个人简介

1987 B.A. Goucher College 1993 Ph.D. University of Virginia 1992-1995 Cornell University, NIH Postdoctoral Fellow 1995-1996 Cornell University, Postdoctoral Fellow 1996-1997 Cornell University, Research Associate Fall 2007 Honorary Senior Research Fellow Fall 2007 Leeds Institute of Genetics, Health, and Therapeutics (LIGHT)

研究领域

Biochemistry: Protein Structure-Function

Our research is focused on enzymes involved in blood coagulation and related processes. Members of this critical protein cascade have far reaching effects on wound healing, heart disease, stroke, and cancer. Further knowledge is still needed on the activation and the substrate/ligand binding properties of individual enzymes. In our laboratory, emphasis has been placed on examining the transglutaminase Factor XIII (FXIII) and the serine protease thrombin. Activated FXIII catalyzes the formation of covalent cross-links within the fibrin blood clot network. Thrombin is involved in converting fibrinogen into fibrin and in activating a variety of enzymes including FXIII and the protease activated receptors found in platelets. In our research studies, we employ a combination of kinetic measurements, solution NMR studies, and mass spectrometry approaches. Greater understanding of the structural and biological features of FXIII and thrombin may lead to novel medical strategies to control the actions of these vital proteins and the resultant clot architecture.

近期论文

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Ligand Binding to Anion Binding Exosites Regulates Conformational Properties of Thrombin Malovichko, M.V., Sabo, T.M., Maurer, M.C. J. Biol. Chem 2013, 288, 8667-78. Liberating R169 promotes anticoagulant protein C. Maurer, M.C. Blood 2012, 120, 501-2. Design of Factor XIII V34X activation peptides to control ability to interact with thrombin mutants. Jadhav, M.A., Lucas, R.C., Goldsberry, W.N., Maurer, M.C. BBA: Proteins and Proteomics, 2011, 1814, 1955-63. Role of calcium in the conformational dynamics of factor XIII activation examined by hydrogen-deuterium exchange coupled with MALDI-TOF MS. Woofter, R.T., Maurer, M.C., Arch. Biochem. Biophys.2011, 512, 87-95. Switching cation-binding loops paves the way for redesigning allosteric activation. Maurer, M.C. Proc. Natl. Acad. Sci. USA2011, 108, 5145-6. Effects of introducing fibrinogen Aalpha character into the factor XIII activation peptide segment. Jadhav, M.A., Isetti, G., Trumbo, T.A., Maurer, M.C. Biochemistry 2010, 49, 2918-24. A non-reactive glutamine residue of alpha-antiplasmin promotes interactions with the factor XIIIa active site region. Cleary, D.B., Doiphode, P.G., Sabo, T. M., Maurer, M. C. J. Thromb. Haemost.2009, 7, 1947-9. Biophysical Investigation of GpIbα Binding to Thrombin Anion Binding Exosite II Sabo, T. M., Maurer, M. C. Biochemistry 2009, 48, 7110–7122 Perturbations in Factor XIII Resulting From Activation and Inhibition Conditions Examined by Solution Based Methods and Detected by MALDI-TOF MS Sabo, T. M., Brasher, P. B., Maurer, M. C. Biochemistry 2007, 46, 10089-10101 Employing Mutants to Study Thrombin Residues Responsible for Factor XIII Activation Peptide Recognition: A Kinetic Study Isetti, G., Maurer, M. C. Biochemistry 2007, 46, 2444-2452 Conformational Analysis of y' peptide (410-427) Interactions with Thrombin Anion Binding Exosite II Sabo, T. M., Farrell, D. H., Maurer, M. C. Biochemistry 2006, 45, 7434-45 Characterizing the Specificity of Activated Factor XIII for Glutamine-Containing Substrate Peptides Cleary, D. B., Maurer, M. C. Biochim Biophys Acta2006, 1764, 1207-17 Probing Interactions Between the Coagulants Thrombin, Factor XIII, and Fibrin(ogen) Maurer, M. C., Trumbo, T. A., Isetti, G., Turner, B. T. Jr. Archives of Biochemistry and Biophysics 2006,445, 36-45