic disorders, such as familial hypertrophic cardiac myopathy, will require intimate knowledge of the structural mechanisms responsible for regulation of heart muscle contraction. Phosphorylation and mutation of sarcomere proteins are known to play crucial roles in modulating cardiac contraction in both normal and disease states.  Disorder to order transitions induced by phosphorylation of cardiac thin filament proteins alter both the rate and Ca²⁺-sensitivity of contraction at the muscle fiber level. Our general hypothesis is that understanding charge–induced conformational events in cardiac troponin and in cardiac myosin binding protein C, either by mutation or phosphorylation, will provide molecular insights into the pathologies of cardiovascular disease states such as hypertrophic cardiomyopathy, dilated cardiomyopathy, and end-stage heart failure. A combination of high-resolution NMR, small-angle scattering, molecular dynamics, computational modeling, and mutagenesis are being applied to study the effects of phosphorylation on cardiac troponin and on cardiac myosin binding protein C. Understanding conformational transitions induced by phosphorylation or mutation of cardiac thin filament proteins will aid in the design of pharmacological agents capable of modulating contraction through alterations in sarcomere protein-protein interactions.

Bachelor's Degree: Old Dominion University Norfolk, VA, 1975 (Chemistry)

Master's Degree: Old Dominion University Norflok, VA, 1976 (Chemistry)

Doctoral Degree: Michigan State University East Lansing, MI, 1980 (Biochemistry)

Postdoctoral fellowship: Fox Chase Cancer Center Philadelphia, PA, 1982 (Mechanistic enzymology and biological NMR)

Research Fellowship: The Johns Hopkins School of Medicine Baltimore, MD, 1984 (Biological NMR, Protein structure/function)

Research Associate : Brandeis University Waltham, MA, 1985 (Biophysics, NMR Spectroscopy)

My major interest is the use of nuclear magnetic resonance (NMR) to solve biological and physiological problems.  Elucidating the relationships between protein structure and function has been a major research interest over the last 20 years.  Currently we are interested in the role that natively disordered regions play in protein recognition and binding.  In particular, we are interested in disorder-to-order transitions that occur with phosphoryltions and other post-translatinal modifications. 

We are currently studying structure/function relationships in cardiac thin filament proteins with particular emphasis on the role of phosphorylation in health and disease. The rational and efficient design of effective pharmaceuticals to treat heart failure and genetic disorders, such as familial hypertrophic cardiac myopathy, will require intimate knowledgeof the structural mechanisms responsible for regulation of heart muscle contraction. Phosphorylation and mutation of sarcomere proteins are known to play crucial roles in modulating cardiac contraction in both normal and disease states.  Disorder to order transitions induced by phosphorylation of cardiac thin filament proteins alter both the rate and Ca2+-sensitivity of contraction at the muscle fiber level. Our general hypothesis is that understanding charge–induced conformational events in cardiac troponin and in cardiac myosin binding protein C, either by mutation or phosphorylation, will provide molecular insights into the pathologies of cardiovascular disease states such as hypertrophic cardiomyopathy, dilated cardiomyopathy, and end-stage heart failure. A combination of high-resolution NMR, small-angle scattering, molecular dynamic, computational modeling, and mutagenesis are being applied to study the effects of phosphorylation on cardiac troponin and on cardiac myosin binding protein C. Understanding conformational transitions induced by phosphorylation or mutation of cardiac thin filament proteins will aid in the design of pharmacological agents capable of modulating contraction through alterations in sarcomere protein-protein interactions.

A recent research interest is the use of NMR for metabolic profiling.  This new area of research  is termed metabolomics. Metabolomics follows the recent advances in genomics and proteomics. It involves the measurement of compounds or metabolites in biological fluids providing a metabolic profile. Metabolic profiles enable the detection of various disease processes, environmental effects, and drug toxicity. One of our projects involves understanding metabolic changes that ocur following gastric bypass surgery. The overall goal of this project is to characterize metabolic fingerprints caused by alteration in islet function following gastric bypass surgery. Identifying and quantitating the specific metabolites to create a biomarker profile will be useful for drug discovery and patient prognosis.

1985 -1991 Assistant Professor, Biochemistry and Molecular Biology, University of Texas, Health Science Center Hoouston, Houston, TX

1991 -1995 Associate Professor, Biochemistry and Molecular Biology, University of Texas, Health Science Center Houston, Houston, TX

1996 -2008 Associate Professor, Molecular Genetics, Biochemistry, and Microbiology, University Cincinnati, College of Medicine, Cincinnati, OH

2008 -To Present Professor, Molecular Genetics, Biochemistry, and Microbiology, University Cincinnati, College of Medicine, Cincinnati, OH

Grant: #5-R01-GM-62153-04-A0-S0-E0 Investigators:Rosevear, Paul 02-01-2001 -01-31-2005 National Institute of General Medical Sciences Protein Folding Using Paramagnetic Derived Restraints Role:PI $1,032,168.00 Closed Level:Federal

Grant: #DAAD19-02-1-0227 Investigators:Beck, Thomas; Boerio, F James; Cuppoletti, John; Lin, Jerry Y.S.; Rosevear, Paul 06-10-2002 -06-09-2007 Department of the Army Flexible Membranes for Active Transport of HCl Role:Collaborator $4,999,999.39 Closed Level:Federal

Grant: #5-R01-AR-44324-04-A0-S0-E0 Investigators:Rosevear, Paul 12-01-1996 -11-30-2001 National Institute of Arthritis, Musculoskeletal and Skin Disease NMR Studies of Troponin Complex Role:PI $988,867.00 Closed Level:Federal

Grant: #R01 HL083334 Investigators:Finley, Natosha; Howarth, Jack; Rance, Mark; Rosevear, Paul 06-15-2007 -04-30-2011 National Heart, Lung and Blood Institute Structural Mechanisms Modulating Contraction in Normal and Diseased Heart Role:PI $1,532,112.00 Closed Level:Federal

Grant: #1 S10 RR027755-01 Investigators:Herr, Andrew; Rance, Mark; Rosevear, Paul 12-10-2009 -12-09-2010 National Center for Research Resources 800 MHz NMR Console Replacement Role:Collaborator $358,323.00 Closed Level:Federal

Grant: #S10OD011944 Investigators:Adler, Caleb; Clark, Joseph; Ho, Shuk Mei; Howarth, Jack; Komoroski, Richard; Lu, Aigang; Pyne-Geithman, Gail Jean; Rosevear, Paul; Strakowski, Stephen 04-02-2012 -03-31-2014 Office of the Director, National Institutes of Health Bruker Avance III Wide-Bore (89-mm, 9.4T), Vertical-Bore 400-Mhz NMR Spectrometer Role:Collaborator $595,000.00 Active Level:Federal

Peer Reviewed Publications

Millard, Ronald W; Rosevear, Paul R (2012. ) Metabolomics: seeking a unique biomarker signature for coronary artery syndromes.Journal of the American College of Cardiology, , 59 (18 ) ,1642-4 More Information

Howarth, Jack W; Ramisetti, Srinivas; Nolan, Kristof; Sadayappan, Sakthivel; Rosevear, Paul R (2012. ) Structural insight into unique cardiac myosin-binding protein-C motif: a partially folded domain.The Journal of biological chemistry, , 287 (11 ) ,8254-62 More Information

Sadayappan, Sakthivel; Finley, Natosha; Howarth, Jack W; Osinska, Hanna; Klevitsky, Raisa; Lorenz, John N; Rosevear, Paul R; Robbins, Jeffrey (2008. ) Role of the acidic N' region of cardiac troponin I in regulating myocardial function.FASEB journal : official publication of the Federation of American Societies for Experimental Biology, , 22 (4 ) ,1246-57 More Information

Howarth, Jack W; Meller, Jarek; Solaro, R John; Trewhella, Jill; Rosevear, Paul R (2007. ) Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin.Journal of molecular biology, , 373 (3 ) ,706-22 More Information

Sakthivel, Sadayappan; Finley, Natosha L; Rosevear, Paul R; Lorenz, John N; Gulick, James; Kim, Scott; VanBuren, Peter; Martin, Lisa A; Robbins, Jeffrey (2005. ) In vivo and in vitro analysis of cardiac troponin I phosphorylation.The Journal of biological chemistry, , 280 (1 ) ,703-14 More Information

Finley, Natosha L; Rosevear, Paul R (2004. ) Introduction of negative charge mimicking protein kinase C phosphorylation of cardiac troponin I. Effects on cardiac troponin C.The Journal of biological chemistry, , 279 (52 ) ,54833-40 More Information

Finley, Natosha L; Howarth, Jack W; Rosevear, Paul R (2004. ) Structure of the Mg2+-loaded C-lobe of cardiac troponin C bound to the N-domain of cardiac troponin I: comparison with the Ca2+-loaded structure.Biochemistry, , 43 (36 ) ,11371-9 More Information

Sorsa, Tia; Pollesello, Piero; Rosevear, Paul R; Drakenberg, Torbjörn; Kilpeläinen, Ilkka (2004. ) Stereoselective binding of levosimendan to cardiac troponin C causes Ca2+-sensitization. European journal of pharmacology, , 486 (1 ) ,1-8

Rosevear, Paul R; Finley, Natosha (2003. ) Molecular mechanism of levosimendan action: an update. Journal of molecular and cellular cardiology, , 35 (9 ) ,1011-5

Heller, William T; Finley, Natosha L; Dong, Wen-Ji; Timmins, Peter; Cheung, Herbert C; Rosevear, Paul R; Trewhella, Jill (2003. ) Small-angle neutron scattering with contrast variation reveals spatial relationships between the three subunits in the ternary cardiac troponin complex and the effects of troponin I phosphorylation.Biochemistry, , 42 (25 ) ,7790-800 More Information

Heller, William T; Abusamhadneh, Ekram; Finley, Natosha; Rosevear, Paul R; Trewhella, Jill (2002. ) The solution structure of a cardiac troponin C-troponin I-troponin T complex shows a somewhat compact troponin C interacting with an extended troponin I-troponin T component. Biochemistry, , 41 (52 ) ,15654-63

Dvoretsky, Alex; Abusamhadneh, Ekram M; Howarth, Jack W; Rosevear, Paul R (2002. ) Solution structure of calcium-saturated cardiac troponin C bound to cardiac troponin I.The Journal of biological chemistry, , 277 (41 ) ,38565-70 More Information

Dvoretsky, Alex; Gaponenko, Vadim; Rosevear, Paul R (2002. ) Derivation of structural restraints using a thiol-reactive chelator. FEBS letters, , 528 (1-3 ) ,189-92

Abusamhadneh, E; Abbott, M B; Dvoretsky, A; Finley, N; Sasi, S; Rosevear, P R (2001. ) Interaction of bepridil with the cardiac troponin C/troponin I complex. FEBS letters, , 506 (1 ) ,51-4

Abbott, M B; Dong, W J; Dvoretsky, A; DaGue, B; Caprioli, R M; Cheung, H C; Rosevear, P R (2001. ) Modulation of cardiac troponin C-cardiac troponin I regulatory interactions by the amino-terminus of cardiac troponin I. Biochemistry, , 40 (20 ) ,5992-6001

Sorsa, T; Heikkinen, S; Abbott, M B; Abusamhadneh, E; Laakso, T; Tilgmann, C; Serimaa, R; Annila, A; Rosevear, P R; Drakenberg, T; Pollesello, P; Kilpelainen, I (2001. ) Binding of levosimendan, a calcium sensitizer, to cardiac troponin C.The Journal of biological chemistry, , 276 (12 ) ,9337-43 More Information

Gaponenko, V; Dvoretsky, A; Walsby, C; Hoffman, B M; Rosevear, P R (2000. ) Calculation of z-coordinates and orientational restraints using a metal binding tag. Biochemistry, , 39 (49 ) ,15217-24

Finley, N; Dvoretsky, A; Rosevear, P R (2000. ) Magnesium-calcium exchange in cardiac troponin C bound to cardiac troponin I.Journal of molecular and cellular cardiology, , 32 (8 ) ,1439-46 More Information

Abbott, M B; Gaponenko, V; Abusamhadneh, E; Finley, N; Li, G; Dvoretsky, A; Rance, M; Solaro, R J; Rosevear, P R (2000. ) Regulatory domain conformational exchange and linker region flexibility in cardiac troponin C bound to cardiac troponin I.The Journal of biological chemistry, , 275 (27 ) ,20610-7 More Information

Permi, P; Rosevear, P R; Annila, A (2000. ) A set of HNCO-based experiments for measurement of residual dipolar couplings in 15N, 13C, (2H)-labeled proteins. Journal of biomolecular NMR, , 17 (1 ) ,43-54

Abbott, M B; Dvoretsky, A; Gaponenko, V; Rosevear, P R (2000. ) Cardiac troponin I inhibitory peptide: location of interaction sites on troponin C. FEBS letters, , 469 (2-3 ) ,168-72

Gaponenko, V; Howarth, J W; Columbus, L; Gasmi-Seabrook, G; Yuan, J; Hubbell, W L; Rosevear, P R (2000. ) Protein global fold determination using site-directed spin and isotope labeling.Protein science : a publication of the Protein Society, , 9 (2 ) ,302-9 More Information

Gasmi-Seabrook, G M; Howarth, J W; Finley, N; Abusamhadneh, E; Gaponenko, V; Brito, R M; Solaro, R J; Rosevear, P R (1999. ) Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I.Biochemistry, , 38 (26 ) ,8313-22 More Information

Finley, N; Abbott, M B; Abusamhadneh, E; Gaponenko, V; Dong, W; Gasmi-Seabrook, G; Howarth, J W; Rance, M; Solaro, R J; Cheung, H C; Rosevear, P R (1999. ) NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation. FEBS letters, , 453 (1-2 ) ,107-12

Gaponenko, V; Abusamhadneh, E; Abbott, M B; Finley, N; Gasmi-Seabrook, G; Solaro, R J; Rance, M; Rosevear, P R (1999. ) Effects of troponin I phosphorylation on conformational exchange in the regulatory domain of cardiac troponin C. The Journal of biological chemistry, , 274 (24 ) ,16681-4

Zhou, L; Rosevear, P R (1995. ) Mutation of the carboxy terminal zinc finger of E. coli isoleucyl-tRNA synthetase alters zinc binding and aminoacylation activity.Biochemical and biophysical research communications, , 216 (2 ) ,648-54 More Information

Kleerekoper, Q; Howarth, J W; Guo, X; Solaro, R J; Rosevear, P R (1995. ) Cardiac troponin I induced conformational changes in cardiac troponin C as monitored by NMR using site-directed spin and isotope labeling. Biochemistry, , 34 (41 ) ,13343-52

Howarth, J W; Krudy, G A; Lin, X; Putkey, J A; Rosevear, P R (1995. ) An NMR and spin label study of the effects of binding calcium and troponin I inhibitory peptide to cardiac troponin C.Protein science : a publication of the Protein Society, , 4 (4 ) ,671-80 More Information

Lin, X; Krudy, G A; Howarth, J; Brito, R M; Rosevear, P R; Putkey, J A (1994. ) Assignment and calcium dependence of methionyl epsilon C and epsilon H resonances in cardiac troponin C. Biochemistry, , 33 (48 ) ,14434-42

Krudy, G A; Kleerekoper, Q; Guo, X; Howarth, J W; Solaro, R J; Rosevear, P R (1994. ) NMR studies delineating spatial relationships within the cardiac troponin I-troponin C complex. The Journal of biological chemistry, , 269 (38 ) ,23731-5

Jones, C M; Reyes, C J; Cook, R G; Krudy, G A; Rosevear, P R (1994. ) Synthetic macrophage activating peptides derived from the N-terminus of human MCF.Biochemical and biophysical research communications, , 199 (1 ) ,20-5 More Information

Xu, B; Trawick, B; Krudy, G A; Phillips, R M; Zhou, L; Rosevear, P R (1994. ) Probing the metal binding sites of Escherichia coli isoleucyl-tRNA synthetase. Biochemistry, , 33 (2 ) ,398-402

Brito, R M; Krudy, G A; Negele, J C; Putkey, J A; Rosevear, P R (1993. ) Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C. The Journal of biological chemistry, , 268 (28 ) ,20966-73

Xu, B; Krudy, G A; Rosevear, P R (1993. ) Identification of the metal ligands and characterization of a putative zinc finger in methionyl-tRNA synthetase. The Journal of biological chemistry, , 268 (22 ) ,16259-64

Krudy, G A; Brito, R M; Putkey, J A; Rosevear, P R (1992. ) Conformational changes in the metal-binding sites of cardiac troponin C induced by calcium binding. Biochemistry, , 31 (6 ) ,1595-602

Brito, R M; Putkey, J A; Strynadka, N C; James, M N; Rosevear, P R (1991. ) Comparative NMR studies on cardiac troponin C and a mutant incapable of binding calcium at site II. Biochemistry, , 30 (42 ) ,10236-45

Williams, J S; Rosevear, P R (1991. ) A novel alpha-proton exchange reaction catalyzed by Escherichia coli methionyl-tRNA synthetase. Biochemistry, , 30 (26 ) ,6412-6

Williams, J S; Rosevear, P R (1991. ) Nuclear overhauser effect studies of the conformations of Mg(alpha, beta-methylene)ATP bound to E. coli isoleucyl-tRNA synthetase. Biochemical and biophysical research communications, , 176 (2 ) ,682-9

Brito, R M; Rudolph, F B; Rosevear, P R (1991. ) Conformation of NADP+ bound to a type II dihydrofolate reductase. Biochemistry, , 30 (6 ) ,1461-9

Williams, J S; Rosevear, P R (1991. ) Nuclear Overhauser effect studies on the conformations of Mg(alpha,beta-methylene)ATP bound to Escherichia coli methionyl-tRNA synthetase. The Journal of biological chemistry, , 266 (4 ) ,2089-98

Sweeney, H L; Brito, R M; Rosevear, P R; Putkey, J A (1990. ) The low-affinity Ca2(+)-binding sites in cardiac/slow skeletal muscle troponin C perform distinct functions: site I alone cannot trigger contraction. Proceedings of the National Academy of Sciences of the United States of America, , 87 (24 ) ,9538-42

Brito, R M; Reddick, R; Bennett, G N; Rudolph, F B; Rosevear, P R (1990. ) Characterization and stereochemistry of cofactor oxidation by a type II dihydrofolate reductase. Biochemistry, , 29 (42 ) ,9825-31

Flores-Carreón, A; Hixson, S H; Gómez, A; Shao, M C; Krudy, G; Rosevear, P R; Wold, F (1990. ) The processing of N-linked glycans in yeast. Mutually exclusive steps in the processing of a Man6 derivative by yeast membrane preparations. The Journal of biological chemistry, , 265 (2 ) ,754-9

Shao, M C; Krudy, G; Rosevear, P R; Wold, F (1989. ) Protein matrix effects on glycan processing by mannosidase II and sialyl transferase from rat liver. Biochemistry, , 28 (9 ) ,4077-83

Rosevear, P R; Mildvan, A S (1989. ) Ligand conformations and ligand-enzyme interactions as studied by the nuclear Overhauser effect. Methods in enzymology, , 177 ,333-58

Rosevear, P R (1988. ) Purification and NMR studies of [methyl-13C]methionine-labeled truncated methionyl-tRNA synthetase. Biochemistry, , 27 (20 ) ,7931-9

Rosevear, P R; Powers, V M; Dowhan, D; Mildvan, A S; Kenyon, G L (1987. ) Nuclear overhauser effect studies on the conformation of magnesium adenosine 5'-triphosphate bound to rabbit muscle creatine kinase. Biochemistry, , 26 (17 ) ,5338-44

Rosevear, P R; Fox, T L; Mildvan, A S (1987. ) Nuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase. Biochemistry, , 26 (12 ) ,3487-93

Mildvan, A S; Rosevear, P R; Fry, D C; Bramson, H N; Kaiser, E T (1985. ) NMR studies of the mechanism of action and regulation of protein kinase. Current topics in cellular regulation, , 27 ,133-44

Rosevear, P R; Sellin, S; Mannervik, B; Kuntz, I D; Mildvan, A S (1984. ) NMR and computer modeling studies of the conformations of glutathione derivatives at the active site of glyoxalase I. The Journal of biological chemistry, , 259 (18 ) ,11436-47

Mildvan, A S; Kaiser, E T; Rosevear, P R; Bramson, H N (1984. ) NMR studies of the mechanism of cyclic AMP-dependent protein kinase. Federation proceedings, , 43 (11 ) ,2634-9

Rosevear, P R; Fry, D C; Mildvan, A S; Doughty, M; O'Brian, C; Kaiser, E T (1984. ) NMR studies of the backbone protons and secondary structure of pentapeptide and heptapeptide substrates bound to bovine heart protein kinase. Biochemistry, , 23 (14 ) ,3161-73

Rosevear, P R; Bramson, H N; O'Brian, C; Kaiser, E T; Mildvan, A S (1983. ) Nuclear Overhauser effect studies of the conformations of tetraamminecobalt(III)-adenosine 5'-triphosphate free and bound to bovine heart protein kinase. Biochemistry, , 22 (14 ) ,3439-47

Rosevear, P R; Chari, R V; Kozarich, J W; Sellin, S; Mannervik, B; Mildvan, A S (1983. ) 13C NMR studies of the product complex of glyoxalase I. The Journal of biological chemistry, , 258 (11 ) ,6823-6

Roff, C F; Rosevear, P R; Wang, J L; Barker, R (1983. ) Identification of carbohydrate-binding proteins from mouse and human fibroblasts. The Biochemical journal, , 211 (3 ) ,625-9

Mildvan, A S; Rosevear, P R; Granot, J; O (1983. ) Use of NMR and EPR to study cAMP-dependent protein kinase. Methods in enzymology, , 99 ,93-119

Sellin, S; Rosevear, P R; Mannervik, B; Mildvan, A S (1982. ) Nuclear relaxation studies of the role of the essential metal in glyoxalase I. The Journal of biological chemistry, , 257 (17 ) ,10023-9

Rosevear, P R; Nunez, H A; Barker, R (1982. ) Synthesis and solution conformation of the type 2 blood group oligosaccharide alpha LFuc(1 leads to 2) beta DGal(1 leads to 4) beta DGlcNAc. Biochemistry, , 21 (6 ) ,1421-31

Rosevear, P R; Desmeules, P; Kenyon, G L; Mildvan, A S (1981. ) Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase. Biochemistry, , 20 (21 ) ,6155-64

Solaro, R John; Rosevear, Paul; Kobayashi, Tomoyoshi (2008. ) The unique functions of cardiac troponin I in the control of cardiac muscle contraction and relaxation.Biochemical and biophysical research communications, , 369 (1 ) ,82-7 More Information

Barker, R; Nunez, H A; Rosevear, P; Serianni, A S (1982. ) 13C NMR analysis of complex carbohydrates. Methods in enzymology, , 83 ,58-69

Rosevear, P; VanAken, T; Baxter, J; Ferguson-Miller, S (1980. ) Alkyl glycoside detergents: a simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase. Biochemistry, , 19 (17 ) ,4108-15

Michalek, A.J., Gulick, J., Robbins, J. Howarth, J.W., Rosevear, P.R. and Warshaw, D.M. (2013. ) Phosphorylation modulates mechanical stability of the cardiac myosin binding protein-C motif .Biophysical Journal-Biophysical Letters, , 104 (2 ) ,442

1974 -1975 American Institute of Chemists Student Award Status:Recipient Level:National Type:Recognition

1975 -1976 Sigma Xi Award for Devotion to the Promotion of Research in Science Status:Recipient Level:National Type:Recognition

1975 -1975 American Chemical Society Outstanding Senior Majoring in Chemistry Status:Recipient Level:Regional Type:Recognition

1981 -1982 American Cancer Society Postdoctoral Fellowship American Cancer Society Status:Recipient Level:National Type:Fellowship

1983 -1984 National Institutes of Health Postdoctoral Fellowship Status:Recipient Level:National Type:Fellowship

1984 -1985 National Institutes of Health Medical Training Grant Status:Recipient Level:National Type:Grant

2004 -2004 Twenty-second Annual John A. Boezi Memorial Alumnus Award Michigan State University Michigan State University Status:Recipient Level:University Type:Recognition

Journal of Biological Chemistry Editorial Board Member Type:Editorial Service Level:International 1990 -1995

Journal of Biological Chemistry Editorial Board Member Type:Editorial Service Level:International 1997 -2001

Journal of Biological Chemistry Editorial Board Member Type:Editorial Service Level:International 2005 -2010

International Journal of Molecular Sciences: Muscle Contraction Editor of Journal Type:Editorial Service Level:International 2009 -To Present

NIH (General Medicine B Study Section ) Committee Member Type:Grant Panel Level:National 2000 -2001

American Cancer Society (Scientific Advisory Committee ) Member Type:Grant Panel Level:National 2000 -2001

NIH (BBCB Study Section ) Committee Member Type:Grant Panel Level:National 2001 -2001

Florida Department of Health (Florida Biomedical Peer Review Committee ) Committee Member Type:Grant Panel Level:State 2001 -2003

DOE (Genomes to Life Workshop ) Committee Member Type:Grant Panel Level:National 2004 -2005

NIH (Fellowship Review ) Committee Member Type:Grant Panel Level:National 2012 -2012

NIH (COBRE Study Section ) Committee Member Type:Grant Panel Level:National 2005 -2005

NIH (Biological Chemistry Macromolecular Biophysics ) Committee Member Type:Grant Panel Level:National 2005 -2006

NIH (Biophysical and Biochemical Science Fellowship Study Section ) Committee Member Type:Grant Panel Level:National 2007 -2007

NMR, Protein Structure, Metabolomics, Cardiac Contractile Proteins, Heart Failure, Natively Disordered Proteins, Circular Dichroism, EPR

Academic - 2203 Medical Sciences Building
231 Albert Sabin Way
Cincinnati  Ohio, 45267-0524
Phone: (513) 558-3370
Fax: (513) 558-8474
paul.rosevear@uc.edu