2000 - Fellow of the American Association for the Advancement of Science (AAAS)
Her main research concerns Protein folding, Crystallography, Biochemistry, Biophysics and Cell biology. Her studies in Protein folding integrate themes in fields like Unfolded protein response, Small-angle X-ray scattering, Denaturation and Thermodynamics. Her Nmr data study in the realm of Crystallography connects with subjects such as Hydrostatic pressure.
Her Biophysics research is multidisciplinary, relying on both Tryptophan, Guanine nucleotide exchange factor, Fluorescence and Golgi apparatus. Her Cell biology study combines topics in areas such as Coactivator, Nuclear receptor, Corepressor and Retinoic acid receptor. Her Repressor study which covers Retinoic acid receptor alpha that intersects with Molecular biology.
Catherine A. Royer focuses on Biophysics, Crystallography, Biochemistry, Protein folding and Cell biology. Her research on Biophysics also deals with topics like
As part of one scientific family, Catherine A. Royer deals mainly with the area of Protein folding, narrowing it down to issues related to the Denaturation, and often Small-angle X-ray scattering. Her Cell biology study integrates concerns from other disciplines, such as Promoter, Cell division and Nuclear receptor, Transcription factor. Her Fluorescence anisotropy research focuses on subjects like Dimer, which are linked to Dissociation constant, Dissociation and Stereochemistry.
The scientist’s investigation covers issues in Biophysics, Cell biology, Transcription factor, Protein folding and Small-angle X-ray scattering. Biophysics and Hydrostatic pressure are two areas of study in which Catherine A. Royer engages in interdisciplinary research. Her Cell biology study combines topics from a wide range of disciplines, such as Cerebellum, Promoter and Secretion.
Catherine A. Royer interconnects Budding yeast, Nutrient and Yeast in the investigation of issues within Transcription factor. Her Protein folding research is multidisciplinary, incorporating perspectives in Protein structure, Quantitative fluorescence and Evolutionary biology. Her Small-angle X-ray scattering research includes themes of Cooperativity and Denaturation.
Her primary areas of investigation include Biophysics, Population, Cooperativity, Protein folding and Cell biology. Her biological study spans a wide range of topics, including Dimer, Lipid translocation and Förster resonance energy transfer. Catherine A. Royer combines subjects such as Small-angle X-ray scattering and Mutant with her study of Cooperativity.
Her Protein structure research extends to the thematically linked field of Protein folding. Her Protein structure research incorporates elements of Protein stability, Proteostasis, Denaturation and Sequence. Her Cell biology research integrates issues from Secretion, Cell cycle, Cyclin and Promoter.
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Probing protein folding and conformational transitions with fluorescence.
Catherine A. Royer.
Chemical Reviews (2006)
Revisiting volume changes in pressure-induced protein unfolding
Catherine A. Royer.
Biochimica et Biophysica Acta (2002)
Pressure provides new insights into protein folding, dynamics and structure.
Jerson L Silva;Debora Foguel;Catherine A Royer.
Trends in Biochemical Sciences (2001)
Cavities determine the pressure unfolding of proteins
Julien Roche;Jose A. Caro;Douglas R. Norberto;Philippe Barthe.
Proceedings of the National Academy of Sciences of the United States of America (2012)
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.
Gunda Panick;Ralf Malessa;Roland Winter;Gert Rapp.
Journal of Molecular Biology (1998)
Scavenger receptor class B type I is a key host factor for hepatitis C virus infection required for an entry step closely linked to CD81
Mirjam B. Zeisel;George Koutsoudakis;Eva K. Schnober;Anita Haberstroh;Anita Haberstroh.
Hepatology (2007)
Ligand binding and protein dynamics: a fluorescence depolarization study of aspartate transcarbamylase from Escherichia coli.
C. A. Royer;P. Tauc;G. Herve;J. C. Brochon.
Biochemistry (1987)
Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding
Veronique LeTilly;Catherine A. Royer.
Biochemistry (1993)
Exploring the temperature-pressure phase diagram of staphylococcal nuclease.
Gunda Panick;Gediminas J. A. Vidugiris;Ralf Malessa;G. Rapp.
Biochemistry (1999)
Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants
C. A. Royer;C. J. Mann;C. R. Matthews.
Protein Science (1993)
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