Wintrode:Publications: Difference between revisions
(New page: == Research Papers == Snyder, G.A., Deredge, D.*, Waldhuber, A., Fresquez, T., Wilkins, D.Z., Smith, P., Durr, S., Cirl, C., Jian, J., Jennings, W., Luchetti, T., Snyder, N., Sundberg, ...) |
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Revision as of 07:33, 12 December 2013
Research Papers
Snyder, G.A., Deredge, D.*, Waldhuber, A., Fresquez, T., Wilkins, D.Z., Smith, P., Durr, S., Cirl, C., Jian, J., Jennings, W., Luchetti, T., Snyder, N., Sundberg, E.J., Wintrode, P.L., Miethke, T. and Xiao, T.S. (2013) Crystal structures of the TIR domains from the Brucella protein TcpB and the host adaptor protein TIRAP reveal mechanisms of molecular mimicry. J. Biol. Chem., in press.
Cheng, J., Karri, S*., Roberts, M.F., Wintrode, P.L. and Gershenson, A. (2013) Do mutations predicted to change the dynamics of a phospholipase C alter activity and membrane binding? Biophys. J. 104 185-195. DOI:10.1016/j.bpj.2012.11.015
Stocks, B.B., Sarkar, A.*, Wintrode, P.L. and Konermann, L. (2012) Early hydrophobic collapse of α1-antitrypsin facilitates formation of a metastable state: Insights from oxidative labeling and mass spectrometry. J. Mol. Biol. 423 789-799. DOI: 10.1016/j.jmb.2012.08.019.
Cheng, I., Nikita, N., Fishovitz, J., Frase, H., Wintrode, P.L. and Lee, I. (2012) Identification of a region in the N-terminus of escherichia coli lon that affects ATPase, substrate translocation and proteolytic activity. J. Mol. Biol. 418 208-225. DOI: 10.1016/j.jmb.2012.02.039
Tsutsui, Y.*, dela Cruz, R.G. and Wintrode, P.L. (2012) Folding mechanism of the metastable serpin a1-antitrypsin. Proc. Natl. Acad. Sci. USA, 109 4467-4472. DOI: 10.1073/pnas.1109125109
Sarkar, A.*, Zhou, C.*, Meklemburg, R.* and Wintrode, P.L. (2011) Local conformational flexibility provides a basis for facile polymer formation in human neuroserpin. Biophys. J. 101 1758-1765. DOI: 10.1016/j.bpj.2011.08.037
Sarkar, A.* and Wintrode, P.L. (2011) Effects of glycosylation on the stability and flexibility of a metastable protein: the human serpin α1-antitrypsin. Int. J. Mass Spectrom. 302, 69-75. DOI: 10.1016/j.ijms.2010.08.003
Seckler, J.M.*, Barkley, M.D. and Wintrode, P.L. (2011) Allosteric suppression of HIV-1 reverse transcriptase structural dynamics upon inhibitor binding. Biophys. J. 100 144-153. DOI: 10.1016/j.bpj.2010.11.004
Braz, V. Barkley, M.D., Jockusch, R. and Wintrode, P.L. (2010) The Efavirenz Binding Site in HIV-1 Reverse Transcriptase Monomers. Biochemistry 49 10565-10573. DOI: 10.1021/bi101480z
Sengupta, T.*, Tsutsui, Y.* and Wintrode, P.L. (2009) Local and global effects of a cavity filling mutation in a metastable serpin. Biochemistry 48 8233-8240. DOI: 10.1021/bi900342d
Seckler, J.M.*, Howard, K.J., Barkley, M.D and Wintrode, P.L. (2009) Solution structural dynamics of HIV-1 reverse transcriptase heterodimer. Biochemistry 48 7646-7655. DOI: 10.1021/bi900790x
Goc, A., Angel, T., Jastrzebska, B. Wang, B. Wintrode, P.L. and Palczewski, K. (2008) Different properties of the native and reconstituted heterotrimeric G protein transducin. Biochemistry 47 12409-12419. DOI: 10.1021/bi8015444
Tsutsui, Y.*, Kuri, B.*, Sengupta, T.* and Wintrode, P.L. (2008) The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem. 283 30804-30811. DOI: 10.1074/jbc.M804048200
Zheng, X., Wintrode, P.L. and Chance, M.R. (2008) Complementary structural mass spectrometry techniques reveal local dynamics in functionally important regions of a metastable serpin. Structure 16 1-14. DOI: 10.1016/j.str.2007.10.019
Tsutsui, Y.* and Wintrode, P.L. (2007) Cooperative unfolding of a metastable serpin to a molten globule suggests a link between functional and folding energy landscapes. J. Mol. Biol. 371 245-255. DOI: 10.1016/j.jmb.2007.05.039
Lu, X., Wintrode, P.L. and Surewicz, W.K. (2007) Beta-Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc. Natl. Acad. Sci. USA 104 1510-1515. DOI: 10.1073/pnas.0608447104
Tsutsui, Y.*, Liu, L., Gershenson, A. and Wintrode, P.L. (2006) The conformational dynamics of a metastable serpin studied by hydrogen exchange and mass spectrometry. Biochemistry 45 6561-6569. DOI: 10.1021/bi060431f
Review Articles
Tsutsui, Y.*, Sarkar, A.* & Wintrode, P.L. (2011) Probing serpin conformational change using mass spectrometry and related methods. Methods in Enzymology, 501 325-350.
Tsutsui, Y.* & Wintrode, P.L.(2007) Hydrogen/deuterium exchange-mass spectrometry: a powerful tool for probing protein structure, dynamics and interactions. Curr. Med. Chem. 22 2344-2358.