C. Royer

发表

Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding.

V. LeTilly, C. Royer, Veronique LeTilly, 1993, Biochemistry.

Characterization of charge change super-repressor mutants of trp repressor: effects on oligomerization conformation, ligation and stability.

R. J. Reedstrom, C. Royer, K. Martin, 1996, Journal of molecular biology.

Affinity and specificity of trp repressor-DNA interactions studied with fluorescent oligonucleotides.

C A Royer, R. J. Reedstrom, C. Royer, 1997, Journal of molecular biology.

Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states

Ovidiu Radulescu, Stéphane Aymerich, Matthieu Jules, 2011, Proceedings of the National Academy of Sciences.

Reorientational dynamics of enzymes adsorbed on quartz: a temperature-dependent time-resolved TIRF anisotropy study.

W. Mantulin, C. Royer, C. Czeslik, 2003, Biophysical journal.

Probing protein folding and conformational transitions with fluorescence.

C. Royer, 2006, Chemical reviews.

Evidence for coupling of folding and function in trp repressor: physical characterization of the superrepressor mutant AV77.

R. J. Reedstrom, C. Royer, 1995, Journal of molecular biology.

The consequences of cavity creation on the folding landscape of a repeat protein depend upon context

Zackary White, Sol M. Gruner, Catherine A. Royer, 2018, Proceedings of the National Academy of Sciences.

Lessons from pressure denaturation of proteins

C. Royer, J. Roche, Julien Roche, 2018, Journal of The Royal Society Interface.

Exploring the temperature-pressure phase diagram of staphylococcal nuclease.

C. Royer, R. Winter, G. Rapp, 1999, Biochemistry.

Ligand-induced asymmetry as observed through fluorophore rotations and free energy couplings: application to neurophysin.

C. Royer, S. Scarlata, 1986, Biochemistry.

Volumetric properties underlying ligand binding in a monomeric hemoglobin: a high-pressure NMR study.

C. Roumestand, C. Royer, J. Lecomte, 2013, Biochimica et biophysica acta.

G1/S transcription factors assemble in increasing numbers of discrete clusters through G1 phase

M. Tyers, M. Nollmann, Jing Cheng, 2020, The Journal of cell biology.

Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of Staphylococcal nuclease.

C. Royer, R. Winter, H. Seemann, 2001, Journal of molecular biology.

High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States.

D. Raleigh, C. Royer, S. McCallum, 2016, Journal of the American Chemical Society.

Pressure perturbation calorimetic studies of the solvation properties and the thermal unfolding of staphylococcal nuclease

C. Royer, R. Winter, R. Ravindra, 2004 .

Driving forces for the adsorption of enzymes at the water/silica interface studied by total internal reflection fluorescence spectroscopy and optical reflectometry

C. Royer, C. Czeslik, G. Jackler, 2002 .

Low-cost equilibrium unfolding of heme proteins using 2 μl samples.

B. Vallone, C. Roumestand, C. Royer, 2013, Analytical biochemistry.

Probing pH and pressure effects on the apomyoglobin heme pocket with the 2'-(N,N-dimethylamino)-6-naphthoyl-4-trans-cyclohexanoic acid fluorophore.

C. Royer, O. Sire, B. Alpert, 1996, Biophysical journal.

Estrogen receptor interactions and dynamics monitored in live cells by fluorescence cross-correlation spectroscopy.

C. Royer, M. L. Ferguson, J. Savatier, 2010, Biochemistry.

Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer

C. Royer, A. Menon, Savanna Dorsey, 2018, The Journal of Biological Chemistry.

Solution studies of the interactions between the histone core proteins and DNA using fluorescence spectroscope

C. Royer, S. Scarlata, T. Ropp, 1992 .

Role of protein--protein interactions in the regulation of transcription by trp repressor investigated by fluorescence spectroscopy.

C. Royer, T. Fernando, 1992, Biochemistry.

Subunit interactions in hemoglobin probed by fluorescence and high-pressure techniques.

E. Gratton, C. Royer, B. Alpert, 1990, Biochemistry.

Size and sequence and the volume change of protein folding.

D. Barrick, A. Garcia, C. Royer, 2011, Journal of the American Chemical Society.

Oligomerization of the EK18 mutant of the trp repressor of Escherichia coli as observed by NMR spectroscopy.

J. Markley, F. Abildgaard, C. Royer, 1999, Archives of biochemistry and biophysics.

Preferential retrotransposition in aging yeast mother cells is correlated with increased genome instability.

C. Royer, P. Maxwell, Savanna Dorsey, 2015, DNA repair.

Porphyrin dynamics in the heme-pockets of myoglobin and hemoglobin

C. Royer, B. Alpert, 1987 .

Ligands differentially modulate the protein interactions of the human estrogen receptors alpha and beta.

R. Margueron, E. Margeat, C. Royer, 2003, Journal of molecular biology.

Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutants.

J. Beechem, K. Matthews, J. Brochon, 1990, Biophysical journal.

Equilibrium Binding Assays Reveal the Elevated Stoichiometry and Salt Dependence of the Interaction between Full-length Human Sex-determining Region on the Y Chromosome (SRY) and DNA*

E. Margeat, C. Royer, S. Lumbroso, 2002, The Journal of Biological Chemistry.

Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4,5 bisphosphate.

G. Blin, E. Margeat, C. Royer, 2008, Biophysical journal.

Effect of osmolytes on pressure-induced unfolding of proteins: a high-pressure SAXS study.

C. Royer, R. Winter, M. Paulus, 2008, Chemphyschem : a European journal of chemical physics and physical chemistry.

Scanning number and brightness yields absolute protein concentrations in live cells: a crucial parameter controlling functional bio-molecular interaction networks

C. Royer, Christina M Papini, Christina Papini, 2018, Biophysical Reviews.

Testing the correlation between delta A and delta V of protein unfolding using m value mutants of staphylococcal nuclease.

C. Royer, K. Frye, C. S. Perman, 1996, Biochemistry.

Application of pressure to biochemical equilibria: the other thermodynamic variable.

C. Royer, 1995, Methods in enzymology.

Exploring Protein Conformational Landscapes Using High-Pressure NMR.

C. Roumestand, C. Royer, J. Roche, 2019, Methods in enzymology.

Fluorescence approaches to quantifying biomolecular interactions.

C. Royer, S. Scarlata, 2008, Methods in enzymology.

Investigation of the structural determinants of the intrinsic fluorescence emission of the trp repressor using single tryptophan mutants.

C. Royer, 1992, Biophysical journal.

Protein unfolded states populated at high and ambient pressure are similarly compact.

D. Raleigh, R. Gillilan, C. Royer, 2021, Biophysical journal.

Probing the physical determinants of thermal expansion of folded proteins.

Mohammad M. Islam, B. García-Moreno E., C. Royer, 2013, The journal of physical chemistry. B.

Why and How Does Pressure Unfold Proteins?

C. Royer, 2015, Sub-cellular biochemistry.

Improvements in the numerical analysis of thermodynamic data from biomolecular complexes.

C. Royer, 1993, Analytical biochemistry.

Analysis of binding in macromolecular complexes: a generalized numerical approach.

J. Beechem, C. Royer, W. R. Smith, 1990, Analytical biochemistry.

Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics

L. Prézeau, E. Margeat, J. Pin, 2018, Scientific Reports.

High-pressure fluorescence methods for observing subunit dissociation in hemoglobin.

C. Royer, S. Pin, 1994, Methods in enzymology.

Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors.

E. Margeat, C. Royer, A. Boulahtouf, 1999, Molecular endocrinology.

The timing of Start is determined primarily by increased synthesis of the Cln3 activator rather than dilution of the Whi5 inhibitor

M. Tyers, Matthias Heinemann, A. Milias-Argeitis, 2022, Molecular biology of the cell.

NEGATIVE EFFECTIVE PRESSURES IN LIQUID MIXTURES

C. Royer, D. Faux, D. Dunstan, 2003 .

NMR and Computation Reveal a Pressure-Sensitive Folded Conformation of Trp-Cage.

A. Garcia, C. Royer, S. McCallum, 2017, The journal of physical chemistry. B.

A unique secondary-structure switch controls constitutive gene repression by retinoic acid receptor

H. Gronemeyer, A. Lera, C. Royer, 2010, Nature Structural &Molecular Biology.

Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH

B. García-Moreno E., C. Roumestand, C. Royer, 2011, Proteins.

Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure

C. Roumestand, C. Royer, N. Sibille, 2013, Journal of Biomolecular NMR.

Pressure provides new insights into protein folding, dynamics and structure.

C A Royer, D. Foguel, Jerson L. Silva, 2001, Trends in biochemical sciences.

Determination of the volume changes for pressure-induced transitions of apomyoglobin between the native, molten globule, and unfolded states.

C. Royer, G. Vidugiris, Gediminas J. A. Vidugiris, 1998, Biophysical journal.

Probing Protein Folding and Conformational Transitions with Fluorescence

C. Royer, 2006 .

Ligand binding and protein dynamics: a fluorescence depolarization study of aspartate transcarbamylase from Escherichia coli.

P. Tauc, J. Brochon, C. Royer, 1987, Biochemistry.

A high-throughput fluorescence polarization assay specific to the CD4 binding site of HIV-1 glycoproteins based on a fluorescein-labelled CD4 mimic.

F. Stricher, P. Barthe, C. Roumestand, 2005, The Biochemical journal.

Approaches to teaching fluorescence spectroscopy.

C A Royer, C. Royer, C. A. Royer, 1995, Biophysical journal.

Modulators of the structural dynamics of the retinoid X receptor to reveal receptor function

H. Gronemeyer, C. Royer, Efrén Pérez, 2007, Proceedings of the National Academy of Sciences.

Evidence for a molten globule-like transition state in protein folding from determination of activation volumes.

J. Markley, C. Royer, G. Vidugiris, 1995, Biochemistry.

The microprotein Nrs1 rewires the G1/S transcriptional machinery during nitrogen limitation in budding yeast

M. Tyers, S. Moore, J. Coulombe-Huntington, 2022, PLoS biology.

A nitrogen source-regulated microprotein confers an alternative mechanism of G1/S transcriptional activation in budding yeast

M. Tyers, S. Moore, J. Coulombe-Huntington, 2020 .

Histone subunit interactions as investigated by high pressure.

C. Royer, S. Scarlata, T. Ropp, 1989, Biochemistry.

G1/S transcription factors assemble in discrete clusters that increase in number as cells grow

M. Tyers, M. Nollmann, Jing Cheng, 2019 .

G1/S Transcription Factor Copy Number Is a Growth-Dependent Determinant of Cell Cycle Commitment in Yeast.

Mike Tyers, Catherine A Royer, Stephen Notley, 2018, Cell systems.

Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein–protein complexes

Jacqueline Cherfils, Catherine A. Royer, Alain Chavanieu, 2007, Proceedings of the National Academy of Sciences.

Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants

C. Matthews, C. Royer, C. J. Mann, 1993, Protein science : a publication of the Protein Society.

Pressure perturbation calorimetric studies of the solvation properties and the thermal unfolding of proteins in solution--experiments and theoretical interpretation.

N. Smolin, C. Royer, R. Winter, 2006, Physical chemistry chemical physics : PCCP.

Revisiting volume changes in pressure-induced protein unfolding.

C. Royer, 2002, Biochimica et biophysica acta.

The nuclear receptor coactivator PGC-1alpha exhibits modes of interaction with the estrogen receptor distinct from those of SRC-1.

G. Labesse, R. Margueron, C. Royer, 2005, Journal of molecular biology.

Numerical analysis of binding data: advantages, practical aspects, and implications.

C A Royer, J M Beechem, J. Beechem, 1992, Methods in enzymology.

Ligands Differentially Modulate the Protein Interactions of the Human Estrogen Receptors α and β

R. Margueron, E. Margeat, C. Royer, 2003 .

Single-molecule analysis of CD9 dynamics and partitioning reveals multiple modes of interaction in the tetraspanin web

C. le Grimellec, E. Margeat, C. Royer, 2008, The Journal of cell biology.

Fluorescence approaches to study of protein-nucleic acid complexation.

C. Royer, J. Hill, John J. Hill, 1997, Methods in enzymology.

Characterization of the Interaction between Retinoic Acid Receptor/Retinoid X Receptor (RAR/RXR) Heterodimers and Transcriptional Coactivators through Structural and Fluorescence Anisotropy Studies*

H. Gronemeyer, C. Royer, Efrén Pérez, 2005, Journal of Biological Chemistry.

The Molecular Basis for Life in Extreme Environments.

M. Gruebele, B. Barquera, A. Byer, 2021, Annual review of biophysics.

High-Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine-rich Repeat Protein.

D. Barrick, C. Royer, S. McCallum, 2018, Journal of molecular biology.

Temperature and pressure limits of guanosine monophosphate self-assemblies

C. Royer, S. McCallum, R. Winter, 2017, Scientific Reports.

Thermodynamic, kinetic and conformational analysis of proteins diffusion-sorption on a solid surface.

C. Royer, A. Sanfeld, A. Steinchen, 2015, Advances in colloid and interface science.

Recruitment, Assembly, and Molecular Architecture of the SpoIIIE DNA Pump Revealed by Superresolution Microscopy

E. Margeat, C. Clerté, C. Royer, 2013, PLoS biology.

Differential action on coregulator interaction defines inverse retinoid agonists and neutral antagonists.

H. Gronemeyer, M. Lazar, C. Royer, 2009, Chemistry & biology.

Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites

M. Springer, C. Royer, F. Allemand, 2007, Nucleic acids research.

Cavities determine the pressure unfolding of proteins

Jose A. Caro, Julien Roche, Catherine A. Royer, 2012, Proceedings of the National Academy of Sciences.

The Deep Sea Osmolyte Trimethylamine N-Oxide and Macromolecular Crowders Rescue the Antiparallel Conformation of the Human Telomeric G-Quadruplex from Urea and Pressure Stress.

C. Royer, R. Winter, S. Patra, 2018, Chemistry.

Putting the Piezolyte Hypothesis under Pressure.

G. Makhatadze, C. Royer, P. Pandharipande, 2017, Biophysical journal.

Electrostatic forces contribute to interactions between trp repressor dimers.

J. Lee, K. Matthews, J. Carey, 1994, Biophysical journal.

Pressure Denaturation of Proteins

C. Royer, 1999 .

Probing the contribution of internal cavities to the volume change of protein unfolding under pressure

C. Royer, K. Frye, 1998, Protein science : a publication of the Protein Society.

High-pressure effects in molecular biophysics and enzymology

J. Markley, C. Royer, D. Northrop, 1996 .

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

Jianhua Xu, Tilman Rosales, Jianhua Xu, 2007, European Biophysics Journal.

Absolute quantification of gene expression in individual bacterial cells using two-photon fluctuation microscopy.

M. Jules, S. Aymerich, D. le Coq, 2011, Analytical biochemistry.

High pressure activation of the Mrr restriction endonuclease in Escherichia coli involves tetramer dissociation

A. Aertsen, C. Royer, N. Declerck, 2017, Nucleic acids research.

Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA.

Stéphane Aymerich, Catherine A Royer, Carlos Alfonso, 2007, Biophysical journal.

Equilibrium Binding of Estrogen Receptor with DNA Using Fluorescence Anisotropy*

M. S. Ozers, J. Wood, A. Nardulli, 1997, The Journal of Biological Chemistry.

Mechanism of protein binding to spherical polyelectrolyte brushes studied in situ using two-photon excitation fluorescence fluctuation spectroscopy.

E. Gratton, C. Royer, C. Czeslik, 2004, Physical review. E, Statistical, nonlinear, and soft matter physics.

Salt effects on histone subunit interactions as studied by fluorescence spectroscopy.

C A Royer, C. Royer, S. Scarlata, 1989, Biochemistry.

Using Fluorescence to Characterize the Role of Protein Oligomerization in the Regulation of Gene Expression

C. Royer, 2016 .

Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex

C. Royer, N. Declerck, A. van Dorsselaer, 2010, Nucleic acids research.

Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V

P. Bayley, C. Royer, S. Martin, 2003, European Biophysics Journal.

Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity‐creating mutations

A. Garcia, B. García-Moreno E., C. Roumestand, 2013, Proteins.

Fluorescence approaches to the study of protein-DNA interactions

Kathleen Martin, Catherine A. Royer, Veronique Le Tilly, 1992, Photonics West - Lasers and Applications in Science and Engineering.

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

M. Springer, C. Royer, F. Allemand, 2005, Molecular microbiology.

Quantitative characterization of the interaction between purified human estrogen receptor and DNA using fluorescence anisotropy

Catherine A. Royer, Emmanuel Margeat, Mireille Boyer, 2000, Nucleic Acids Res..

The kinetic basis for the stabilization of staphylococcal nuclease by xylose

C. Royer, K. Frye, 1997, Protein science : a publication of the Protein Society.

High-pressure fluorescence applications.

C. Royer, M. Dellarole, 2014, Methods in molecular biology.

Fluorescence spectroscopy.

C. Royer, 1995, Methods in molecular biology.

Macromolecular binding equilibria in the lac repressor system: studies using high-pressure fluorescence spectroscopy.

K. Matthews, C. Royer, A. Chakerian, 1990, Biochemistry.

Probing the relation between protein structure and intrinsic tryptophan fluorescence using superrepressor mutants of thetrp repressor

C. Royer, S. Vangala, G. Vidugiris, 1998, Journal of Fluorescence.

Bacterial expression and characterization of the ligand-binding domain of the vitamin D receptor.

H. DeLuca, C. Royer, D. McCaslin, 1999, Archives of Biochemistry and Biophysics.

Structural Evolution of the Ancient Enzyme, Dissimilatory Sulfite Reductase

G. Montelione, G. Labesse, E. Boyd, 2021, bioRxiv.

Molecular mechanisms of transcriptional control by Rev‐erbα: An energetic foundation for reconciling structure and binding with biological function

G. Ferry, J. Boutin, C. Royer, 2015, Protein science : a publication of the Protein Society.

Protein hydration and volumetric properties

C. Royer, R. Winter, 2011 .

Towards a quantitative understanding of protein hydration and volumetric properties.

C. Royer, R. Winter, B. García-Moreno, 2008, Chemphyschem : a European journal of chemical physics and physical chemistry.

The human estrogen receptor alpha dimer binds a single SRC-1 coactivator molecule with an affinity dictated by agonist structure.

E. Gratton, E. Margeat, C. Royer, 2001, Journal of molecular biology.

Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy.

A. Hinck, J. Markley, S. Loh, 1993, Biochemistry.

Tryptophan replacements in the trp aporepressor from escherichia coli: Probing the equilibrium and kinetic folding models

C. Matthews, C. Royer, C. J. Mann, 1993, Protein science : a publication of the Protein Society.

An oligomeric switch controls the Mrr-induced SOS response in E. coli.

A. Aertsen, G. Labesse, C. Royer, 2020, DNA repair.

Monitoring protein folding through high pressure NMR spectroscopy.

C. Roumestand, C. Royer, Julien Roche, 2017, Progress in nuclear magnetic resonance spectroscopy.

Pressure-jump small-angle x-ray scattering detected kinetics of staphylococcal nuclease folding.

C. Royer, S. Seifert, R. Winter, 2001, Biophysical journal.

Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1.

C. Roumestand, C. Royer, H. Yamada, 2002, Journal of molecular biology.

Pressure-jump studies of the folding/unfolding of trp repressor.

C. Royer, R. Winter, G. Panick, 1999, Journal of molecular biology.

Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy.

C. Royer, R. Winter, G. Rapp, 1998, Journal of molecular biology.

Unique features of the folding landscape of a repeat protein revealed by pressure perturbation.

D. Barrick, C. Royer, R. Winter, 2010, Biophysical journal.

Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure.

K. Matthews, C. Royer, G. Weber, 1986, Biochemistry.

The nature of the transition state ensemble and the mechanisms of protein folding: a review.

C. Royer, 2008, Archives of biochemistry and biophysics.

Interactions in gene expression networks studied by two-photon fluorescence fluctuation spectroscopy.

C. Royer, N. Declerck, 2013, Methods in enzymology.

Characterizing proteins in their cellular environment: Examples of recent advances in quantitative fluorescence microscopy

C. Royer, 2019, Protein science : a publication of the Protein Society.

Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations.

A. Garcia, C. Roumestand, C. Royer, 2012, Biochemistry.

V(i)-value analysis: a pressure-based method for mapping the folding transition state ensemble of proteins.

C. Royer, R. Winter, B. García-Moreno, 2007, Journal of the American Chemical Society.

V67L Mutation Fills an Internal Cavity To Stabilize RecA Mtu Intein.

A. Garcia, C. Royer, Chunyu Wang, 2017, Biochemistry.

Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR).

G. Rivas, S. Aymerich, E. Margeat, 2007, Biochemistry.

Hydration of the folding transition state ensemble of a protein.

C. Royer, B. García-Moreno, D. Isom, 2006, Biochemistry.

The stoichiometry of scaffold complexes in living neurons – DLC2 functions as a dimerization engine for GKAP

G. Labesse, L. Fagni, C. Clerté, 2014, Journal of Cell Science.

The Characterization of Biomolecular Interactions Using Fluorescence Fluctuation Techniques

E. Margeat, C. Royer, H. Boukari, 2007 .

Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy.

A. Garcia, C. Roumestand, C. Royer, 2013, Journal of the American Chemical Society.

Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure

C. Roumestand, C. Royer, N. Sibille, 2014, Journal of biomolecular NMR.

High Pressure CPMG and CEST Reveal That Cavity Position Dictates Distinct Dynamic Disorder in the PP32 Repeat Protein.

R. Gillilan, C. Royer, S. McCallum, 2022, The journal of physical chemistry. B.

High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.

D. Barrick, A. Garcia, C. Roumestand, 2016, Biophysical journal.

Visualization of trp repressor and its complexes with DNA by atomic force microscopy.

C. le Grimellec, E. Margeat, C. Royer, 1998, Biophysical journal.

Assessing the Contribution of Cavity Density to Protein Partial Molar Expansivity by High-Pressure NMR

A. Garcia, C. Roumestand, C. Royer, 2013 .

Effects of chaotropic and kosmotropic cosolvents on the pressure-induced unfolding and denaturation of proteins: an FT-IR study on staphylococcal nuclease.

C. Royer, R. Winter, H. Herberhold, 2004, Biochemistry.

Characterization of the control catabolite protein of gluconeogenic genes repressor by fluorescence cross-correlation spectroscopy and other biophysical approaches.

G. Rivas, S. Aymerich, C. Royer, 2008, Biophysical journal.

Investigating Transcriptional Regulation by Fluorescence Spectroscopy, from Traditional Methods to State‐of‐the‐Art Single‐Molecule Approaches

E. Margeat, C. Royer, N. Declerck, 2008, Annals of the New York Academy of Sciences.

Probing the physical basis for trp repressor-operator recognition.

C A Royer, C. Royer, A. Grillo, 1999, Journal of molecular biology.

Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.

C. Roumestand, C. Royer, Julien Roche, 2015, Sub-cellular biochemistry.

Structural Basis for the Co-activation of Protein Kinase B by T-cell Leukemia-1 (TCL1) Family Proto-oncoproteins*

M. Stern, S. Arold, P. Barthe, 2004, Journal of Biological Chemistry.

Probing the role of water in the tryptophan repressor‐operator complex

C. Royer, A. Grillo, M. Boyer, 1999, Protein science : a publication of the Protein Society.

Ral GTPases promote metastasis by controlling biogenesis and organ colonization of exosomes

N. Paul, F. Delalande, P. Timpson, 2020, bioRxiv.

The basis for the super-repressor phenotypes of the AV77 and EK18 mutants of trp repressor.

C. Royer, A. Grillo, 2000, Journal of molecular biology.

Protocol for production and purification of SARS-CoV-2 3CLpro

G. Montelione, L. Mazzei, T. Acton, 2023, STAR Protocols.

Single-molecule analysis of CD9 dynamics and partitioning reveals multiple modes of interaction in the tetraspanin web

C. le Grimellec, E. Margeat, C. Royer, 2008, The Journal of cell biology.

Understanding fluorescence decay in proteins.

C. Royer, 1993, Biophysical journal.

A high-throughput fluorescence polarization assay specific to the CD4 binding site of HIV-1 glycoproteins based on a fluorescein-labelled CD4 mimic.

F. Stricher, P. Barthe, C. Roumestand, 2005, The Biochemical journal.

Estrogen receptor interactions and dynamics monitored in live cells by fluorescence cross-correlation spectroscopy.

C. Royer, J. Savatier, V. Cavaillès, 2010, Biochemistry.

A discussion of the physical basis for the pressure unfolding of proteins

C. Royer, 2002 .

Size and sequence and the volume change of protein folding.

D. Barrick, A. Garcia, C. Royer, 2011, Journal of the American Chemical Society.

Fluorescence approaches to quantifying biomolecular interactions.

C. Royer, S. Scarlata, 2008, Methods in enzymology.

Monitoring protein folding through high pressure NMR spectroscopy.

C. Roumestand, C. Royer, Julien Roche, 2017, Progress in nuclear magnetic resonance spectroscopy.

Effect of solvent diffusion on the apomyoglobin-water interface

C. Royer, B. Alpert, Charles Twist, 2002 .

Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates.

D. Raleigh, C. Royer, S. McCallum, 2019, Biophysical journal.

Interactions in gene expression networks studied by two-photon fluorescence fluctuation spectroscopy.

C. Royer, N. Declerck, 2013, Methods in enzymology.

Evolutionarily Conserved Pattern of Interactions in a Protein Revealed by Local Thermal Expansion Properties.

P. Barthe, C. Roumestand, C. Royer, 2015, Journal of the American Chemical Society.

Characterization of the folding and unfolding reactions of a small beta-barrel protein of novel topology, the MTCP1 oncogene product P13.

P. Barthe, C. Roumestand, C. Royer, 2001, Journal of molecular biology.

Molecular mechanisms of transcriptional control by Rev‐erbα: An energetic foundation for reconciling structure and binding with biological function

G. Ferry, J. Boutin, C. Royer, 2015, Protein science : a publication of the Protein Society.

Absolute quantification of protein number and dynamics in single cells.

M. Tyers, C. Royer, S. Tollis, 2023, Current opinion in structural biology.