| Year |
Citation |
Score |
| 2020 |
Bourges AC, Lazarev A, Declerck N, Rogers KL, Royer CA. Quantitative High-Resolution Imaging of Live Microbial Cells at High Hydrostatic Pressure. Biophysical Journal. PMID 32402241 DOI: 10.1016/J.Bpj.2020.04.017 |
0.352 |
|
| 2019 |
Royer CA. Characterizing Proteins in their Cellular Environment: Examples of recent advances in quantitative fluorescence microscopy. Protein Science : a Publication of the Protein Society. PMID 31012169 DOI: 10.1002/Pro.3630 |
0.373 |
|
| 2019 |
Zhang S, Zhang Y, Stenzoski NE, Zou J, Peran I, McCallum SA, Raleigh DP, Royer CA. Pressure-Temperature Analysis of the Stability of the CTL9 Domain Reveals Hidden Intermediates. Biophysical Journal. PMID 30685054 DOI: 10.1016/J.Bpj.2019.01.002 |
0.387 |
|
| 2019 |
Roche J, Royer CA, Roumestand C. Exploring Protein Conformational Landscapes Using High-Pressure NMR. Methods in Enzymology. 614: 293-320. PMID 30611428 DOI: 10.1016/Bs.Mie.2018.07.006 |
0.408 |
|
| 2019 |
Zhang S, McCallum S, Royer CA. Probing Pressure Effects on Core Packing of a Repeat Protein using 13C NMR Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.250 |
0.359 |
|
| 2019 |
Kilpatrick K, Gerlich G, Royer CA. Effects of Hydrostatic Pressure on a Putative Piezophilic Homologue of Staphylococcal Nuclease by Fluorescence and High-Pressure NMR Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.1836 |
0.338 |
|
| 2019 |
Royer CA. Cavities in Context: Distinct Consequences of Packing Defects in a Repeat Protein Folding Landscape Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.1607 |
0.318 |
|
| 2018 |
Roche J, Royer CA. Lessons from pressure denaturation of proteins. Journal of the Royal Society, Interface. 15. PMID 30282759 DOI: 10.1098/Rsif.2018.0244 |
0.396 |
|
| 2018 |
Jenkins KA, Fossat MJ, Zhang S, Rai DK, Klein S, Gillilan R, White Z, Gerlich G, McCallum SA, Winter R, Gruner SM, Barrick D, Royer CA. The consequences of cavity creation on the folding landscape of a repeat protein depend upon context. Proceedings of the National Academy of Sciences of the United States of America. PMID 30104366 DOI: 10.1073/Pnas.1807379115 |
0.381 |
|
| 2018 |
Winter RHA, Knop JM, Patra S, Balasubramanian H, Royer C. The Deep Sea Osmolyte TMAO and Macromolecular Crowders Rescue the Antiparallel Conformation of the Human Telomeric G-Quadruplex from Urea and Pressure Stress. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 29993151 DOI: 10.1002/Chem.201802444 |
0.336 |
|
| 2018 |
Møller TC, Hottin J, Clerté C, Zwier JM, Durroux T, Rondard P, Prézeau L, Royer CA, Pin JP, Margeat E, Kniazeff J. Oligomerization of a G protein-coupled receptor in neurons controlled by its structural dynamics. Scientific Reports. 8: 10414. PMID 29991736 DOI: 10.1038/S41598-018-28682-6 |
0.311 |
|
| 2018 |
Andra KK, Dorsey S, Royer C, Menon AK. Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer. The Journal of Biological Chemistry. PMID 29903908 DOI: 10.1074/Jbc.Ra118.003648 |
0.335 |
|
| 2018 |
Zhang Y, Berghaus M, Klein S, Jenkins K, Zhang S, McCallum SA, Morgan J, Winter R, Barrick D, Royer CA. High Pressure NMR and SAXS Reveals How Capping Modulates Folding Cooperativity of the pp32 Leucine Rich Repeat Protein. Journal of Molecular Biology. PMID 29545082 DOI: 10.1016/J.Jmb.2018.03.005 |
0.402 |
|
| 2018 |
Papini C, Royer CA. Scanning number and brightness yields absolute protein concentrations in live cells: a crucial parameter controlling functional bio-molecular interaction networks. Biophysical Reviews. PMID 29383593 DOI: 10.1007/S12551-017-0394-Z |
0.346 |
|
| 2017 |
Roche J, Royer CA, Roumestand C. Monitoring protein folding through high pressure NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy. 102: 15-31. PMID 29157491 DOI: 10.1016/J.Pnmrs.2017.05.003 |
0.395 |
|
| 2017 |
Papini CM, Pandharipande PP, Royer CA, Makhatadze GI. Putting the Piezolyte Hypothesis under Pressure. Biophysical Journal. PMID 28803626 DOI: 10.1016/J.Bpj.2017.07.012 |
0.385 |
|
| 2017 |
Zwarycz AS, Fossat MJ, Akanyeti O, Lin Z, Rosenman DJ, Garcia AE, Royer CA, Mills KV, Wang C. V67L Mutation Fills Internal Cavity to Stabilize RecA Mtu Intein. Biochemistry. PMID 28488863 DOI: 10.1021/Acs.Biochem.6B01264 |
0.359 |
|
| 2017 |
Bourges AC, Torres Montaguth OE, Ghosh A, Tadesse WM, Declerck N, Aertsen A, Royer CA. High pressure activation of the Mrr restriction endonuclease in Escherichia coli involves tetramer dissociation. Nucleic Acids Research. PMID 28369499 DOI: 10.1093/Nar/Gkx192 |
0.35 |
|
| 2017 |
Kitazawa S, Fossat MJ, McCallum SA, Garcia AE, Royer CA. NMR and Computation Reveal a Pressure-Sensitive Folded Conformation of Trp-Cage. The Journal of Physical Chemistry. B. PMID 28107009 DOI: 10.1021/Acs.Jpcb.6B11810 |
0.399 |
|
| 2017 |
Jenkins KA, Fossat M, Dao T, Zhang Y, White Z, Barrick D, Royer CA. Cavities and Cooperativity in the Folding of the Leucine Rich Repeat Protein PP32: A Pressure-Jump Fluorescence and High Pressure NMR Study Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.983 |
0.422 |
|
| 2017 |
Zhang Y, Kitazawa S, Peran I, Stenzoski N, McCallum S, Raleigh D, Royer C. Using High Pressure NMR to Study Folding Cooperativity and Kinetics of Protein L9 Biophysical Journal. 112: 168a. DOI: 10.1016/J.Bpj.2016.11.926 |
0.401 |
|
| 2017 |
Fossat MJ, Kitazawa S, McCallum S, Garcia A, Royer C. A Novel Trp Cage Conformer Revealed by Combining High Pressure NMR and MD Simulations Biophysical Journal. 112: 61a. DOI: 10.1016/J.Bpj.2016.11.366 |
0.366 |
|
| 2017 |
Dorsey SB, Tollis S, Cheng J, Olofsson L, Tyers M, Royer CA. Quantification of Nutrient Dependence of SBF/MBF Transcription Factors Controlling Start in Budding Yeast Biophysical Journal. 112: 279a. DOI: 10.1016/J.Bpj.2016.11.1512 |
0.329 |
|
| 2016 |
Fossat MJ, Dao TP, Jenkins K, Dellarole M, Yang Y, McCallum SA, Garcia AE, Barrick D, Roumestand C, Royer CA. High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape. Biophysical Journal. 111: 2368-2376. PMID 27926838 DOI: 10.1016/J.Bpj.2016.08.027 |
0.398 |
|
| 2016 |
Zhang Y, Kitazawa S, Peran I, Stenzoski N, McCallum SA, Raleigh DP, Royer CA. High Pressure ZZ-Exchange NMR Reveals Key Features of Protein Folding Transition States. Journal of the American Chemical Society. PMID 27781428 DOI: 10.1021/Jacs.6B09887 |
0.397 |
|
| 2016 |
Dorsey SB, Tollis S, Cheng J, Olofsson L, Tyers M, Royer CA. Quantification of the Nutrient Dependence of Factors Controlling Start in Budding Yeast by 2-Photon Scanning Number and Brightness Biophysical Journal. 110: 141a. DOI: 10.1016/J.Bpj.2015.11.804 |
0.32 |
|
| 2016 |
Fossat MJ, Garcia A, Barrick D, Roumestand C, Royer CA. Exploring Folding Cooperativity of a Repeat Protein Folding by 2D-NMR Detected Pressure Perturbation Biophysical Journal. 110: 391a. DOI: 10.1016/J.Bpj.2015.11.2115 |
0.411 |
|
| 2016 |
Bourges A, Ghosh A, Declerck N, Aertsen A, Royer C. High Pressure Induced DNA Damage in Escherichia Coli Involves Pressure-Mediated Dissociation of the Tetrameric Mrr Restriction Endonuclease Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.1694 |
0.347 |
|
| 2015 |
Roche J, Dellarole M, Royer CA, Roumestand C. Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies. Sub-Cellular Biochemistry. 72: 261-78. PMID 26174386 DOI: 10.1007/978-94-017-9918-8_13 |
0.393 |
|
| 2015 |
Royer CA. Why and How Does Pressure Unfold Proteins? Sub-Cellular Biochemistry. 72: 59-71. PMID 26174377 DOI: 10.1007/978-94-017-9918-8_4 |
0.363 |
|
| 2015 |
Dellarole M, Caro JA, Roche J, Fossat M, Barthe P, García-Moreno E B, Royer CA, Roumestand C. Evolutionarily Conserved Pattern of Interactions in a Protein Revealed by Local Thermal Expansion Properties. Journal of the American Chemical Society. 137: 9354-62. PMID 26135981 DOI: 10.1021/Jacs.5B04320 |
0.39 |
|
| 2015 |
Vaissière A, Berger S, Harrus D, Dacquet C, Le Maire A, Boutin JA, Ferry G, Royer CA. Molecular mechanisms of transcriptional control by Rev-erbα: An energetic foundation for reconciling structure and binding with biological function. Protein Science : a Publication of the Protein Society. 24: 1129-46. PMID 25969949 DOI: 10.1002/Pro.2701 |
0.358 |
|
| 2015 |
Sanfeld A, Royer C, Steinchen A. Thermodynamic, kinetic and conformational analysis of proteins diffusion–sorption on a solid surface Advances in Colloid and Interface Science. 222: 639-660. PMID 25433959 DOI: 10.1016/J.Cis.2014.10.006 |
0.305 |
|
| 2015 |
Royer CA. Mechanisms of Pressure Effects in Biology: From Proteins to Live Bacteria Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.1967 |
0.352 |
|
| 2014 |
Moutin E, Compan V, Raynaud F, Clerté C, Bouquier N, Labesse G, Ferguson ML, Fagni L, Royer CA, Perroy J. The stoichiometry of scaffold complexes in living neurons - DLC2 functions as a dimerization engine for GKAP. Journal of Cell Science. 127: 3451-62. PMID 24938595 DOI: 10.1242/Jcs.145748 |
0.631 |
|
| 2014 |
Sibille N, Dellarole M, Royer C, Roumestand C. Measuring residual dipolar couplings at high hydrostatic pressure: robustness of alignment media to high pressure. Journal of Biomolecular Nmr. 58: 9-16. PMID 24292655 DOI: 10.1007/S10858-013-9798-7 |
0.363 |
|
| 2014 |
Dellarole M, Royer CA. High-pressure fluorescence applications. Methods in Molecular Biology (Clifton, N.J.). 1076: 53-74. PMID 24108623 DOI: 10.1007/978-1-62703-649-8_4 |
0.385 |
|
| 2013 |
Roche J, Dellarole M, Caro JA, Norberto DR, Garcia AE, Garcia-Moreno B, Roumestand C, Royer CA. Effect of internal cavities on folding rates and routes revealed by real-time pressure-jump NMR spectroscopy. Journal of the American Chemical Society. 135: 14610-8. PMID 23987660 DOI: 10.1021/Ja406682E |
0.41 |
|
| 2013 |
Guca E, Roumestand C, Vallone B, Royer CA, Dellarole M. Low-cost equilibrium unfolding of heme proteins using 2 μl samples. Analytical Biochemistry. 443: 13-5. PMID 23958270 DOI: 10.1016/J.Ab.2013.08.006 |
0.365 |
|
| 2013 |
Docquier A, Garcia A, Savatier J, Boulahtouf A, Bonnet S, Bellet V, 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. Molecular Endocrinology (Baltimore, Md.). 27: 1429-41. PMID 23885094 DOI: 10.1210/Me.2012-1351 |
0.307 |
|
| 2013 |
Dellarole M, Roumestand C, Royer C, Lecomte JT. Volumetric properties underlying ligand binding in a monomeric hemoglobin: a high-pressure NMR study. Biochimica Et Biophysica Acta. 1834: 1910-22. PMID 23619242 DOI: 10.1016/J.Bbapap.2013.04.016 |
0.379 |
|
| 2013 |
Declerck N, Royer CA. Interactions in gene expression networks studied by two-photon fluorescence fluctuation spectroscopy. Methods in Enzymology. 519: 203-30. PMID 23280112 DOI: 10.1016/B978-0-12-405539-1.00007-5 |
0.404 |
|
| 2013 |
Roche J, Caro JA, Dellarole M, Guca E, Royer CA, GarcÃa-Moreno BE, 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. PMID 23239146 DOI: 10.1002/Prot.24231 |
0.353 |
|
| 2013 |
Moutin E, Clerté C, Compan V, Raynaud F, Ferguson ML, Fagni L, Royer CA, Perroy J. Quantitative Characterization of Reversible GKAP-DLC2 Interactions in Live Neurons by Scanning Number and Brightness Biophysical Journal. 104: 573a-574a. DOI: 10.1016/J.Bpj.2012.11.3185 |
0.611 |
|
| 2013 |
Caro JA, Dellarole M, Schlessman JL, Roumestand C, Royer CA, E BG. Internal Cavities and their Role as Determinants of Pressure Unfolding of Proteins Biophysical Journal. 104: 48. DOI: 10.1016/J.Bpj.2012.11.2214 |
0.407 |
|
| 2013 |
Dellarole M, Roche J, Caro JA, Rouget J, Garcia AE, Garcia-Moreno B, Roumestand C, Royer CA. Assessing the Contribution of Cavity Density to Protein Partial Molar Expansivity by High-Pressure NMR Biophysical Journal. 104: 397a. DOI: 10.1016/J.Bpj.2012.11.2213 |
0.391 |
|
| 2012 |
Roche J, Dellarole M, Caro JA, Guca E, Norberto DR, Yang Y, Garcia AE, Roumestand C, GarcÃa-Moreno B, Royer CA. Remodeling of the folding free energy landscape of staphylococcal nuclease by cavity-creating mutations. Biochemistry. 51: 9535-46. PMID 23116341 DOI: 10.1021/Bi301071Z |
0.348 |
|
| 2012 |
Roche J, Caro JA, Norberto DR, Barthe P, Roumestand C, Schlessman JL, Garcia AE, GarcÃa-Moreno BE, Royer CA. Cavities determine the pressure unfolding of proteins. Proceedings of the National Academy of Sciences of the United States of America. 109: 6945-50. PMID 22496593 DOI: 10.1073/Pnas.1200915109 |
0.404 |
|
| 2012 |
Ferguson ML, Le Coq D, Jules M, Aymerich S, Radulescu O, Declerck N, Royer CA. Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states. Proceedings of the National Academy of Sciences of the United States of America. 109: 155-60. PMID 22190493 DOI: 10.1073/Pnas.1110541108 |
0.619 |
|
| 2012 |
Roche J, Caro JA, Norberto D, Barthe P, Roumestand C, Schlessman JL, Garcia AE, Garcia-Moreno E. B, Royer CA. Cavities in the Hydrophobic Core Govern Pressure Unfolding of Proteins Biophysical Journal. 102: 218a. DOI: 10.1016/J.Bpj.2011.11.1194 |
0.41 |
|
| 2011 |
Ferguson ML, Le Coq D, Jules M, Aymerich S, Declerck N, Royer CA. Absolute quantification of gene expression in individual bacterial cells using two-photon fluctuation microscopy. Analytical Biochemistry. 419: 250-9. PMID 21907700 DOI: 10.1016/J.Ab.2011.08.017 |
0.639 |
|
| 2011 |
Rouget JB, Aksel T, Roche J, Saldana JL, Garcia AE, Barrick D, Royer CA. Size and sequence and the volume change of protein folding. Journal of the American Chemical Society. 133: 6020-7. PMID 21446709 DOI: 10.1021/Ja200228W |
0.41 |
|
| 2011 |
Kitahara R, Hata K, Maeno A, Akasaka K, Chimenti MS, Garcia-Moreno E B, Schroer MA, Jeworrek C, Tolan M, Winter R, Roche J, Roumestand C, Montet de Guillen K, Royer CA. Structural plasticity of staphylococcal nuclease probed by perturbation with pressure and pH. Proteins. 79: 1293-305. PMID 21254234 DOI: 10.1002/Prot.22966 |
0.376 |
|
| 2011 |
Royer C, Winter R. Protein hydration and volumetric properties Current Opinion in Colloid and Interface Science. 16: 568-571. DOI: 10.1016/J.Cocis.2011.04.008 |
0.368 |
|
| 2011 |
Caro JA, Roche J, Rouget J, Schlessman J, García AE, Royer CA, García-Moreno B. Role of Internal Cavities as Determinants of Pressure Unfolding of Proteins Biophysical Journal. 100: 398a. DOI: 10.1016/J.Bpj.2010.12.2363 |
0.411 |
|
| 2011 |
Ferguson ML, Le Coq D, Jules M, Chun B, Aymerich S, Radulescu O, Declerck N, Royer C. Two Types of Transcriptional Repression in Living Cells of Bacillus Subtilis Characterized by Number and Brightness Analysis Biophysical Journal. 100: 175a-176a. DOI: 10.1016/J.Bpj.2010.12.1179 |
0.634 |
|
| 2010 |
Schroer MA, Paulus M, Jeworrek C, Krywka C, Schmacke S, Zhai Y, Wieland DC, Sahle CJ, Chimenti M, Royer CA, Garcia-Moreno B, Tolan M, Winter R. High-pressure SAXS study of folded and unfolded ensembles of proteins. Biophysical Journal. 99: 3430-7. PMID 21081092 DOI: 10.1016/J.Bpj.2010.09.046 |
0.396 |
|
| 2010 |
Rouget JB, Schroer MA, Jeworrek C, Pühse M, Saldana JL, Bessin Y, Tolan M, Barrick D, Winter R, Royer CA. Unique features of the folding landscape of a repeat protein revealed by pressure perturbation. Biophysical Journal. 98: 2712-21. PMID 20513416 DOI: 10.1016/J.Bpj.2010.02.044 |
0.403 |
|
| 2010 |
Chaix D, Ferguson ML, Atmanene C, Van Dorsselaer A, Sanglier-Cianférani S, Royer CA, Declerck N. Physical basis of the inducer-dependent cooperativity of the Central glycolytic genes Repressor/DNA complex. Nucleic Acids Research. 38: 5944-57. PMID 20462860 DOI: 10.1093/Nar/Gkq334 |
0.613 |
|
| 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: 772-81. PMID 20039662 DOI: 10.1021/Bi9013006 |
0.648 |
|
| 2010 |
Ferguson ML, Jules M, Le Coq D, Aymerich S, Declerck N, Royer CA. Counting Up the Molecules in Live Bacillus Subtilis by Fluctuation Imaging and Analysis: An in Vivo Study of Transcriptional Regulation Biophysical Journal. 98: 750a. DOI: 10.1016/J.Bpj.2009.12.4111 |
0.617 |
|
| 2009 |
Rouget J, Aksel T, Barrick D, Royer CA. Volume changes in protein folding: A Modular Approach Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.3080 |
0.374 |
|
| 2009 |
Ferguson ML, Clerté C, Margeat E, Declerck N, Royer CA. Investigating The Structural Dynamics Of The Lict Transcriptional Antiterminator And Its RNA Target By Single Molecule FRET Biophysical Journal. 96: 56a. DOI: 10.1016/J.Bpj.2008.12.186 |
0.623 |
|
| 2009 |
Ferguson ML, Declerck N, Royer CA. Fluorescence Correlation Spectroscopy In Live Bacillus Subtilis Cells: An In Vivo Study Of Transcriptional Regulation Biophysical Journal. 96: 26a. DOI: 10.1016/J.Bpj.2008.12.022 |
0.639 |
|
| 2008 |
Royer CA, Scarlata SF. Fluorescence approaches to quantifying biomolecular interactions. Methods in Enzymology. 450: 79-106. PMID 19152857 DOI: 10.1016/S0076-6879(08)03405-8 |
0.366 |
|
| 2008 |
Krywka C, Sternemann C, Paulus M, Tolan M, Royer C, Winter R. Effect of Osmolytes on Pressure‐Induced Unfolding of Proteins: A High‐Pressure SAXS Study Chemphyschem. 9: 2809-2815. PMID 18924198 DOI: 10.1002/Cphc.200800522 |
0.386 |
|
| 2008 |
Mitra L, Rouget JB, Garcia-Moreno B, Royer CA, Winter R. Towards a quantitative understanding of protein hydration and volumetric properties. Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry. 9: 2715-21. PMID 18814170 DOI: 10.1002/Cphc.200800405 |
0.347 |
|
| 2008 |
Zorrilla S, Ortega A, Chaix D, Alfonso C, Rivas G, Aymerich S, Lillo MP, Declerck N, Royer CA. Characterization of the control catabolite protein of gluconeogenic genes repressor by fluorescence cross-correlation spectroscopy and other biophysical approaches. Biophysical Journal. 95: 4403-15. PMID 18658229 DOI: 10.1529/Biophysj.108.135863 |
0.408 |
|
| 2008 |
Zorrilla S, Lillo MP, Chaix D, Margeat E, Royer CA, Declerck N. Investigating transcriptional regulation by fluorescence spectroscopy, from traditional methods to state-of-the-art single-molecule approaches. Annals of the New York Academy of Sciences. 1130: 44-51. PMID 18596330 DOI: 10.1196/Annals.1430.023 |
0.399 |
|
| 2008 |
Royer CA. The nature of the transition state ensemble and the mechanisms of protein folding: a review. Archives of Biochemistry and Biophysics. 469: 34-45. PMID 17923105 DOI: 10.1016/J.Abb.2007.08.022 |
0.31 |
|
| 2008 |
Blin G, Margeat E, Carvalho K, Royer CA, Roy C, Picart C. Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4,5 bisphosphate. Biophysical Journal. 94: 1021-33. PMID 17827228 DOI: 10.1529/Biophysj.107.110213 |
0.354 |
|
| 2008 |
Mitra L, Rouget J, Garcia-Moreno B, Royer CA, Winter R, Oleinikova A, Winter R, Holzmann J, Ludwig R, Geiger A, Paschek D, Riemenschneider J, Rüppert A, Pühse M, Perez-Goicochea A, ... ... Royer C, et al. Cover Picture: Towards a Quantitative Understanding of Protein Hydration and Volumetric Properties / Intrinsic Volumetric Properties of Trialanine Isomers in Aqueous Solution / Temperature and Concentration Effects on the Solvophobic Solvation of Methane Chemphyschem. 9: 2633-2633. DOI: 10.1002/Cphc.200890072 |
0.3 |
|
| 2007 |
Zorrilla S, Chaix D, Ortega A, Alfonso C, Doan T, Margeat E, Rivas G, Aymerich S, Declerck N, Royer CA. Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR). Biochemistry. 46: 14996-5008. PMID 18052209 DOI: 10.1021/Bi701805E |
0.352 |
|
| 2007 |
Mitra L, Hata K, Kono R, Maeno A, Isom D, Rouget JB, Winter R, Akasaka K, García-Moreno B, Royer CA. V(i)-value analysis: a pressure-based method for mapping the folding transition state ensemble of proteins. Journal of the American Chemical Society. 129: 14108-9. PMID 17960902 DOI: 10.1021/Ja073576Y |
0.375 |
|
| 2007 |
Nahoum V, Pérez E, Germain P, Rodríguez-Barrios F, Manzo F, Kammerer S, Lemaire G, Hirsch O, Royer CA, Gronemeyer H, de Lera AR, Bourguet W. Modulators of the structural dynamics of the retinoid X receptor to reveal receptor function. Proceedings of the National Academy of Sciences of the United States of America. 104: 17323-8. PMID 17947383 DOI: 10.1073/Pnas.0705356104 |
0.307 |
|
| 2007 |
Viaud J, Zeghouf M, Barelli H, Zeeh JC, Padilla A, Guibert B, Chardin P, Royer CA, Cherfils J, Chavanieu A. Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein-protein complexes Proceedings of the National Academy of Sciences of the United States of America. 104: 10370-10375. PMID 17563369 DOI: 10.1073/Pnas.0700773104 |
0.366 |
|
| 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. Biophysical Journal. 92: 3215-27. PMID 17293407 DOI: 10.1529/Biophysj.106.095109 |
0.353 |
|
| 2007 |
Rosales T, Georget V, Malide D, Smirnov A, Xu J, Combs C, Knutson JR, Nicolas JC, Royer CA. 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. European Biophysics Journal : Ebj. 36: 153-61. PMID 17021805 DOI: 10.1007/S00249-006-0095-1 |
0.355 |
|
| 2006 |
Royer CA. Probing protein folding and conformational transitions with fluorescence. Chemical Reviews. 106: 1769-84. PMID 16683754 DOI: 10.1021/Cr0404390 |
0.368 |
|
| 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 Physical Chemistry Chemical Physics. 8: 1249-1265. PMID 16633605 DOI: 10.1039/B516608J |
0.407 |
|
| 2006 |
Brun L, Isom DG, Velu P, GarcÃa-Moreno B, Royer CA. Hydration of the folding transition state ensemble of a protein. Biochemistry. 45: 3473-80. PMID 16533028 DOI: 10.1021/Bi052638Z |
0.408 |
|
| 2005 |
Royer CA. Insights into the role of hydration in protein structure and stability obtained through hydrostatic pressure studies Brazilian Journal of Medical and Biological Research. 38: 1167-1173. PMID 16082456 DOI: 10.1590/S0100-879X2005000800003 |
0.396 |
|
| 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. Molecular Microbiology. 56: 1441-56. PMID 15916597 DOI: 10.1111/J.1365-2958.2005.04644.X |
0.305 |
|
| 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. The Biochemical Journal. 390: 29-39. PMID 15836438 DOI: 10.1042/Bj20041953 |
0.305 |
|
| 2005 |
Bourdoncle A, Labesse G, Margueron R, Castet A, Cavaillès V, Royer CA. The nuclear receptor coactivator PGC-1alpha exhibits modes of interaction with the estrogen receptor distinct from those of SRC-1. Journal of Molecular Biology. 347: 921-34. PMID 15784253 DOI: 10.1016/J.Jmb.2005.01.048 |
0.336 |
|
| 2005 |
Pogenberg V, Guichou JF, Vivat-Hannah V, Kammerer S, Pérez 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. The Journal of Biological Chemistry. 280: 1625-33. PMID 15528208 DOI: 10.1074/Jbc.M409302200 |
0.333 |
|
| 2004 |
Auguin D, Barthe P, Royer C, Stern MH, Noguchi M, Arold ST, Roumestand C. Structural basis for the co-activation of protein kinase B by T-cell leukemia-1 (TCL1) family proto-oncoproteins. The Journal of Biological Chemistry. 279: 35890-902. PMID 15169787 DOI: 10.1074/Jbc.M400364200 |
0.352 |
|
| 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. PMID 15035605 DOI: 10.1021/Bi036106Z |
0.372 |
|
| 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 Physical Review E - Statistical, Nonlinear, and Soft Matter Physics. 69: 021401-1-021401-9. DOI: 10.1103/Physreve.69.021401 |
0.374 |
|
| 2004 |
Ravindra R, Royer C, Winter R. Pressure perturbation calorimetic studies of the solvation properties and the thermal unfolding of staphylococcal nuclease Physical Chemistry Chemical Physics. 6: 1952-1961. DOI: 10.1039/B314172A |
0.397 |
|
| 2003 |
Poujol N, Margeat E, Baud S, Royer CA. RAR antagonists diminish the level of DNA binding by the RAR/RXR heterodimer. Biochemistry. 42: 4918-25. PMID 12718533 DOI: 10.1021/Bi027056L |
0.333 |
|
| 2003 |
Czeslik C, Royer C, Hazlett T, Mantulin W. Reorientational Dynamics of Enzymes Adsorbed on Quartz: A Temperature-Dependent Time-Resolved TIRF Anisotropy Study Biophysical Journal. 84: 2533-2541. PMID 12668461 DOI: 10.1016/S0006-3495(03)75058-9 |
0.376 |
|
| 2003 |
Margeat E, Bourdoncle A, Margueron R, Poujol N, Cavaillès V, Royer C. Ligands Differentially Modulate the Protein Interactions of the Human Estrogen Receptors α and β Journal of Molecular Biology. 326: 77-92. PMID 12547192 DOI: 10.1016/S0022-2836(02)01355-4 |
0.357 |
|
| 2003 |
Van Uden NWA, Hubel H, Faux DA, Dunstan DJ, Royer CA. Negative effective pressures in liquid mixtures High Pressure Research. 23: 205-209. DOI: 10.1080/0895795032000102351 |
0.321 |
|
| 2002 |
Maleki SJ, Royer CA, Hurlburt BK. Analysis of the DNA-binding properties of MyoD, myogenin, and E12 by fluorescence anisotropy. Biochemistry. 41: 10888-94. PMID 12196028 DOI: 10.1021/Bi025528Q |
0.358 |
|
| 2002 |
Twist C, Royer C, Alpert B. Effect of solvent diffusion on the apomyoglobin-water interface. Biochemistry. 41: 10343-50. PMID 12162750 DOI: 10.1021/Bi012210+ |
0.352 |
|
| 2002 |
Kitahara R, Royer C, Yamada H, Boyer M, Saldana JL, Akasaka K, Roumestand C. Equilibrium and pressure-jump relaxation studies of the conformational transitions of P13MTCP1. Journal of Molecular Biology. 320: 609-28. PMID 12096913 DOI: 10.1016/S0022-2836(02)00516-8 |
0.394 |
|
| 2002 |
Royer CA. Revisiting volume changes in pressure-induced protein unfolding. Biochimica Et Biophysica Acta. 1595: 201-9. PMID 11983396 DOI: 10.1016/S0167-4838(01)00344-2 |
0.381 |
|
| 2002 |
Baud S, Margeat E, Lumbroso S, Paris F, Sultan C, Royer C, Poujol N. 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. The Journal of Biological Chemistry. 277: 18404-10. PMID 11877434 DOI: 10.1074/Jbc.M112366200 |
0.377 |
|
| 2002 |
Declerck N, Dutartre H, Receveur V, Dubois V, Royer C, Aymerich S, van Tilbeurgh H. Dimer stabilization upon activation of the transcriptional antiterminator LicT. Journal of Molecular Biology. 314: 671-81. PMID 11733988 DOI: 10.1006/Jmbi.2001.5185 |
0.341 |
|
| 2002 |
Czeslik C, Jackler G, Royer C. Driving forces for the adsorption of enzymes at the water/silica interface studied by total internal reflection fluorescence spectroscopy and optical reflectometry Spectroscopy. 16: 139-145. DOI: 10.1155/2002/473035 |
0.319 |
|
| 2002 |
Royer CA. A discussion of the physical basis for the pressure unfolding of proteins Progress in Biotechnology. 19: 17-25. DOI: 10.1016/S0921-0423(02)80074-0 |
0.387 |
|
| 2001 |
Silva JL, Foguel D, Royer CA. Pressure provides new insights into protein folding, dynamics and structure Trends in Biochemical Sciences. 26: 612-618. PMID 11590014 DOI: 10.1016/S0968-0004(01)01949-1 |
0.393 |
|
| 2001 |
Roumestand C, Boyer M, Guignard L, Barthe P, Royer CA. Characterization of the folding and unfolding reactions of a small beta-barrel protein of novel topology, the MTCP1 oncogene product P13. Journal of Molecular Biology. 312: 247-59. PMID 11545600 DOI: 10.1006/Jmbi.2001.4928 |
0.381 |
|
| 2001 |
Seemann H, Winter R, Royer CA. Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of Staphylococcal nuclease. Journal of Molecular Biology. 307: 1091-1102. PMID 11286558 DOI: 10.1006/Jmbi.2001.4517 |
0.35 |
|
| 2001 |
Woenckhaus J, Köhling R, Thiyagarajan P, Littrell KC, Seifert S, Royer CA, Winter R. Pressure-jump small-angle x-ray scattering detected kinetics of staphylococcal nuclease folding. Biophysical Journal. 80: 1518-23. PMID 11222312 DOI: 10.1016/S0006-3495(01)76124-3 |
0.359 |
|
| 2001 |
Margeat E, Poujol N, Boulahtouf A, Chen Y, Müller JD, Gratton E, Cavailles V, Royer CA. The human estrogen receptor alpha dimer binds a single SRC-1 coactivator molecule with an affinity dictated by agonist structure. Journal of Molecular Biology. 306: 433-42. PMID 11178903 DOI: 10.1006/Jmbi.2000.4418 |
0.397 |
|
| 2000 |
Boyer M, Poujol N, Margeat E, Royer CA. Quantitative characterization of the interaction between purified human estrogen receptor α and DNA using fluorescence anisotropy Nucleic Acids Research. 28: 2494-2502. PMID 10871398 DOI: 10.1093/Nar/28.13.2494 |
0.362 |
|
| 2000 |
Grillo AO, Royer CA. The basis for the super-repressor phenotypes of the AV77 and EK18 mutants of trp repressor. Journal of Molecular Biology. 295: 17-28. PMID 10623505 DOI: 10.1006/Jmbi.1999.3317 |
0.336 |
|
| 2000 |
Royer CA. Protein folding and stability: What can we learn from high pressure? High Pressure Research. 19: 213-222. DOI: 10.1080/08957950008202557 |
0.386 |
|
| 1999 |
Thénot S, Bonnet S, Boulahtouf A, Margeat E, Royer CA, Borgna J, Cavaillès V. Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors. Molecular Endocrinology. 13: 2137-2150. PMID 10598587 DOI: 10.1210/Mend.13.12.0387 |
0.334 |
|
| 1999 |
Chae YK, Abildgaard F, Royer CA, Markley JL. Oligomerization of the EK18 mutant of the trp repressor of Escherichia coli as observed by NMR spectroscopy. Archives of Biochemistry and Biophysics. 371: 35-40. PMID 10525287 DOI: 10.1006/Abbi.1999.1394 |
0.369 |
|
| 1999 |
Brown MP, Grillo AO, Boyer M, Royer CA. Probing the role of water in the tryptophan repressor-operator complex Protein Science. 8: 1276-1285. PMID 10386877 DOI: 10.1110/Ps.8.6.1276 |
0.35 |
|
| 1999 |
Desai G, Panick G, Zein M, Winter R, Royer CA. Pressure-jump studies of the folding/unfolding of trp repressor Journal of Molecular Biology. 288: 461-475. PMID 10329154 DOI: 10.1006/Jmbi.1999.2692 |
0.41 |
|
| 1999 |
Panick G, Vidugiris GJA, Malessa R, Rapp G, Winter R, Royer CA. Exploring the temperature-pressure phase diagram of staphylococcal nuclease. Biochemistry. 38: 4157-4164. PMID 10194332 DOI: 10.1021/Bi982608E |
0.363 |
|
| 1999 |
Grillo AO, Brown MP, Royer CA. Probing the physical basis for trp repressor-operator recognition. Journal of Molecular Biology. 287: 539-54. PMID 10092458 DOI: 10.1006/Jmbi.1999.2625 |
0.367 |
|
| 1999 |
Strugnell SA, Hill JJ, McCaslin DR, Wiefling BA, Royer CA, DeLuca HF. Bacterial expression and characterization of the ligand-binding domain of the vitamin D receptor. Archives of Biochemistry and Biophysics. 364: 42-52. PMID 10087163 DOI: 10.1006/Abbi.1999.9999 |
0.371 |
|
| 1998 |
Margeat E, Le Grimellec C, Royer CA. Visualization of trp repressor and its complexes with DNA by atomic force microscopy. Biophysical Journal. 75: 2712-20. PMID 9826594 DOI: 10.1016/S0006-3495(98)77715-X |
0.355 |
|
| 1998 |
Frye KJ, Royer CA. Probing the contribution of internal cavities to the volume change of protein unfolding under pressure Protein Science. 7: 2217-2222. PMID 9792110 DOI: 10.1002/Pro.5560071020 |
0.347 |
|
| 1998 |
Vidugiris GJA, Royer CA. Determination of the Volume Changes for Pressure-Induced Transitions of Apomyoglobin between the Native, Molten Globule, and Unfolded States Biophysical Journal. 75: 463-470. PMID 9649407 DOI: 10.1016/S0006-3495(98)77534-4 |
0.358 |
|
| 1998 |
Panick G, Malessa R, Winter R, Rapp G, Frye KJ, Royer CA. 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. Journal of Molecular Biology. 275: 389-402. PMID 9466917 DOI: 10.1006/Jmbi.1997.1454 |
0.374 |
|
| 1998 |
Vangala S, Vidugiris GAJ, Royer CA. Probing the relation between protein structure and intrinsic tryptophan fluorescence using superrepressor mutants of thetrp repressor Journal of Fluorescence. 8: 1-11. DOI: 10.1007/Bf02758230 |
0.401 |
|
| 1997 |
Ozers MS, Hill JJ, Ervin K, Wood JR, Nardulli AM, Royer CA, Gorski J. Equilibrium binding of estrogen receptor with DNA using fluorescence anisotropy Journal of Biological Chemistry. 272: 30405-30411. PMID 9374531 DOI: 10.1074/Jbc.272.48.30405 |
0.307 |
|
| 1997 |
Reedstrom RJ, Brown MP, Grillo A, Roen D, Royer CA. Affinity and specificity of trp repressor-DNA interactions studied with fluorescent oligonucleotides. Journal of Molecular Biology. 273: 572-85. PMID 9356247 DOI: 10.1006/Jmbi.1997.1333 |
0.361 |
|
| 1997 |
Maleki SJ, Royer CA, Hurlburt BK. MyoD-E12 heterodimers and MyoD-MyoD homodimers are equally stable Biochemistry. 36: 6762-6767. PMID 9184158 DOI: 10.1021/Bi970262M |
0.34 |
|
| 1997 |
Hill JJ, Royer CA. Fluorescence approaches to study of protein-nucleic acid complexation. Methods in Enzymology. 278: 390-416. PMID 9170324 DOI: 10.1016/S0076-6879(97)78021-2 |
0.334 |
|
| 1997 |
Frye KJ, Royer CA. The kinetic basis for the stabilization of staphylococcal nuclease by xylose Protein Science. 6: 789-793. PMID 9098888 DOI: 10.1002/Pro.5560060405 |
0.348 |
|
| 1997 |
Brown MP, Royer C. Fluorescence spectroscopy as a tool to investigate protein interactions Current Opinion in Biotechnology. 8: 45-49. DOI: 10.1016/S0958-1669(97)80156-5 |
0.39 |
|
| 1996 |
Reedstrom RJ, Martin KS, Vangala S, Mahoney S, Wilker EW, Royer CA. Characterization of charge change super-repressor mutants of trp repressor: effects on oligomerization conformation, ligation and stability. Journal of Molecular Biology. 264: 32-45. PMID 8950265 DOI: 10.1006/Jmbi.1996.0621 |
0.396 |
|
| 1996 |
Frye KJ, Perman CS, Royer CA. Testing the correlation between delta A and delta V of protein unfolding using m value mutants of staphylococcal nuclease. Biochemistry. 35: 10234-10239. PMID 8756489 DOI: 10.1021/Bi960693P |
0.373 |
|
| 1996 |
Sire O, Alpert B, Royer CA. Probing pH and pressure effects on the apomyoglobin heme pocket with the 2′-(N,N-dimethylamino)-6-naphthoyl-4-trans-cyclohexanoic acid fluorophore Biophysical Journal. 70: 2903-2914. PMID 8744328 DOI: 10.1016/S0006-3495(96)79860-0 |
0.303 |
|
| 1996 |
Vidugiris GJ, Truckses DM, Markley JL, Royer CA. High-pressure denaturation of staphylococcal nuclease proline-to-glycine substitution mutants. Biochemistry. 35: 3857-64. PMID 8620010 DOI: 10.1021/Bi952012G |
0.38 |
|
| 1995 |
Royer CA. [16] Application of pressure to biochemical equilibria: The other thermodynamic variable Methods in Enzymology. 259: 357-377. PMID 8538462 DOI: 10.1016/0076-6879(95)59052-8 |
0.327 |
|
| 1995 |
Vidugiris GJ, Markley JL, Royer CA. Evidence for a molten globule-like transition state in protein folding from determination of activation volumes. Biochemistry. 34: 4909-12. PMID 7711012 DOI: 10.1021/Bi00015A001 |
0.344 |
|
| 1995 |
Reedstrom RJ, Royer CA. Evidence for coupling of folding and function in trp repressor: physical characterization of the superrepressor mutant AV77. Journal of Molecular Biology. 253: 266-76. PMID 7563088 DOI: 10.1006/Jmbi.1995.0551 |
0.407 |
|
| 1994 |
Pin S, Royer CA. High-pressure fluorescence methods for observing subunit dissociation in hemoglobin. Methods in Enzymology. 232: 42-55. PMID 8057872 DOI: 10.1016/0076-6879(94)32042-X |
0.396 |
|
| 1994 |
Martin KS, Royer CA, Howard KP, Carey J, Liu YC, Matthews K, Heyduk E, Lee JC. Electrostatic forces contribute to interactions between trp repressor dimers. Biophysical Journal. 66: 1167-73. PMID 8038388 DOI: 10.1016/S0006-3495(94)80898-7 |
0.364 |
|
| 1993 |
Royer CA, Hinck AP, Loh SN, Prehoda KE, Peng X, Jonas J, Markley JL. Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry. 32: 5222-32. PMID 8494899 DOI: 10.1021/Bi00070A034 |
0.369 |
|
| 1993 |
Royer CA. Improvements in the numerical analysis of thermodynamic data from biomolecular complexes. Analytical Biochemistry. 210: 91-97. PMID 8489028 DOI: 10.1006/Abio.1993.1155 |
0.346 |
|
| 1993 |
Royer CA. Understanding fluorescence decay in proteins Biophysical Journal. 65: 9-10. PMID 8369464 DOI: 10.1016/S0006-3495(93)81024-5 |
0.356 |
|
| 1993 |
LeTilly V, Royer CA. Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding Biochemistry. 32: 7753-7758. PMID 8347584 DOI: 10.1021/Bi00081A021 |
0.41 |
|
| 1993 |
Mann CJ, Royer CA, Matthews CR. Tryptophan replacements in the trp aporepressor from Escherichia coli: probing the equilibrium and kinetic folding models. Protein Science : a Publication of the Protein Society. 2: 1853-61. PMID 8268796 DOI: 10.1002/Pro.5560021107 |
0.359 |
|
| 1993 |
Royer CA, Mann CJ, Matthews CR. Resolution of the fluorescence equilibrium unfolding profile of trp aporepressor using single tryptophan mutants. Protein Science : a Publication of the Protein Society. 2: 1844-52. PMID 8268795 DOI: 10.1002/Pro.5560021106 |
0.378 |
|
| 1993 |
Royer CA, Ropp T, Scarlata SF. Solution studies of the interactions between the histone core proteins and DNA using fluorescence spectroscopy (biophys. chem. 43 (1992) 197–211) Biophysical Chemistry. 46: 295-296. DOI: 10.1016/0301-4622(93)80024-D |
0.335 |
|
| 1992 |
Fernando T, Royer CA. Unfolding of trp repressor studied using Fluorescence spectroscopic techniques Biochemistry. 31: 6683-6691. PMID 1637807 DOI: 10.1021/Bi00144A007 |
0.383 |
|
| 1992 |
Fernando T, Royer C. Role of protein-protein interactions in the regulation of transcription by trp repressor investigated by fluorescence spectroscopy Biochemistry®. 31: 3429-3441. PMID 1554725 DOI: 10.1021/Bi00128A018 |
0.436 |
|
| 1992 |
Royer CA. Investigation of the structural determinants of the intrinsic fluorescence emission of the trp repressor using single tryptophan mutants Biophysical Journal. 63: 741-750. PMID 1420911 DOI: 10.1016/S0006-3495(92)81658-2 |
0.304 |
|
| 1992 |
Royer CA, Ropp T, Scarlata SF. Solution studies of the interactions between the histone core proteins and DNA using fluorescence spectroscopy. Biophysical Chemistry. 43: 197-211. PMID 1307864 DOI: 10.1016/0301-4622(92)80034-3 |
0.319 |
|
| 1990 |
Pin S, Royer CA, Gratton E, Alpert B, Weber G. Subunit interactions in hemoglobin probed by fluorescence and high-pressure techniques. Biochemistry. 29: 9194-202. PMID 2271588 DOI: 10.1021/Bi00491A013 |
0.382 |
|
| 1990 |
Royer CA, Gardner JA, Beechem JM, Brochon JC, Matthews KS. Resolution of the fluorescence decay of the two tryptophan residues of lac repressor using single tryptophan mutants. Biophysical Journal. 58: 363-78. PMID 2207244 DOI: 10.1016/S0006-3495(90)82383-3 |
0.395 |
|
| 1990 |
Royer CA, Chakerian AE, Matthews KS. Macromolecular binding equilibria in the lac repressor system: studies using high-pressure fluorescence spectroscopy. Biochemistry. 29: 4959-66. PMID 2194564 DOI: 10.1021/Bi00472A028 |
0.405 |
|
| 1990 |
Royer CA, Smith WR, Beechem JM. Analysis of binding in macromolecular complexes: A generalized numerical approach Analytical Biochemistry. 191: 287-294. PMID 2085174 DOI: 10.1016/0003-2697(90)90221-T |
0.334 |
|
| 1989 |
Scarlata SF, Ropp T, Royer CA. Histone subunit interactions as investigated by high pressure. Biochemistry. 28: 6637-41. PMID 2790018 DOI: 10.1021/Bi00442A016 |
0.339 |
|
| 1989 |
Royer CA, Rusch RM, Scarlata SF. Salt effects on histone subunit interactions as studied by fluorescence spectroscopy. Biochemistry. 28: 6631-7. PMID 2790017 DOI: 10.1021/Bi00442A015 |
0.309 |
|
| 1986 |
Royer CA, Weber G, Daly TJ, Matthews KS. Dissociation of the lactose repressor protein tetramer using high hydrostatic pressure. Biochemistry. 25: 8308-15. PMID 3545291 DOI: 10.1021/Bi00373A027 |
0.388 |
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