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Wachter,Rebekka
2023-09-22
  • Wachter,Rebekka
  • Wachter,Rebekka - 副教授-亚利桑那州立大学-个人资料

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近期论文


Wachter, R. M., Salvucci, M. E., Carmo-Silva, A. E., Barta, C., Genkhov, T., Spreitzer, R. J. (2013), Activation of Interspecies-hybrid Rubisco Enzymes to Assess Different Models for the Rubisco – Rubisco Activase Interaction Photosynth. Res. (in press) DOI: 10.1007/s11120-013-9827-0.r
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Kennis, J. T. M., van Stokkum, I. H. M., Peterson, D. S., Pandit, A., Wachter, R. M. (2013), Ultrafast Proton Shuttling in Psammocora Cyan Fluorescent Protein. The Journal of Physical Chemistry B (in press) DOI: 10.1021/jp401114e.r
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Watkins, J. L., Kim, H., Markwardt, M. L., Chen, L., Fromme, R., Rizzo, M. A., Wachter, R. M. (2013), The 1.6 Å structure of a FRET-optimized Cerulean Fluorescent Protein. Acta Crystallogr. D69, 767-773.r
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Henderson, J. N., Hazra, S., Dunkle, A. M., Salvucci, M. E., Wachter, R. M. (2013) Biophysical Characterization of Higher Plant Rubisco Activase. Biophys. Biochim. Acta 1834, 87-97.r
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Chakraborty, M., Kuriata, A. M., Henderson, J. N., Salvucci, M. E., Wachter, R. M., Levitus*, M. (2012) Protein Oligomerization Monitored by Fluorescence Fluctuation Spectroscopy: Self-Assembly of Rubisco Activase. Biophys. J. 103, 949-958.r
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Henderson, J. N., Kuriata, A. M., Fromme, R., Salvucci, M. E., Wachter, R. M. (2011) Atomic Resolution X-ray Structure of the Substrate Recognition Domain of Higher Plant Rubisco Activase. J. Biol. Chem. 286, 35683-35688.r
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Markwardt, M. L., Kremers, G.-J., Kraft, C. A., Ray, K., Cranfill, P. J. C., Wilson, K. A., Day, R. N., Wachter, R. M., Davidson, M. W., Rizzo, M. A. (2011) An Improved Cerulean Flourescent Protein with Enhanced Brightness and Reduced Reversible Photoswitching. PlosOne 6, e17896.r
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Wachter, R. M., Watkins, J. L., Kim, H. (2010) Mechanistic Diversity of Red Fluorescence Acquisition by GFP-like Proteins. Current Topics Invited Review. Biochemistry 49, 7417-7427.r
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Barta, C., Dunkle, A. M., Wachter, R. M., Salvucci, M. E. (2010) Structural Changes Associated with the Acute Thermal Instability of Rubisco Activase. Archives of Biochemistry and Biophysics 499, 17-25.r
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Pouwels, L. J., Zhang, L., Chan, N. H., Dorrestein, P. C., Wachter, R. M. (2008) Kinetic Isotope Effect Studies on the de novo Rate of Chromophore Formation in Fast- and Slow-maturing GFP Variants. Biochemistry 47, 10111-10122.r
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Malo, G. D., Wang, M., Wu, D., Stellin, A., Tonge, P. J., Wachter, R. M. (2008) Crystal Structure and Raman Studies of dsFP483, a Cyan Fluorescent Protein from Discosoma striata. J. Mol. Biol. 378, 869-884.r
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Malo, G. D., Pouwels, L. J., Wang, M., Weichsel, A., Montfort, W. R., Rizzo, M. A., Piston, D. W., Wachter, R. M. (2007). X-ray Structure of Cerulean GFP: A Tryptophan-Based Chromophore Useful for Fluorescence Lifetime Imaging. Biochemistry 46, 9865-9873. Accelerated Publication.r
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Wachter, R. M. (2007). Chromogenic Cross-link Formation in Green Fluorescent Protein. Acc. Chem. Res. 40, 120-127r
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Zhang, L., Patel, H. N., Lappe, J. W., Wachter, R. M. (2006). Reaction Progress of Chromophore Biogenesis in Green Fluorescent Protein. J. Am. Chem. Soc. 128, 4766-4772.r
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Wachter, R. M. (2006). The family of GFP-like proteins: Structure, Function, Photophysics and Biosensor Applications. Introduction and Perspective, Symposium-in-print, Photochem. Photobiol. 82, 339-344r
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Wachter, R. M. (2006). Mechanistic Aspects of GFP Chromophore Biogenesis. Progress in Biomedical Optics and Imaging 7. Proc. of SPIE Vol. 6098, 609803-1 – 609803-8. Keynote Paper.r
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Wang, M., Patel, H. N., Wachter, R. M. (2005). X-ray Diffraction Analysis and Molecular Replacement Solution of the Cyan Fluorescent Protein dsFP483. Acta Crystallogr. F61, 922-924.r
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Sniegowski, J. A., Phail, M. E., Wachter, R. M. (2005). Maturation Efficiency, Trypsin Sensitivity and Optical Properties of Arg96, Glu222 and Gly67 Variants of Green Fluorescent Protein. Biochem. Biophys. Res. Comm. 332, 657-663.r
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Scruggs, A. W., Flores, C. L., Wachter, R. M., Woodbury, N. W. (2005). Development and Characterization of Green Fluorescent Protein Mutants with Altered Lifetimes. Biochemistry 44, 13377- 13384.r
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Rosenow, M. A., Patel, H. N, Wachter, R. M. (2005). Oxidative Chemistry in the GFP Active Site Leads to Covalent Cross-Linking of a Modified Leucine Side Chain with a Histidine Imidazole: Implications for the Mechanism of Chromophore Formation. Biochemistry 44, 8303-8311.r
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Sniegowski, J. A., Lappe, J. W., Patel, H. N., Huffman, H. A., Wachter, R. M. (2005). Base-catalysis of Chromophore Fromation in Arg96 and Glu222 variants of Green Fluorescent Protein. J. Biol. Chem. 280, 26248-26255.r
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Remington, S. J., Wachter, R. M., Yarbrough, D. K., Branchaud, B. P., Anderson, D. C., Kallio, K., Lukyanov, K. A. (2005). zFP538, a Yellow Fluorescent Protein from Zoanthus, Contains a Novel Three-Ring Chromophore. Biochemistry 44, 202-212.r
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Rosenow, M. A., Huffman, H. A., Phail, M. E., Wachter, R. M. (2004). The Crystal Structure of the Y66L Variant of Green Fluorescent Protein Supports a Cyclization-Oxidation-Dehydration Mechanism for Chromophore Maturation. Biochemistry 43, 4464-4472.r
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Wachter, R. M. (2004). Focus Note: The Art of Disentangling Difference Electron Density Maps: Snapshots of Early States in the Photoactive Yellow Protein Photocycle? Photochem. Photobiol. 80, No.1, ix-xr
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Bell, A. F., Stoner-Ma, D., Wachter, R. M., Tonge, P. J. (2003). Light Driven Decarboxylation of Wild-Type Green Fluorescent Protein. J. Am. Chem. Soc. 125, 6919-6926.r
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Yarbrough, D., Wachter, R. M., Kallio, K., Matz, M. V., Remington, S. J. (2001). Refined Crystal Structure of DsRed, a Red Fluorescent Protein from Coral, at 2.0 Å Resolution. Proc. Natl. Acad. Sci. USA 98, 462-467.r
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Wachter, R. M., Yarbrough, D., Kallio, K., Remington, S. J. (2000). Crystallographic and Energetic Analysis of Binding of Selected Anions to the Yellow Variants of Green Fluorescent Protein. J. Mol. Biol. 301, 159-173.r
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Bell, A. F., He, X., Wachter, R. M., Tonge, P. J. (2000). Probing the Ground State Structure of the Green Fluorescent Protein Chromophore Using Raman Spectroscopy. Biochemistry 39, 4423-4431.r
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Jayaraman, S., Haggie, P., Wachter, R. M., Remington, S. J., Verkman, A. S. (2000). Mechanism and Cellular Applications of a Green Fluorescent Protein-based Halide Sensor. J. Biol. Chem. 275, 6047-6050.r
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Wachter, R. M., Remington, S. J. (1999). Sensitivity of the YFP Form of Green Fluorescent Protein to Halides and Nitrate. Curr. Biol. 9, R628-R629.r
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Elsliger, M.-A., Wachter, R. M., Kallio, K., Hanson, G. T., Remington, S. J. (1999). Structural and Spectral Response of Green Fluorescent Protein Variants to Changes in pH. Biochemistry 38, 5296-5301.r
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Wachter, R. M., Elsliger, M.-A., Kallio, K., Hanson, G. T., Remington, S. J. (1998). Structural Basis of Spectral Shifts in the Yellow-emission Variants (YFPs) of Green Fluorescent Protein. Structure 6, 1267-1277.r
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Wachter, R. M., Branchaud, B. P. (1998). Construction and Analysis of a Semi-quantitative Energy Profile for the Reaction Catalyzed by the Radical Enzyme Galactose Oxidase. Biochim. Biophys. Acta 1384, 43-54.r
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Wachter, R. M., King, B. A., Heim, R., Kallio, K., Tsien, R. Y., Boxer, S. G., Remington, S. J. (1997). Crystal Structure and Photodynamic Behavior of the Blue-emission Variant Y66H/Y145F of Green Fluorescent Protein. Biochemistry 36, 9759-9765.r
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Wachter, R. M., Montague-Smith, M. P., Branchaud, B. P. (1997). Beta-Haloethanol Substrates as Probes for Radical Mechanisms for Galactose Oxidase. J. Am. Chem. Soc. 119, 7743-7749.r
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Wachter, R. M., Branchaud, B. P. (1996). Thiols as Mechanistic Probes for Catalysis by the Free Radical Enzyme Galactose Oxidase. Biochemistry 35, 14425-14435.r
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Wachter, R. M., Branchaud, B. P (1996). Molecular Modeling Studies on Oxidation of Hexopyranoses by Galactose Oxidase. An Active Site Topology Apparently Designed to Catalyze Radical Reactions, Either Concerted or Stepwise. J. Am. Chem. Soc. 118, 2782-2789.
Montague-Smith, M. P., Wachter, R. M., Branchaud, B. P. (1992). Preparation of Fully Oxidized Active and Reduced Inactive Forms of Galactose Oxidase from Dactylium dendroides Using Ferricyanide-containing Oxidizing and Ferrocyanide-containing Reducing Forms of Ion Exchange Resins. Anal. Biochem. 207, 353-355.

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