Publications 2001 - Present

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2024

  • Koduru, T., Hantman, N., Peters, E. V., Jaworek, M. W., Wang, J., Zhang, S., McCallum, S. A. Gillilan, R. E., Fossat, M. J., Roumestand, C., Sagar, A., Winter, R., Bernadó, P., Cherfils J. & Royer, C.A., A molten globule ensemble primes Arf1-GDP for the nucleotide switch, PNAS (in press).

    • 2023

  • Mazzei, L., Greene-Cramer, R., Bafna, K., Jovanovic, A., De Falco, A, Royer, C.A., Ciurli, S., and Montelione, G.T., Protocol for production and purification of SARS-CoV-2 3CLpro, Star Protocols, 4, 102326 (2023).
  • Royer, C.A., Tyers, M. and Tollis, S. Absolute Quantification of Proteins in Single Cells Current Opinion in Structural Biology 82, 102673 (2023).
  • Wang, J., Koduru, T., Harish, B., McCallum, S.A., Larsen, K.P., Patel, K.S., Peters, E.V., Gillilan, R.E., Puglisi, E.V., Puglisi, J., Makhatadze, G. & Royer, C.A., Pressure pushes tRNALys3 into excited conformational states, Proc. Natl. Acad. Sci. USA 120, e2215556120. (2023).

    • 2022

  • Zhang, S., McCallum, S.A., Gillilan, R.E., Wang, J. & Royer, C.A., High pressure CPMG and CEST reveal that cavity position dictates distinct dynamic disorder in the pp32 repeat protein, J. Phys. Chem. B. 126, 10597-10607 (2022).
  • 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, Biophys. J., 121, 421-429 (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).
  • 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. 33, rp2 (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).

    • 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).
  • 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).
  • 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).

    • 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
  • 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).
  • Bourges A.C., Torres-Montaguth, O.E., Tadess, 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 2020.

    • 2019

  • Zhang, S., Zhang, Y., Stenzoski, N., 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).
  • Royer, C. A. Characterizing proteins in their cellular environment: Examples of recent advances in quantitative fluorescence microscopy, Protein Science, 28, 1210–1221 (2019).
  • Roche, J., Royer, C.A. & Roumestand, C., Exploring protein conformational landscapes using high pressure NMR, Methods Enz., 614, 293-320 (2019).

    • 2018

  • Roche, J. & Royer, C. A. Lessons from Pressure Denaturation of Proteins, J. Royal Soc. Interface, (in press) 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).
  • Roche, J., Royer, C.A. & Roumestand, C., Exploring protein conformational landscapes using high pressure NMR, Methods Enz., (in press) (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 (in press) (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).
  • 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).

    • 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).
  • 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. (2016), in press.
  • 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).

    • 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).
  • 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, JACS, 137, 9354-9362 (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).
  • 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).

    • 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).
  • Dellarole M, Royer CA., High-pressure fluorescence applications, Methods Mol Biol., 1076, 53-74. (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).

    • 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).
  • 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).
  • 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).
  • 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., 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).
  • 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).
  • 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).
  • 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).

    • 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).
  • 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). * This paper was the object of a Commentary in PNAS called “Proteins Under Pressure” by National Academy member Brian W. Matthews.
  • Roche 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).

    • 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).
  • 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, JACS, 133, 6020-7, (2011).
  • Royer, C.A. and Winter, R. Protein Hydration and Volumetric Properties, Current Opinion in Colloid and Interface Sci., 16, 568-571, (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).

    • 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).
  • 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).
  • 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).
  • 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).
  • 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).

    • 2009

  • Pierre 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).

    • 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).
  • 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).
  • 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).
  • 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).
  • 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).
  • 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, (2008).

    • 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).
  • 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).
  • 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, PNAS, 104,10370 (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).
  • 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).
  • 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, PNAS, 104(44):17323-8 (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).
  • 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, JACS, 129, 14108-14109, (2007).

    • 2006

  • Royer, C.A. Probing Protein Folding and Conformational Transitions in Proteins with Fluorescence, Chemical Reviews 106, 1769. (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).
  • 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).
  • 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).
  • 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).

    • 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).
  • 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).
  • 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).
  • 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).

    • 2004

  • 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).
  • 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).
  • 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).
  • 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).

    • 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 alpha and beta, J. Mol. Biol. 326, 77-92 (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).
  • 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).
  • Poujol, N., Margeat, E., Baud, S. & Royer, C.A., RAR Antagonists Diminish DNA Binding by the RAR/RXR Heterodimer, Biochemistry 42, 4918-4925 (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).

    • 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 Proceeding 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).

    • 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).

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