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Hagen Hofmann - Publications

Affiliations: 
Weizmann Institute of Science, Rehovot, Israel 
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34 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2021 Wiggers F, Wohl S, Dubovetskyi A, Rosenblum G, Zheng W, Hofmann H. Diffusion of a disordered protein on its folded ligand. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34504002 DOI: 10.1073/pnas.2106690118  0.356
2021 Makarov DE, Hofmann H. Does Electric Friction Matter in Living Cells? The Journal of Physical Chemistry. B. 125: 6144-6153. PMID 34081479 DOI: 10.1021/acs.jpcb.1c02783  0.306
2020 Lasitza-Male T, Bartels K, Jungwirth J, Wiggers F, Rosenblum G, Hofmann H, Löw C. Membrane Chemistry Tunes the Structure of a Peptide Transporter. Angewandte Chemie (International Ed. in English). PMID 32744783 DOI: 10.1002/Anie.202008226  0.351
2019 Vancraenenbroeck R, Harel YS, Zheng W, Hofmann H. Polymer effects modulate binding affinities in disordered proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 31488718 DOI: 10.1073/Pnas.1904997116  0.556
2018 Zheng W, Hofmann H, Schuler B, Best RB. Origin of Internal Friction in Disordered Proteins Depends on Solvent Quality. The Journal of Physical Chemistry. B. PMID 30277791 DOI: 10.1021/Acs.Jpcb.8B07425  0.718
2018 Vancraenenbroeck R, Hofmann H. Occupancies in the DNA-Binding Pathways of Intrinsically Disordered Helix-Loop-Helix Leucine-Zipper Proteins. The Journal of Physical Chemistry. B. 122: 11460-11467. PMID 30184429 DOI: 10.1021/Acs.Jpcb.8B07351  0.421
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  0.755
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  0.751
2018 Grossman-Haham I, Rosenblum G, Namani T, Hofmann H. Slow domain reconfiguration causes power-law kinetics in a two-state enzyme. Proceedings of the National Academy of Sciences of the United States of America. PMID 29298911 DOI: 10.1073/Pnas.1714401115  0.407
2017 Benke S, Nettels D, Hofmann H, Schuler B. Quantifying kinetics from time series of single-molecule Förster resonance energy transfer efficiency histograms. Nanotechnology. 28: 114002. PMID 28103588 DOI: 10.1088/1361-6528/Aa5Abd  0.645
2016 Hofmann H. Understanding disordered and unfolded proteins using single-molecule FRET and polymer theory. Methods and Applications in Fluorescence. 4: 042003. PMID 28192291 DOI: 10.1088/2050-6120/4/4/042003  0.584
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  0.788
2016 Hofmann H. Chaperones: Speedy motion for function. Nature Chemical Biology. 12: 576-7. PMID 27434765 DOI: 10.1038/Nchembio.2130  0.394
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  0.785
2015 Grossman I, Yuval Aviram H, Armony G, Horovitz A, Hofmann H, Haran G, Fass D. Single-molecule spectroscopy exposes hidden states in an enzymatic electron relay. Nature Communications. 6: 8624. PMID 26468675 DOI: 10.1038/Ncomms9624  0.377
2015 Best RB, Hofmann H, Nettels D, Schuler B. Quantitative interpretation of FRET experiments via molecular simulation: force field and validation. Biophysical Journal. 108: 2721-31. PMID 26039173 DOI: 10.1016/J.Bpj.2015.04.038  0.63
2015 Best RB, Hofmann H, Nettels D, Schuler B. Quantitative Interpretation of FRET Experiments via Molecular Simulation: Force Field and Validation Biophysical Journal. 108: 2721-2731. DOI: 10.1016/j.bpj.2015.04.038  0.599
2014 Hofmann H, Hillger F, Delley C, Hoffmann A, Pfeil SH, Nettels D, Lipman EA, Schuler B. Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopy. Biophysical Journal. 107: 2891-2902. PMID 25517154 DOI: 10.1016/J.Bpj.2014.11.002  0.698
2014 Kellner R, Hofmann H, Barducci A, Wunderlich B, Nettels D, Schuler B. Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein Proceedings of the National Academy of Sciences of the United States of America. 111: 13355-13360. PMID 25165400 DOI: 10.1073/Pnas.1407086111  0.708
2014 Wuttke R, Hofmann H, Nettels D, Borgia MB, Mittal J, Best RB, Schuler B. Temperature-dependent solvation modulates the dimensions of disordered proteins Proceedings of the National Academy of Sciences of the United States of America. 111: 5213-5218. PMID 24706910 DOI: 10.1073/Pnas.1313006111  0.715
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  0.778
2014 Hofmann H. Single-molecule spectroscopy of unfolded proteins and chaperonin action. Biological Chemistry. 395: 689-98. PMID 24620016 DOI: 10.1515/hsz-2014-0132  0.528
2013 Hofmann H, Nettels D, Schuler B. Single-molecule spectroscopy of the unexpected collapse of an unfolded protein at low pH. The Journal of Chemical Physics. 139: 121930. PMID 24089742 DOI: 10.1063/1.4820490  0.669
2013 Aznauryan M, Nettels D, Holla A, Hofmann H, Schuler B. Single-molecule spectroscopy of cold denaturation and the temperature-induced collapse of unfolded proteins. Journal of the American Chemical Society. 135: 14040-3. PMID 24010673 DOI: 10.1021/Ja407009W  0.764
2013 Wunderlich B, Nettels D, Benke S, Clark J, Weidner S, Hofmann H, Pfeil SH, Schuler B. Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes. Nature Protocols. 8: 1459-74. PMID 23845960 DOI: 10.1038/Nprot.2013.082  0.588
2013 Schuler B, Hofmann H. Single-molecule spectroscopy of protein folding dynamics--expanding scope and timescales. Current Opinion in Structural Biology. 23: 36-47. PMID 23312353 DOI: 10.1016/J.Sbi.2012.10.008  0.729
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  0.783
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  0.781
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  0.781
2010 Hofmann H, Hillger F, Pfeil SH, Hoffmann A, Streich D, Haenni D, Nettels D, Lipman EA, Schuler B. Single-molecule spectroscopy of protein folding in a chaperonin cage. Proceedings of the National Academy of Sciences of the United States of America. 107: 11793-8. PMID 20547872 DOI: 10.1073/Pnas.1002356107  0.707
2009 Nettels D, Müller-Späth S, Küster F, Hofmann H, Haenni D, Rüegger S, Reymond L, Hoffmann A, Kubelka J, Heinz B, Gast K, Best RB, Schuler B. Single-molecule spectroscopy of the temperature-induced collapse of unfolded proteins. Proceedings of the National Academy of Sciences of the United States of America. 106: 20740-5. PMID 19933333 DOI: 10.1073/Pnas.0900622106  0.709
2009 Schulenburg C, Löw C, Weininger U, Mrestani-Klaus C, Hofmann H, Balbach J, Ulbrich-Hofmann R, Arnold U. The folding pathway of onconase is directed by a conserved intermediate Biochemistry. 48: 8449-8457. PMID 19655705 DOI: 10.1021/Bi900596J  0.446
2009 Hofmann H, Weininger U, Löw C, Golbik RP, Balbach J, Ulbrich-Hofmann R. Fast amide proton exchange reveals close relation between native-state dynamics and unfolding kinetics Journal of the American Chemical Society. 131: 140-146. PMID 19061322 DOI: 10.1021/Ja8048942  0.484
2008 Hofmann H, Golbik RP, Ott M, Hübner CG, Ulbrich-Hofmann R. Coulomb forces control the density of the collapsed unfolded state of barstar. Journal of Molecular Biology. 376: 597-605. PMID 18164723 DOI: 10.1016/J.Jmb.2007.11.083  0.503
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