Catherine Ann Royer Principle Investigator

  1. Members
  2. Catherine Ann Royer

How can you be contacted?

royerc (at) rpi.edu

Education

University of Illinois at U-C Champaign, IL

  • PhD, Biochemistry; 1985

    • Université Pierre et Marie Curie Paris, France

  • Licence, Biochemistry; 1979

    • Université Pierre et Marie Curie Paris, France

  • D.E.U.G., Natural Sciences; 1978

    • Awards and Recognition

  • NSF-CNRS Postdoctoral Fellow – 1985-1986
  • NIH FIRST Award – 1988
  • Whitaker Foundation Young Investigator Award in Bio-Engineering 1992
  • Teacher of the Year – University of Wisconsin Madison School of Pharmacy 1993, 1994
  • Elected Fellow – American Association for the Advancement of Science, 2000
  • PES – Prime pour l’Excellence Scientifique – INSERM – 2012
  • Honorary Professor and Foreign Expert – East China Normal University – Shanghai China – 2013 - present

    • Publications Most Current

    1986

  • Scarlata, S.F. and C.A. Royer. Ligand Induced Asymmetry as Observed through Fluorophore Rotations and Free Energy Couplings: Application to Neurophysin", Biochemistry 25, 4925, (1986).
  • Royer, C.A., G. Weber, T.J. Daly, and K.S. Matthews. Dissociation of the lactose Repressor Tetramer Using High Hydrostatic Pressure, Biochemistry 25, 8308 (1986).

    • 1987

  • Royer, C.A. and Alpert., B. Porphyrin Dynamics in the Heme Pockets of Myoglobin and Hemoglobin., Chem. Phys. Lett. 134, 454 (1987).
  • Royer, C.A., P. Tauc, G. Herve, and J.C. Brochon. Ligand Binding and Protein Dynamics: A Fluorescence Depolarization Study of Aspartate Transcarbamylase from Escherichia coli, Biochemistry 26, 6472 (1987).

    • 1989

  • Royer, C.A., Rusch, R. and Scarlata, S.F. Salt Effects on Histone Subunit Interactions, Biochemistry 28, 6631 (1989).
  • Scarlata, S.F., Ropp, T. and Royer, C.A. Histone Subunit Interactions as Investigated by High Pressure, Biochemistry 28, 6637 (1989).

    • 1990

  • Royer, C.A., Matthews, K.S. and Chakerian, A. Macromolecular Binding Equilibria in the lac Repressor System as Studied by High Pressure Fluorescence Spectroscopy, Biochemistry 29, 959 (1990).
  • Royer, C.A., Gardner, J., Beechem, J.M., Brochon, J.C. and Matthews, K.S. Resolution of the Intrinsic Fluorescence Decay Kinetics of the Two Trytophan Residues of the Lactose Repressor of E. coli Using Site Directed Single Tryptophan Mutants, Biophys J, 58, 363 (1990).
  • Pin, S., Royer, C. A., Alpert, B., Gratton, E. and Weber, G. Subunit Interactions in Hemoglobin Probed by Fluorescence and High Pressure Techniques, Biochemistry 29, 9194 (1990).

    • 1991

  • Royer, C. A. "Macromolecular Assemblies Studied Using High Pressure Fluorescence Spectroscopy", published in Time-Resolved Laser Spectroscopy in Biochemistry, J.R. Lackowicz, editor, Vol. II, Proc. SPIE OE/LASE, 1202, (1991).
  • Royer, C. A., Smith, W. R. and Beechem, J.M. Analysis of Binding in Macromolecular Complexes: A Generalized Numerical Approach, Analytical Biochem 192, 287 (1991).

    • 1992

  • Royer, C. A., Ropp, T. and Scarlata, S.F. Solution Studies of the Interaction Between Histone Core Proteins and DNA using Fluorescence Spectroscopy, Biophysical Chem 43, 197 (1992).
  • Royer, C. A. and Beechem, J.M. Numerical Analysis of Binding Data: Advantages, Practical Aspects and Implications, Methods in Enzymology, 210: 481. (1992).
  • Fernando, T. and Royer, C.A. The Role of Protein-Protein Interactions in the Regulation of Transcription by trp Repressor Investigated by Fluorescence Spectroscopy, Biochemistry 31, 3429-3441 (1992).
  • Fernando, T. and Royer, C. A. Unfolding of trp Repressor Studied Using Fluorescence Spectroscopic Techniques, Biochemistry 31, 6683 (1992).
  • Royer, C. A., Le Tilly, V. & Martin, K. Fluorescence Approaches to the Studyof Protein-DNA Interactions, Time-Resolved Laser Spectroscopy in Biochemistry III, J.R. Lackowicz, editor, Proc. SPIE OE/LASE, Vol. 1640, 126. (1992).
  • Royer, C. A. Characterization of the Structural Determinants of the Intrinsic Fluorescence of trp repressor, Biophys J. 63, 741 (1992).
  • Moss, M. L., Palmer, R. E., Kuzmic, P., Dunlap, B. E., Mellon, W. S., Royer, C.A. & Rich, D. H. Identification of Actin and HSP70 as Cyclosporin A Binding Proteins by Photoaffinity Labeling and Fluorescence Displacement Assays, J. Biol. Chem. 267, 2054 (1992).

    • 1993

  • Royer, C. A. Improvements in the Numerical Analysis of Thermodynamic Data from Biomolecular Complexes, Analytical Biochem, 210, 91-97 (1993).
  • Royer, C. A., Hinck, A., Loh, S., Prehoda, K., Xiangdong, P., Jonas, J. & Markley, J., Effect of Amino Acid Substitution on the Pressure Denaturation of Staphylococcal Nuclease as Monitored by Fluorescence and NMR Spectroscopy, Biochemistry, 32, 5222-5232 (1993).
  • LeTilly, V. & Royer, C. A. Fluorescence Anisotropy Assays Implicate Protein-Protein Interactions in Regulating trp Repressor DNA Binding, Biochemistry 32, 7753-7758 (1993).
  • Royer, C. A., Mann, C. & Matthews, C.R. Resolution of the Fluorescence Equilibrium Denaturation Profile of trp Repressor Using Single Tryptophan Mutants, Protein Science 2, 1844 (1993).
  • Mann, C. J., Royer, C. A. & Matthews, C. R. Folding and Stability of Three Tryptophan Mutants of trp Aporepressor from Escherichia coli, Protein Science 2, 1853 (1993).
  • Govindjee, Van de Ven, M., Cao, J., Royer, C. & Gratton, E. Multi-frequency cross-correlation phase fluorometry of chlorophyll a fluorescence in thylalkaloid and PSII enriched membranes, Photochem. Photobiol. 58, 438-45 (1993).

    • 1994

  • Pin, S. and Royer, C. A. Using High Pressure Fluorescence Methods to Observe Subunit Dissociation in Hemoglobin, Methods in Enzymology, (1994).
  • Martin, K. S., Royer, C. A., Howard, K. P., Carey, J., Liu, Y-C., Matthews, K. S., Heyduk, E. & Lee, J. C. Electrostatic Forces Contribute to Interactions Between trp Repressor Dimers, Biophys. J. 66, 1167 (1994).

    • 1995

  • Royer, C. A. Protein Folding Studied by Fluorescence Spectroscopy, Methods in Molecular Biology, Humana Press, Inc. (1995).
  • Vidugiris, G.A.J., Markley, J. L. & Royer, C. A. Evidence for a Molten-Globule-Like Transition State in Protein Folding from Determination of Activation Volumes, Biochemistry 34, 4909-4912 (1995).
  • Royer, C.A. Approaches to Teaching Fluorescence Spectroscopy, Biophys J. 68, 1191-1195 (1995).
  • Reedstrom, R. J. & Royer, C. A. Evidence for Coupled Folding and Function in trp Repressor: Physical Characterization of the AV77 Super-repressor, J. Mol. Biol. 253, 266-276 (1995).
  • Royer, C. A. The Application of High Pressure to Biochemical Equilibria: What Can We Learn from The Other Thermodynamic Variable? Methods in Enzymology, 259, 357-376, M. Johnson and G. Ackers, editors, (1995).

    • 1996

  • Vidugiris, G. A. J., Truckses, D., Markley, J. L. & Royer, C. A. Proline Isomerization and the High Pressure Denaturation of Staphylococcal Nuclease, Biochemistry 35, 3857-3864. (1996).
  • Sire, O., Alpert, B., Weber, G. & Royer, C. A. Environment of the Myoglobin Heme Pocket Monitored by the DANCA Fluorophore, Biophys J., 70, 2903-2914. (1996).
  • Vidugiris, G., Thomas, R. & Royer, C. A. Pressure-Jump Relaxation Kinetics of Unfolding and Refolding Transitions of Staphylococcal Nuclease and Proline Isomerization Mutants, in High Pressure Effects in Molecular Biophysics and Enzymology, J.L. Markley, D. B. Northrup and C. A. Royer, eds., Oxford University Press, Oxford, England (1996).
  • Frye, K. J., Perman, C. & Royer, C. A. Correlation Between Area and Volume of Unfolding for Site Specific Mutants of Staphylococcal Nuclease, Biochemistry 31 10234-10239 (1996).
  • Gratton, E., Mantulin, W. W., Weber, G, Royer, C. A., Jameson, D. M., Reininger, R & Hansen, R. W. C., "Fluorescence Dynamics of Biological Systems Using Synchrotron Radiation", Rev. Sci. Instrum., 67, 1-9 (1996).
  • Reedstrom, R. J., Martin, K. S., Vangala, S., Mahoney, S. Wilker, E. W. & Royer, C.A. Characterization of Charge Change Super-Repressor Mutants of trp Repressor: Effects on Oligomerization, Conformation, Ligation and Stability J. Mol. Biol. 264, 32- 45 (1996).

    • 1997

  • Frye, K. J. & Royer, C. A. The Kinetic Basis for the Stabilization of Staphylococcal Nuclease by Xylose, Protein Science 6, 789-793 (1997).
  • Maleki, S.J., Royer, C.A. & Hurlburt, B.K. MyoD-E12 Heterodimers and MyoD-MyoD Homodimers are Equally stable, Biochemistry 36, 6762-6767 (1997).
  • Hill, J. J & Royer, C. A. Fluorescence Approaches to Characterizing Protein Nucleic Acid Complexes", Meth. Enzymol. 278, 390-416 (1997).
  • Brown, M.P. & Royer, C.A. Fluorescence Spectroscopy as a tool to investigate protein interactions. Curr Opin Biotechnol 8, 45-49 (1997).
  • Reedstrom, R.J., Brown, M.P., Grillo, A., Roen, D. & Royer, C.A. Affinity and Specificity of trp Repressor-DNA Interactions Studied with Fluorescent Oligonucleotides, J. Mol. Biol. 273, 572-585 (1997).
  • Ozers, M.S., Hill, J.J., Ervin, K., Wood, J.R., Nardulli, A., Royer, C.A. & Gorski, J. Equilibrium Binding of Estrogen Receptor with DNA Using Fluorescence Anisotropy, J. Biol. Chem. 272, 30405-30411 (1997).

    • 1998

  • Panick, G. Malessa, R., Winter, R., Rapp, G. Frye, K.J. & Royer, C.A. Structural Characterization of the Pressure-Denatured State and the Kinetics of Folding/Unfolding of Staphylococcal Nuclease by Synchrotron Small Angle X-ray Scattering and Fourier Transform Infrared Spectroscopy, J. Mol. Biol. 275, 389-402 (1998).
  • Vidugiris, G.J.A. & Royer, C.A. Determination of the Volume Changes for the Pressure-Induced Transitions of Apomyoglobin between the Native, Molten Globule and Unfolded States, Biophys. J. 75, 463-470 (1998).
  • Vangala, S., Vidugiris, G.A.J. & Royer, C.A. Probing the Relation Between Protein Structure and Intrinsic Tryptophan Fluorescence Using Super-repressor Mutants of the trp Repressor J. Fluorescence 8, 1-11 (1998).
  • Frye, K.J. & Royer, C.A. Probing the Contribution of Internal Cavities to the Volume Change of Protein Folding Under Pressure, Protein Sci. 7, 2217-2222 (1998).
  • Margeat, E., LeGrimellec, C. & Royer, C.A. Visualization of trp Repressor and its complexes with DNA by Atomic force Microscopy, Biophys. J. 75, 2712-2720 (1998).

    • 1999

  • Strugnell, S.A., Hill, J. J., McCaslin, D. R., Wieffling, B. A., Royer, C. A. & DeLuca, H. F. Bacterial Expression and Characterization of the Ligand Binding Domain of the Vitamin D Receptor, Arch. Bioch. Biophys. 364, 42-52 (1999).
  • Brown, M. P., Grillo, A.O. Boyer, M. & Royer, C. A. Probing the Role of Water in the tryptophan repressor-operator complex, Protein Sci., 8, 1276-1285 (1999).
  • Grillo, A.O., Brown, M.P. & Royer, C.A. Probing the physical basis for trp repressor-operator Recognition, .J. Mol. Biol. 287, 539-554 (1999).
  • Desai, G., Panick, G., Zein, M., Winter, R. & Royer, C. A. High Pressure Studies of the Folding/Unfolding of trp repressor, J. Mol. Biol, 288, 461-475 (1999).
  • Royer, C. A. Pressure Denaturation of Proteins, High Pressure Molecular Science, NATO ASI R. Winter & J. Jonas, eds. Kluwer Academic Publishers, The Netherlands (1999).
  • Panick, G., Vidugiris, GJA, Mallessa, R., Rapp, G., Winter R. & Royer C.A. Exploring the Temperature-Pressure Phase Diagram of staphylococcal Nuclease, Biochemistry 38, 4157-4164 (1999).
  • Chae Y.K., Abildgaard F., Royer C.A., Markley J.L. Oligomerization of the EK18 mutant of the trp repressor of Escherichia coli as observed by NMR spectroscopy., Arch Biochem Biophys 37, 135-40 (1999).
  • Thenot S., Bonnet S., Boulathouf A., Margeat, E., Royer, C., Borgna J.L. and Cavailles V. Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1LPHand estrogen receptors, J. Mol. Endocrino, 13, 2137-2150 (1999).

    • 2000

  • Grillo, A.O. & Royer, C.A. The basis for the super-repressor phenotypes of the AV77 and EK18 mutants of the trp repressor, J. Mol. Biol. 295, 17-28 (2000).
  • Boyer, M., Poujol, N., Margeat, E. & Royer, C.A. Quantitative characterization of the interaction between purified human estrogen receptor  and DNA using fluorescence anisotropy, Nucl. Acids. Res. 28, 2494-2505 (2000).
  • Royer, C.A. Protein folding and stability, What can we learn from high pressure? In High Pressure Research, 19, Harwood Academic Publishers, London, 603-312 (2000).

    • 2001

  • Woenckhaus, J., Köhling, R., Thiyagarajan, P., Littrell, K.C., Seifert, S., Royer, C.A. & Winter, R. Pressure-Jump SAXS Detected Kinetics of Staphylococcal Nuclease Folding, Biophys. J. 80, 1518-23 (2001).
  • Margeat, E., Poujol, N, Boulahtouf, A., Chen, Y., Muller, J., Gratton, E., Cavaillès, V. & Royer, C.A. The Estrogen receptor  dimer binds a single SRC-1 coactivator molecule with an affinity dictated by Agonist structure. J. Mol. Biol. 306, 433-454 (2001).
  • Seeman, H., Winter, R. & Royer, C.A. Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease, J. Mol. Biol 307, 1091-102 (2001).
  • Ozers M, Hill JJ, Ervin K, Royer CA, Gorski J., The dissociation rate of estrogen receptor alpha from the consensus estrogen response element, Mol Cell Endocrinol, 175, 101-9 (2001).
  • Royer, C.A. Super-repressor, in Encyclopedia of Genetics, Academic Press, pub., p1896, (2001).
  • Roumestand, C., Boyer, M., Guignard, L., Barthes, P., & Royer, C.A. Characterization of the Folding and Unfolding Reactions of a Small -Barrel Protein of Novel Topology, the MTCP1 Oncogene Product P13, J. Mol. Biol. 312, 247-259. (2001).
  • Silva, J. L., Foguel, D. & Royer, C.A. New Insights into protein folding, dynamics and structure from high pressure studies, TiBS, 26, 612-618. (2001).
  • Declerck, N., Dutartre, H. Receveur, V., Dubois, V., Royer, C., Aymerich, S. & van Tilbeurgh, H. Dimer stabilization upon activation of the transcriptional anti-terminator, LicT, J. Mol. Biol. 314, 671-681 (2001).

    • 2002

  • Royer, C.A. Revisiting the volume change of protein unfolding by pressure, Biochem. Biophys. Acta, 1595 (1-2), 201-209, (2002).
  • Royer, C.A. A discussion of the physical basis for the pressure unfolding of proteins, in Proceedings of the HPBB, R. Hayashi, ed. Elsevier Science, B.V., The Netherlands, pp.17-25 (2002).
  • Baud, S., Margeat, E., Lumbroso, S., Paris, F., Sultan C., Royer, C. & Poujol, N. Equilibrium Binding studies reveal the elevated stoichiometry and salt dependence of the interaction between full-length human SRY and DNA, J. Biol. Chem. 277, 18404-18410 (2002).
  • Kitahara, R., Royer, C.A., Yamada, H., Boyer, M., Saldana, J.-L., Akasaka, K. & Roumestand, C. Equilibrium and Pressure-jump Relaxation Studies of the Conformational Transitions of P13MTCP1, J. Mol. Biol. 320, 609-628 (2002).
  • Maleki, S. J., Royer, C. A. & Hurlburt, B. K. Analysis of the DNA binding properties of MyoD, myogenin and E12 by fluorescence anisotropy, Biochemistry 41, 10888-10894 (2002).
  • Twist, C., Royer, C. & Alpert, B. Effect of Solvent Diffusion on the Apomyoglobin-Water Interface, Biochemistry 41, 10343-10350 (2002).

    • 2003

  • Van Uden, N.W.A., Hubel, H., Faux, D.A., Dunstan, D. J. & Royer, C.A. Negative effective pressures in liquid mixtures, High Pressure Res. 23, 205-209 (2003).
  • Poujol, N., Margeat, E., Baud, S. & Royer, C.A., RAR Antagonists Diminish DNA Binding by the RAR/RXR Heterodimer, Biochemistry 42, 4918-4925 (2003).
  • Czeslik, C., Royer, C., Hazlett, T. & Mantulin, W., Reorientational Dynamics of Enzymes Adsorbed on Quartz: a Temperature-Dependent Time-Resolved TIRF Anisotropy Study, Biophys. J, 84, 2533-2531 (2003).
  • Bayley, P., Martin, S., Browne, P. & Royer, C.A. Time-Resolved Fluorescence Anisotropy Studies show Domain-Specific Interactions of Calmodulin with IQ Target Sequences of Myosin V, E. Biophys. J., 32, 122-127 (2003).
  • Margeat, E., Bourdoncle, A., Raphael Margueron, Nicolas Poujol, Cavaillès, V. & Royer, C.A. Ligands Differentially Modulate the Protein Interactions of the Human Estrogen Receptors  and , J. Mol. Biol. 326, 77-92 (2003).

    • 2004

  • 82. Herberhold H, Royer CA, Winter R. Effects of Chaotropic and Kosmotropic Cosolvents on the Pressure-Induced Unfolding and Denaturation of Proteins: An FT-IR Study on Staphylococcal Nuclease. Biochemistry 43, 3336-45 (2004).
  • 81. Czeslik C, Jansen R, Ballauff M, Wittemann A, Royer CA, Gratton E, Hazlett T. Mechanism of protein binding to spherical polyelectrolyte brushes studied in situ using two-photon excitation fluorescence fluctuation spectroscopy. Phys Rev E 69, 021401 (2004).
  • 80. Ravindra, R., Royer, C. & Winter, R. Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of staphylococcal nuclease, Phys. Chem. Chem. Phys. 6, 1952-1961 (2004).
  • 79.Auguin, D., Barthe, P., Royer, C., Stern, M-H., Noguchi, M., Arold, S.T. & Roumestand, C. Structural basis for the coactivation of Protein Kinase B by TCL1 family proto-oncoproteins J. Biol. Chem. 279, 35890-902 (2004).

    • 2005

  • Guillier M, Allemand F, Dardel F, Royer CA, Springer M, Chiaruttini C., Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA. Mol Microbiol. 56, 1441-56 (2005).
  • Pogenberg V, Guichou JF, Vivat-Hannah V, Kammerer S, Perez E, Germain P, de Lera AR, Gronemeyer H, Royer CA, Bourguet W. Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. J Biol Chem.; 280:1625-33 (2005).
  • Stricher F, Martin L, Barthe P, Pogenberg V, Mechulam A, Menez A, Roumestand C, Veas F, Royer C, Vita C. A high-throughput fluorescence polarization assay specific to the CD4 binding site of HIV-1 glycoproteins based on a fluorescein-labelled CD4 mimic. Biochem J. 390, 29-39 (2005).
  • Bourdoncle A, Labesse G, Margueron R, Castet A, Cavailles V, Royer CA. The nuclear receptor coactivator PGC-1alpha exhibits modes of interaction with the estrogen receptor distinct from those of SRC-1. J Mol Biol. 347, 921-34 (2005).
  • Jackler G, Czeslik C, Steitz R, Royer CA. Spatial distribution of protein molecules adsorbed at a polyelectrolyte multilayer, Phys Rev E Stat Nonlin Soft Matter Phys. 041912 (2005).

    • 2006

  • Rosales, T, Georget, V, Malide, D., Smirnov, A., Xu, J., Combs, C., Knutson, J.R., Nicolas, J.-C. & Royer, C.A.* Quantitative detection of the ligand-dependent interaction between the androgen receptor and the co-activator, Tif2, in live cells using two color, two photon fluorescence cross-correlation spectroscopy. Eur. Biophys. J., 36, 153-161. (2006).
  • Royer, C.A. and Scarlata, S.F. Fluorescence Approaches to Quantifying Bio-molecular Interactions, Methods in Enzymology, Fluorescence Spectroscopy, Eds., Ludwig Brand, Michael Johnson, pp 79-106, (2006).
  • Margeat, E., Boukari, H. & Royer, C.A The Characterization of Bio-molecular Interactions Using Fluorescence Fluctuation Techniques in Protein Interactions, Protein Reviews, P. Schuck, A. Attassi, Eds. Springer, NY, NY. (2006).
  • Mitra L, Smolin N, Ravindra R, Royer C, Winter R. Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution—experiments and theoretical interpretation, Phys Chem Chem Phys. 8, 1249-65 (2006).
  • Brun, L., Isom, D. Velu, P., Garcia-Moreno, B. & Royer, C.A. Hydration of the folding transition state ensemble of a protein, Biochemistry, 45, 3473-3480 (2006).
  • Royer, C.A. Probing Protein Folding and Conformational Transitions in Proteins with Fluorescence, Chemical Reviews 106, 1769. (2006).

    • 2007

  • Mitra, L., Hata, K., Kono, R., Maeno, A., Isom, D., Rouget, J.B., Winter, R., Akasaka, K.,Garcia-Moreno E., B. & Royer, C.A., Vi-Value Analysis: A Pressure-Based Method for Mapping the Folding Transition State Ensemble of Proteins, J Am Chem Soc, 129, 14108-14109, (2007).
  • Zorrilla,S., Chaix, D., Ortega, A., Alfonso, C., Doan, T., Margeat, E., Rivas, G., Aymerich, S., Declerck, N. & Royer, C.A. Fructose-1,6-Bisphosphate acts both as an inducer and as a structural cofactor of the Central Glycolytic Genes Repressor (CggR), Biochemistry, 46, 14996-15008, (2007).
  • Nahoum, V., Perez, E., Germain, P., Rodriguez-Barrios, F., Manzo, F., Kammerer, S., Lemaire, G., Hirsch, O., Royer, C.A., Gronemeyer, H., De Lera, A.R., & Bourguet, W., Modulators of the Structural Dynamics of RXR to Reveal Receptor Function, Proc. Natl. Acad. Sci. USA, 104(44):17323-8 (2007).
  • Blin, G., Margeat, E., Carvalho, K., Royer, C.A., Roy, C. & Picart, C. Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol(4,5)- bisphosphate, Biophys. J. 94, 1021-1033 (2007).
  • Royer, C. A. The Nature of the Folding Transition State and the Mechanisms of Protein Folding: A Review, Archives of Biochemistry and Biophysics, 469, 34-45 (2007).
  • Viaud, J., Zeghouf, M., Barelli,,H., Zeeh, J.-C., Padilla, A., Guibert, B., Chardin, P., Royer, C., Cherfils, J. & Chavanieu, A., Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein–protein complexes, Proc. Natl. Acad. Sci. USA, 104,10370 (2007).
  • Zorrilla S, Doan T, Alfonso C, Margeat E, Ortega A, Rivas G, Aymerich S, Royer CA, Declerck N. Inducer-Modulated Cooperative Binding of the Tetrameric CggR Repressor to Operator DNA. Biophys J., 92, 3215-27. (2007).
  • Allemand F, Haentjens J, Chiaruttini C, Royer C, Springer M. Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites. Nucleic Acids Res. 35, 3016. (2007).

    • 2008

  • Krywka, C., Sternemann, C., Paulus, M., Tolan, M., Royer, C. & Winter, R Effects of osmolytes on pressure-induced unfolding of proteins, Chem Phys Chem ,9, 2809-2815 (2008).
  • Mitra, L., Rouget, J.B., Royer, C.A. & Winter, R. Towards a quantitative understanding of protein hydration and volume properties, Chem Phys Chem, 9, 2715-2721 (2008).
  • Espenel C, Margeat E, Dosset P, Arduise C, Le Grimellec C, Royer CA, Boucheix C, Rubinstein E, Milhiet PE. Single-molecule analysis of CD9 dynamics and partitioning reveals multiple modes of interaction in the tetraspanin web. J Cell Biol. 182(4):765-76 (2008).
  • Zorrilla S, Ortega A, Chaix D, Alfonso C, Rivas G, Aymerich S, Lillo P, Declerck N, Royer CA, (2008) Characterization of the CcpN repressor by FCCS and other biophysical approaches, Biophys J. 95, 4403-4415, (2008).
  • Rosales, T. and Royer, C.A. A graphical user interface for BIOEQS: a program for simulating and Analyzing complex biomolecular interactions, Anal Biochem. 381(2):270-2, (2008).

    • 2009

  • Germain, P., Gaudon, C., Pogenberg, V. Sanglier, S., Van Dorsselaer, A., Royer, C.A., Lazar, M.A., Bourguet, W., & Gronemeyer, H. Differential Action on Coregulator Interaction Defines Inverse Retinoid Agonists and Neutral Antagonists, Chem. Biol. 16, 1-11 (2009).

    • 2010

  • Schroer, M., Paulus, M., Jeworrek, C., Krywka, C., Schmake, S., Zhai, Y., Florian Weiland, D. C., Sahle, C., J., Chimenti, M., Royer, C. A., Garcia-Moreno, B., Tolan, M. and Winter, R. High pressure SAXS studies of folded and unfolded ensembles of proteins, Biophys. J., 99, 3430-3437 (2010).
  • Chaix, D., Ferguson,M.L., Atmanéné, C., Van Dorsselaer, A., Sanglier-Cianferani, S., Royer, C.A. & Declerck, N. Physical basis of the inducer-dependent cooperativity of the CggR repressor/DNA complex, Nucl. Acids Res., 38, 5944-5957 (2010).
  • Savatier J, Jalaguier S, Ferguson ML, Cavaillès V, Royer CA. Estrogen receptor interactions and dynamics monitored in live cells by fluorescence cross-correlation spectroscopy Biochemistry 49, 772-781 (2010).
  • Rouget, J.B., Schroer, M.A., Jeworrek, C., Pühse, M., Saldana, J.L., Bessin, Y., Tolan, M., Barrick, D., Winter, R., Royer, C.A Unique features of the folding landscape of a repeat protein revealed by pressure perturbation, Biophys J., 98, 2712-2721. (2010).
  • le Maire, A.,Teyssier, C., Erb, C., Grimaldi, M., Alvarez, S., de Lera, A.R., Balaguer, P., Gronemeyer, H., Royer, C.A., Germain, P. & Bourguet, W. A unique secondary structure switch controls constitutive gene silencing by retinoic acid receptor, Nat Struct Mol Biol., 17, 801-807 (2010).

    • 2011

  • Ferguson, M. L., Le Coq, D., Jules, M., Aymerich, S., Declerck, N., and Royer, C. A., Absolute quantification of gene expression in individual bacterial cells using two-photon fluctuation microscopy, Anal. Biochem. 419, 250-9 (2011).
  • Royer, C.A. and Winter, R. Protein Hydration and Volumetric Properties, Current Opinion in Colloid and Interface Sci., 16, 568-571, (2011).
  • Rouget, J.-B., Aksel, T., Roche, J., Saldana, J.-L., Garcia, A. E., Barrick, D., and Royer, C. A. Size and sequence and the volume change of protein folding, J Am Chem Soc S, 133, 6020-7, (2011).
  • Kitahara, R., Hata, K., Maeno, A., Akasaka, K., Chimenti, M., Garcia-Moreno E., B., Schroer , M. A., Jeworrek, C., Tolan, M., Winter, R., Roche, J., Roumestand, C., Montet de Guillen, K. and Royer, C. A. Structural plasticity of staphylococcal nuclease probed by perturbation by pressure and pH, Proteins, 79, 1293-1305 (2011).

    • 2012

  • SRoche J, Dellarole M, Caro JA, Guca E, Norberto DR, Yang Y, Garcia AE, Roumestand C, García-Moreno B, Royer CA. Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations. Biochemistry. 51, 9535-46 (2012).
  • Roche, J., Caro, JJ.A., Norberto D. R., Barthe, P., Roumestand, C., Schlessmann, J.L., Garcia, A.E., Garcia-Moreno E., B. & Royer, C.A. Cavities determine the pressure unfolding of proteins, Proc. Natl. Acad. Sci. USA 109, 6945-6950 (2012).
  • Ferguson, M. L., Le Coq, D., Jules, M., Aymerich, S., Radulescu, O., Declerck, N., and Royer, C. A., Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states, Proc. Natl. Acad. Sci. USA 109, 155-160 (2012).

    • 2013

  • Guca E, Roumestand C, Vallone B, Royer CA, Dellarole, M., Low cost equilibrium unfolding of heme proteins using 2μl samples, Anal Biochem. 443, 13-5, (2013).
  • Roche J., Dellarole M., Caro J.A., Norberto D.R., Garcia A.E., Garcia-Moreno, E. B., Roumestand, C., Royer, C.A., Effect of Internal Cavities on Folding Rates and Routes Revealed by Real-time Pressure-Jump NMR Spectroscopy. J Am Chem Soc., 134, 14610-14618, (2013).
  • Docquier, A., Garcia, A., Savatier, J., Boulahtouf, A., Bonnet, S., Bellet, Busson, M., Margeat, E., Jalaguier, S., Royer, C., Balaguer, P., Cavaillès, V. Negative regulation of estrogen signaling by ERβ and RIP140 in ovarian cancer cells., Mol. Endocrin. 9, 1429-41 (2013).
  • Dellarole, M., Kobayshi, K., Rouget, J.-B., Caro, J. A., Roche, J., Islam, M., Garcia-Moreno E., B., Kuroda, K. & Royer, C. A., Probing the Physical Determinants of Thermal Expansion of Folded Proteins, J. Phys. Chem. B. 117, 12742-9 (2013).
  • Fiche, JB., Cattoni, D. I., Diekmann1, N., Langerak, J., Clerte, C., Royer, C.A., Margeat, E., Doan, T., Nöllmann, M., Recruitment, assembly and molecular architecture of the SpoIIIE DNA pump revealed by super-resolution microscopy, Plos Biology (e1001557.) (2013).
  • Dellarole, M., Roumestand, C., Royer, C. & Lecompte, J.T.J. Volumetric properties underlying ligand binding in a monomeric hemoglobin: A high pressure NMR study, Biochim. Biophys. Acta., 9, 1910-22 (2013).
  • Declerck, N. & Royer, C.A. Interactions in gene expression networks studied by two-photon fluorescence fluctuation spectroscopy, in Fluctuation Spectroscopy, Methods in Enzymology, S. Tetin, ed., Springer, NY 519, 203-230 (2013).
  • Roche J, Caro JA, Dellarole M, Guca E, Royer CA, E BG, Garcia AE, Roumestand C. Structural, energetic and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations. Proteins. 81, 1069-80. (2013).

    • 2014

  • Moutin, E., Compan, V., Raynaud, F., Clerté, C., Bouquier, N., Labesse, G., Ferguson, M., L., Fagni, L., Royer, C.A. , Perroy, J. , Stoichiometry of scaffold complexes in living neurons - DLC2 as a dimerization engine for GKAP, J. Cell Sci. 127, 3451-3462 (2014).
  • Dellarole M, Royer CA., High-pressure fluorescence applications, Methods Mol Biol., 1076, 53-74. (2014).
  • Sibille N, Dellarole M, Royer C, Roumestand C. Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure, J Biomol NMR, 58, 9-16 (2014).

    • 2015

  • Patterson MN, Scannapieco AE, Au PH, Dorsey S, Royer CA, Maxwell PH, Preferential retrotransposition in aging yeast mother cells is correlated with increased genome instability. DNA Repair, 34:18-27 (2015).
  • Vaissiere, A; Berger, S; Harrus, D; Dacquet, C; Le Maire, A Boutin, JA; Ferry, G; Royer, CA Molecular mechanisms of transcriptional control by Rev-erb alpha: An energetic foundation for reconciling structure and binding with biological function, Protein Sci., 24, 1129-1146 (2015).
  • Dellarole, M., Caro, J.A., Roche, J., Fossat, M., Barthe, P., Garcia-Moreno E., B. Royer, C.A. and Roumestand, C. Evolutionarily conserved pattern of interactions in a protein revealed by local thermal expansion properties, J Am Chem Soc, 137, 9354-9362 (2015).
  • Sanfeld A, Royer C, Steinchen A., Thermodynamic, kinetic and conformational analysis of proteins diffusion-sorption on a solid surface. Adv Colloid Interface Sci 222, 639-660 (2015).

    • 2016

  • Zhang, Y., Kitazawa, S., Peran, I., Stenzoski, N., McCallum, S.A., Raleigh, D.P & Royer, C.A., High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States, J. Am. Chem. Soc., 13, 15260–15266 (2016).
  • Fossat, M. J., Dao, T. P., Jenkins, K., Dellarole, M., Yang, Y., McCallum, S. A., Garcia, A. E., Barrick, D., Roumestand, C. and Royer, C. A. High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape, Biophys. J. 111, 2368-2376 (2016).
  • Royer, C.A., Using Fluorescence to Characterize the Role of Oligomerization in the Regulation of Gene Expression, in Perspectives on Fluorescence: A Tribute to Gregorio Weber, D.M. Jameson, editor, Springer Series on Fluorescence, Springer Publishers, Switzerland, in press (2016).

    • 2017

  • Gao, M., Harish, B., Berghaus, M., Seymen, R., Arns, L., McCallum, S., Royer, C. & Winter, R. Temperature and pressure limits of guanosine monophosphate self-assemblies, Scientific Rep. 7 (2017).
  • Papini, C., Pandharapande, Royer, C. and Makhatadze, G. Putting the Piezolyte Hypothesis under Pressure, Biophys J. 113, 974-977 (2017).
  • Zwarycz AS, Fossat M, Akanyeti O, Lin Z, Rosenman DJ, Garcia AE, Royer CA, Mills KV, Wang C., V67L Mutation Fills an Internal Cavity To Stabilize RecA Mtu Intein, Biochemistry, 56:2715-2722, (2017).
  • Roche, J, Royer, C.A. & Roumestand, C. Monitoring Protein Folding Through High Pressure NMR Spectroscopy, Progress in Nuclear Magnetic Resonance Spectroscopy, (2017).
  • Bourges, A., Torres Montaguth, O.E., Ghosh, A., Tadesse, W.M., Declerck, N., Aertsen, A. and Royer, C.A. High pressure activation of the Mrr restriction endonuclease in Escherichia coli involves tetramer dissociation, Nuc. Acids. Res. 45, 5232-5332 (2017).
  • Kitazawa, S., Fossat, M.J., McCallum, S.A., Garcia, A. E and Royer, C.A. NMR and Computation Reveal a Pressure-Sensitive Folded Conformation of Trp-Cage, J. Phys. Chem B., 121, 1258-1267 (2017).

    • 2018

  • Roche, J. & Royer, C. A. Lessons from Pressure Denaturation of Proteins, J. Royal Soc. Interface, 15, 20180244, 2018.
  • Jenkins, K.A., Fossat, M.J., Zhang, S., Rai, D.K., Klein, S. Gillilan, R., White, Z., Gerlich, G., McCallum, S.A., Winter, R., Gruner, S.M., Barrick, D.& Royer, C.A. Consequences of Cavities on the Folding Landscape of a Repeat Protein Depend Upon Context, Proc. Natl. Acad. Sci. USA 115(35): E8153-E8161 (2018).
  • Knop, J.-M., Harish, B. Patra, S., Royer, C.A. & Winter, R., The Deep Sea Osmolyte TMAO and Macromolecular Crowders Rescue the Antiparallel Conformation of the Human Telomeric G-Quadruplex from Urea and Pressure Stress, Chemistry - A European Journal, 24, 14346-14351 (2018).
  • Møller, T.C., Hottin, J., Clerté, C., Zwier, J.M., Durroux, T., Rondard, P., Prézeau, L., Royer, C.A., Pin, J.-P., Margeat, E. & Kniazeff, J. Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics, Sci. Reports 8, 10414, (2018).
  • Dorsey, S., Tollis, S., Cheng, J., Black, L., Notley, S., Tyers, M. and Royer, C. A. G1/S Transcription Factor Copy Number is a Growth-Dependent Determinant of Cell Cycle Commitment in Yeast, Cell Systems, 6, 539+, (2018).
  • Andra, KK, Dorsey, A, Royer, C, Menon, AK Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer, J. Biol. Chem., RA118. 003648 (2018).
  • Papini, C. & Royer, C.A., Scanning Number and Brightness Yields Absolute Protein Concentrations in Live Cells: A Crucial Parameter Controlling Functional Bio-molecular Interaction Networks, Biophysical Reviews 10, 87-96 (2018).
  • Zhang, Y., Berghaus, M., Klein, S., Jenkins, K., Zhang, S., McCallum, S. A., Morgan, J. E., Winter, R., Barrick, D. & Royer, C. A. High Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine Rich Repeat Protein, J. Mol. Biol. 430, 1336-1349 (2018).

    • 2019

  • Royer, C. A. Characterizing proteins in their cellular environment: Examples of recent advances in quantitative fluorescence microscopy, Protein Science, 28, 1210–1221 (2019).
  • Zhang, S., Zhang, Y., Stenzoski, N., Zou, J., Peran, I., McCallum, S.A., Raleigh, D. & Royer, C.A. Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates Folding Intermediates of CTL9, Biophys. J. 116, 445-453 (2019).
  • Roche, J., Royer, C.A. & Roumestand, C., Exploring protein conformational landscapes using high pressure NMR, Methods Enz., 614, 293-320 (2019).

    • 2020

  • Bourges, A., A. Lazarev, N. Declerck, K.L. Rogers, and C. Royer. 2020. Quantitative high-resolution imaging of live microbial cells at high hydrostatic pressure. Biophys. J. 118, 2670-2679 (2020).
  • Black, L., Tollis, S., Fu, G., Fiche, J.-B., Dorsey, S., Cheng, J., Notley, S., Crevier, B., Bigness, J., Nollmann, M., Tyers, M. and Royer, C. A. G1/S transcription factors assemble in discrete clusters that increase in number as cells grow, J. Cell. Biol. 219, e202003041 (2020). 10.1083/jcb.202003041.

    • 2021

  • Bourges A.C., Torres-Montaguth, O.E., Tadesse, W., Labesse, G., Aertsen, A., Royer, C.A & Declerck, N. An oligomeric switch controls the Mrr-induced SOS Response in E. coli, DNA Repair, 97, 103009, 2021.
  • Ando, N., Barquera, B., Bartlett, D., Boyd, E., Burnim, A.A., Byer, A.S., Colman, D., Gillilan, R.E., Gruebele, M., Makhatadze, G., Royer, C.A.*, Shock, E., Wand, A.J. & Watkins, M.B. The molecular basis for life in extreme environments, Ann. Rev. Biophys., 50, 343-372 (2021).
  • Bafna, K., White, K., Harish, B., Rosales, R., Ramelot, T.A., Acton, T.B., Moreno, E., Kehrer, T., Miorin, L., Royer, C.A., Garcia-Sastre, A., Krug, R.M., & Montelione, G.T. HCV drugs that inhibit the SARS-CoV-2 papain-like protease synergize with remdesivir to suppress viral replication in cell culture, Cell Reports, 35, 109133 (2021).
  • Harish, B., Gillilan, R.E., Zou, J., Wang, J., Raleigh, D.P. & Royer, C. A. Protein unfolded states populated at high and ambient pressure are similarly compact, Biophys. J. 120, 2592-2598 (2021).

    • 2022

  • Tollis, S., Singh, J., Palou, R., Thattikota, Y., Ghazal, G., Coulombe-Huntington, J., Tang, X., Moore, S., Blake, D., Bonneil, E., Royer, C.A., Thibault, P. & Tyers, M., The microprotein Nrs1 rewires the G1/S transcriptional machinery during nitrogen limitation in budding yeast, PLoS Biology 20, e3001548 (2022).
  • Colman, D.R., Labesse, G., Swapna, G.V.T., Stefanakis, J. Montelione, G.T., Boyd, E.S. & Royer, C.A., Structural evolution of the ancient enzyme, Dissimilatory Sulfite Reductase, Proteins: Struct. Func. Bioinformatics 90, 1331-1345 (2022).
  • Litsios, A., Goswami, P., Terpstra, H.M., Coffin, C., Vuillemenot, L.-A., Rovetta, M., Ghazal, G., Guerra, P., Buczac, K., Schmidt, A., Tollis, S. Tyers, M.T., Royer, C.A., Milas-Argeitis, A. & Heinemann, M., The timing of Start is determined primarily by increased synthesis of the Cln3 activator rather than dilution of the Whi5 inhibitor, Mol. Biol. Cell. (in press).
  • Harish, B., Wang, J., Hayden, E.J., Grabe, B., Hiller, W, Winter, R. & Royer, C.A., Hidden intermediates in Mango III RNA aptamer folding revealed by pressure perturbation, Bophys. J., 121, 421-429 (2022).