| Year |
Citation |
Score |
| 2023 |
Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. Nucleic Acids Research. PMID 38153183 DOI: 10.1093/nar/gkad1215 |
0.818 |
|
| 2023 |
Mooren OL, Stuchell-Brereton MD, McConnell P, Yan C, Wilkerson EM, Goldfarb D, Cooper JA, Sept D, Soranno A. Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein. Journal of Molecular Biology. 168342. PMID 37924863 DOI: 10.1016/j.jmb.2023.168342 |
0.808 |
|
| 2023 |
Mooren OL, Stuchell-Brereton MD, McConnell P, Yan C, Wilkerson EM, Goldfarb D, Cooper JA, Sept D, Soranno A. Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein. Biorxiv : the Preprint Server For Biology. PMID 37645735 DOI: 10.1101/2023.08.16.553570 |
0.806 |
|
| 2023 |
Alston JJ, Soranno A, Holehouse AS. Conserved molecular recognition by an intrinsically disordered region in the absence of sequence conservation. Biorxiv : the Preprint Server For Biology. PMID 37609146 DOI: 10.1101/2023.08.06.552128 |
0.824 |
|
| 2023 |
Stringer MA, Cubuk J, Incicco JJ, Roy D, Hall KB, Stuchell-Brereton MD, Soranno A. Excluded Volume and Weak Interactions in Crowded Solutions Modulate Conformations and RNA Binding of an Intrinsically Disordered Tail. The Journal of Physical Chemistry. B. PMID 37348142 DOI: 10.1021/acs.jpcb.3c02356 |
0.846 |
|
| 2023 |
Alston JJ, Ginell GM, Soranno A, Holehouse AS. The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins. The Journal of Physical Chemistry. B. PMID 37200094 DOI: 10.1021/acs.jpcb.3c01619 |
0.815 |
|
| 2023 |
Alston JJ, Ginell GM, Soranno A, Holehouse AS. The analytical Flory random coil is a simple-to-use reference model for unfolded and disordered proteins. Biorxiv : the Preprint Server For Biology. PMID 36993592 DOI: 10.1101/2023.03.12.531990 |
0.815 |
|
| 2023 |
Stuchell-Brereton MD, Zimmerman MI, Miller JJ, Mallimadugula UL, Incicco JJ, Roy D, Smith LG, Cubuk J, Baban B, DeKoster GT, Frieden C, Bowman GR, Soranno A. Apolipoprotein E4 has extensive conformational heterogeneity in lipid-free and lipid-bound forms. Proceedings of the National Academy of Sciences of the United States of America. 120: e2215371120. PMID 36749730 DOI: 10.1073/pnas.2215371120 |
0.758 |
|
| 2023 |
Alston JJ, Soranno A. Condensation goes viral: a polymer physics perspective. Journal of Molecular Biology. 167988. PMID 36709795 DOI: 10.1016/j.jmb.2023.167988 |
0.775 |
|
| 2022 |
Cubuk J, Stuchell-Brereton MD, Soranno A. The biophysics of disordered proteins from the point of view of single-molecule fluorescence spectroscopy. Essays in Biochemistry. 66: 875-890. PMID 36416865 DOI: 10.1042/EBC20220065 |
0.819 |
|
| 2022 |
Incicco JJ, Roy D, Stuchell-Brereton MD, Soranno A. Fluorescence Correlation Spectroscopy and Phase Separation. Methods in Molecular Biology (Clifton, N.J.). 2563: 161-198. PMID 36227473 DOI: 10.1007/978-1-0716-2663-4_8 |
0.757 |
|
| 2021 |
Martin EW, Harmon TS, Hopkins JB, Chakravarthy S, Incicco JJ, Schuck P, Soranno A, Mittag T. A multi-step nucleation process determines the kinetics of prion-like domain phase separation. Nature Communications. 12: 4513. PMID 34301955 DOI: 10.1038/s41467-021-24727-z |
0.79 |
|
| 2021 |
Benke S, Holla A, Wunderlich B, Soranno A, Nettels D, Schuler B. Combining Rapid Microfluidic Mixing and Three-Color Single-Molecule FRET for Probing the Kinetics of Protein Conformational Changes. The Journal of Physical Chemistry. B. 125: 6617-6628. PMID 34125545 DOI: 10.1021/acs.jpcb.1c02370 |
0.674 |
|
| 2021 |
Alston JJ, Soranno A, Holehouse AS. Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins. Methods (San Diego, Calif.). PMID 33831596 DOI: 10.1016/j.ymeth.2021.03.018 |
0.833 |
|
| 2021 |
Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. Nature Communications. 12: 1936. PMID 33782395 DOI: 10.1038/s41467-021-21953-3 |
0.778 |
|
| 2021 |
König I, Soranno A, Nettels D, Schuler B. Impact of In-Cell and In-Vitro Crowding on the Conformations and Dynamics of an Intrinsically Disordered Protein. Angewandte Chemie (International Ed. in English). 60: 10724-10729. PMID 33587794 DOI: 10.1002/anie.202016804 |
0.677 |
|
| 2020 |
Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. Biorxiv : the Preprint Server For Biology. PMID 32587966 DOI: 10.1101/2020.06.17.158121 |
0.778 |
|
| 2020 |
Zosel F, Soranno A, Buholzer KJ, Nettels D, Schuler B. Depletion interactions modulate the binding between disordered proteins in crowded environments. Proceedings of the National Academy of Sciences of the United States of America. 117: 13480-13489. PMID 32487732 DOI: 10.1073/Pnas.1921617117 |
0.716 |
|
| 2020 |
Soranno A. Physical basis of the disorder-order transition. Archives of Biochemistry and Biophysics. 685: 108305. PMID 32145247 DOI: 10.1016/J.Abb.2020.108305 |
0.542 |
|
| 2020 |
Martin EW, Holehouse AS, Peran I, Farag M, Incicco JJ, Bremer A, Grace CR, Soranno A, Pappu RV, Mittag T. Valence and patterning of aromatic residues determine the phase behavior of prion-like domains. Science (New York, N.Y.). 367: 694-699. PMID 32029630 DOI: 10.1126/Science.Aaw8653 |
0.79 |
|
| 2020 |
Martin EW, Holehouse AS, Peran I, Incicco J, Soranno A, Pappu RV, Mittag T. Evolutionarily Conserved Amino Acid Organization in Protein Low Complexity Regions Encodes Conformation, Dynamics and Assembly Biophysical Journal. 118: 6a. DOI: 10.1016/J.Bpj.2019.11.226 |
0.475 |
|
| 2020 |
Stuchell-Brereton MD, Calderone L, Baban B, Cubuk J, DeKoster G, Frieden C, Soranno A. Single-Molecule Fluorescence Spectroscopy of Non-Lipidated Forms of Apolipoprotein E Biophysical Journal. 118: 192a. DOI: 10.1016/J.Bpj.2019.11.1165 |
0.779 |
|
| 2019 |
Stuchell-Brereton MD, Baban B, DeKoster G, Frieden C, Soranno A. Single-Molecule Conformational Analysis of Apolipoprotein E Biophysical Journal. 116: 167a. DOI: 10.1016/J.Bpj.2018.11.930 |
0.338 |
|
| 2019 |
Gibson F, Soranno A, Zheng W, Vaiana SM. Extracting Sequence-Dependent Intra-Protein Interaction Parameters from Photo-Induced Electron Transfer Measurements of IDPs Biophysical Journal. 116. DOI: 10.1016/J.Bpj.2018.11.1117 |
0.334 |
|
| 2018 |
Soranno A, Cabassi F, Orselli ME, Cellmer T, Gori A, Longhi R, Buscaglia M. Dynamics of Structural Elements of GB1 β-Hairpin Revealed by Tryptophan-Cysteine Contact Formation Experiments. The Journal of Physical Chemistry. B. 122: 11468-11477. PMID 30215522 DOI: 10.1021/Acs.Jpcb.8B07399 |
0.393 |
|
| 2018 |
Rezaei-Ghaleh N, Parigi G, Soranno A, Holla A, Becker S, Schuler B, Luchinat C, Zweckstetter M. Local and Global Dynamics in Intrinsically Disordered Synuclein. Angewandte Chemie (International Ed. in English). 57: 15262-15266. PMID 30184304 DOI: 10.1002/Anie.201808172 |
0.652 |
|
| 2018 |
Best RB, Zheng W, Borgia A, Buholzer K, Borgia MB, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Schuler B. Comment on "Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water". Science (New York, N.Y.). 361. PMID 30166459 DOI: 10.1126/Science.Aar7101 |
0.781 |
|
| 2018 |
Soranno A, Zosel F, Hofmann H. Internal friction in an intrinsically disordered protein-Comparing Rouse-like models with experiments. The Journal of Chemical Physics. 148: 123326. PMID 29604877 DOI: 10.1063/1.5009286 |
0.759 |
|
| 2018 |
Borgia A, Borgia MB, Bugge K, Kissling VM, Heidarsson PO, Fernandes CB, Sottini A, Soranno A, Buholzer KJ, Nettels D, Kragelund BB, Best RB, Schuler B. Extreme disorder in an ultrahigh-affinity protein complex. Nature. 555: 61-66. PMID 29466338 DOI: 10.1038/Nature25762 |
0.833 |
|
| 2018 |
Rezaei‐Ghaleh N, Parigi G, Soranno A, Holla A, Becker S, Schuler B, Luchinat C, Zweckstetter M. Lokale und globale Dynamik im ungeordneten Synuklein‐Protein Angewandte Chemie. 130: 15482-15486. DOI: 10.1002/Ange.201808172 |
0.513 |
|
| 2017 |
Zosel F, Haenni D, Soranno A, Nettels D, Schuler B. Combining short- and long-range fluorescence reporters with simulations to explore the intramolecular dynamics of an intrinsically disordered protein. The Journal of Chemical Physics. 147: 152708. PMID 29055320 DOI: 10.1063/1.4992800 |
0.718 |
|
| 2017 |
Soranno A, Holla A, Dingfelder F, Nettels D, Makarov DE, Schuler B. Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations. Proceedings of the National Academy of Sciences of the United States of America. PMID 28223518 DOI: 10.1073/Pnas.1616672114 |
0.686 |
|
| 2016 |
Borgia A, Zheng W, Buholzer K, Borgia MB, Schüler A, Hofmann H, Soranno A, Nettels D, Gast K, Grishaev A, Best RB, Schuler B. Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods. Journal of the American Chemical Society. PMID 27583570 DOI: 10.1021/Jacs.6B05917 |
0.81 |
|
| 2016 |
Aznauryan M, Delgado L, Soranno A, Nettels D, Huang JR, Labhardt AM, Grzesiek S, Schuler B. Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS. Proceedings of the National Academy of Sciences of the United States of America. PMID 27566405 DOI: 10.1073/Pnas.1607193113 |
0.831 |
|
| 2016 |
Schuler B, Soranno A, Hofmann H, Nettels D. Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins. Annual Review of Biophysics. 45: 207-31. PMID 27145874 DOI: 10.1146/Annurev-Biophys-062215-010915 |
0.821 |
|
| 2015 |
Borgia A, Kemplen KR, Borgia MB, Soranno A, Shammas S, Wunderlich B, Nettels D, Best RB, Clarke J, Schuler B. Transient misfolding dominates multidomain protein folding. Nature Communications. 6: 8861. PMID 26572969 DOI: 10.1038/Ncomms9861 |
0.662 |
|
| 2015 |
König I, Zarrine-Afsar A, Aznauryan M, Soranno A, Wunderlich B, Dingfelder F, Stüber JC, Plückthun A, Nettels D, Schuler B. Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells. Nature Methods. 12: 773-9. PMID 26147918 DOI: 10.1038/Nmeth.3475 |
0.821 |
|
| 2015 |
Borgia A, Kemplen KR, Borgia MB, Best RB, Soranno A, Nettels D, Wunderlich B, Clarke J, Schuler B. Surprising Abundance of Misfolding during Refolding of Multidomain Proteins Biophysical Journal. 108: 501a. DOI: 10.1016/J.Bpj.2014.11.2746 |
0.677 |
|
| 2015 |
Sizemore S, Cope S, Soranno A, Vaiana S. Charge Patterning, Salt Screening and Denaturant Expansion in the CGRP Neuropeptide Biophysical Journal. 108: 229a-230a. DOI: 10.1016/J.Bpj.2014.11.1268 |
0.378 |
|
| 2014 |
Soranno A, Koenig I, Borgia MB, Hofmann H, Zosel F, Nettels D, Schuler B. Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments Proceedings of the National Academy of Sciences of the United States of America. 111: 4874-4879. PMID 24639500 DOI: 10.1073/Pnas.1322611111 |
0.805 |
|
| 2012 |
Borgia A, Wensley BG, Soranno A, Nettels D, Borgia MB, Hoffmann A, Pfeil SH, Lipman EA, Clarke J, Schuler B. Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy. Nature Communications. 3: 1195. PMID 23149740 DOI: 10.1038/Ncomms2204 |
0.684 |
|
| 2012 |
Hofmann H, Soranno A, Borgia A, Gast K, Nettels D, Schuler B. Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy Proceedings of the National Academy of Sciences of the United States of America. 109: 16155-16160. PMID 22984159 DOI: 10.1073/Pnas.1207719109 |
0.811 |
|
| 2012 |
Schuler B, Müller-Späth S, Soranno A, Nettels D. Application of confocal single-molecule FRET to intrinsically disordered proteins. Methods in Molecular Biology (Clifton, N.J.). 896: 21-45. PMID 22821515 DOI: 10.1007/978-1-4614-3704-8_2 |
0.693 |
|
| 2012 |
Soranno A, Buchli B, Nettels D, Cheng RR, Müller-Späth S, Pfeil SH, Hoffmann A, Lipman EA, Makarov DE, Schuler B. Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 109: 17800-6. PMID 22492978 DOI: 10.1073/Pnas.1117368109 |
0.73 |
|
| 2011 |
Soranno A, Müller-Späth S, Hirschfeld V, Hofmann H, Rüegger S, Reymond L, Nettels D, Schuler B. Charge Interactions Can Dominate the Dimensions of Intrinsically Disordered Proteins Biophysical Journal. 100: 12a-13a. DOI: 10.1016/J.Bpj.2010.12.278 |
0.803 |
|
| 2011 |
Buscaglia M, Soranno A, Cellmer T, Longhi R, Bellini T. Folding Kinetics of Small Proteins Revealed by Tryptophan-Cysteine Contact Formation Experiments Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.1360 |
0.461 |
|
| 2010 |
Müller-Späth S, Soranno A, Hirschfeld V, Hofmann H, Rüegger S, Reymond L, Nettels D, Schuler B. From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proceedings of the National Academy of Sciences of the United States of America. 107: 14609-14. PMID 20639465 DOI: 10.1073/Pnas.1001743107 |
0.803 |
|
| 2010 |
Buscaglia M, Soranno A, Cabassi F, Longhi R, Bellini T. Conformations and Dynamics of Polypeptide Chains Revealed By Tryptophan-Cysteine Contact Formation Kinetics Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.175 |
0.438 |
|
| 2009 |
Soranno A, Longhi R, Bellini T, Buscaglia M. Kinetics of contact formation and end-to-end distance distributions of swollen disordered peptides. Biophysical Journal. 96: 1515-28. PMID 19217868 DOI: 10.1016/J.Bpj.2008.11.014 |
0.696 |
|
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