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Sara Linse

Active 1987–2025

166
Papers
29,985
Citations
87
h-index
158
i10-index

Citations

Citations per year for Sara Linse1971: 1 citations1988: 3 citations1989: 10 citations1990: 14 citations1991: 14 citations1992: 13 citations1993: 11 citations1994: 17 citations1995: 27 citations1996: 11 citations1997: 14 citations1998: 16 citations1999: 13 citations2000: 21 citations2001: 16 citations2002: 32 citations2003: 39 citations2004: 33 citations2005: 42 citations2006: 46 citations2007: 66 citations2008: 117 citations2009: 122 citations2010: 155 citations2011: 219 citations2012: 204 citations2013: 246 citations2014: 284 citations2015: 304 citations2016: 346 citations2017: 427 citations2018: 449 citations2019: 1,195 citations2020: 1,436 citations2021: 1,248 citations2022: 995 citations2023: 797 citations2024: 1,183 citations2025: 668 citations2026: 12 citations1972–1987: no citations, so these years are not shown

Citation sources

Countries

World map of the countries and regions citing this authorUnited States: 1,883 citing papers, 19.9% of this breakdownChina: 1,040 citing papers, 11% of this breakdownUnited Kingdom: 817 citing papers, 8.6% of this breakdownGermany: 577 citing papers, 6.1% of this breakdownSweden: 495 citing papers, 5.2% of this breakdownItaly: 407 citing papers, 4.3% of this breakdownIndia: 374 citing papers, 4% of this breakdownFrance: 301 citing papers, 3.2% of this breakdownSpain: 243 citing papers, 2.6% of this breakdownAustralia: 241 citing papers, 2.5% of this breakdownCanada: 240 citing papers, 2.5% of this breakdownSwitzerland: 237 citing papers, 2.5% of this breakdown
0%19.9%Other 27.6%

Institutions

Fields

  • Medicine36.8%
  • Biochemistry, Genetics and Molecular Biology26%
  • Materials Science16.4%
  • Environmental Science4.6%
  • Neuroscience4.1%
  • Chemistry2.6%
  • Other9.5%

Topics

  • Alzheimer's disease research and treatments11.3%
  • Protein Structure and Dynamics4.9%
  • Nanoparticle-Based Drug Delivery3.9%
  • Computational Drug Discovery Methods3.1%
  • Parkinson's Disease Mechanisms and Treatments2.7%
  • Supramolecular Self-Assembly in Materials2.5%
  • Other71.6%

Coauthors

All papers

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  1. Understanding the nanoparticle–protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles

    Authors: Tommy Cedervall, Iseult Lynch, Stina Lindman, Tord Berggård, Eva Thulin, Hanna Nilsson, Kenneth A. Dawson, Sara Linse - National Academy of Sciences, Proceedings of the National Academy of Sciences 2007 cited by 3,172

  2. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

    Authors: Samuel I. A. Cohen, Sara Linse, Leila M. Luheshi, Erik Hellstrand, Duncan A. White, Luke Rajah, Daniel E. Otzen, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles - National Academy of Sciences, Proceedings of the National Academy of Sciences 2013 cited by 1,447

  3. Molecular mechanisms of protein aggregation from global fitting of kinetic models

    Authors: Georg Meisl, Julius B. Kirkegaard, Paolo Arosio, Thomas C. T. Michaels, Michele Vendruscolo, Christopher M. Dobson, Sara Linse, Tuomas P. J. Knowles - Nature Protocols 2016 cited by 789

  4. On the lag phase in amyloid fibril formation

    Authors: Paolo Arosio, Tuomas P. J. Knowles, Sara Linse - Physical Chemistry Chemical Physics 2015 cited by 774

  5. Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation

    Authors: Alexander K. Buell, Céline Galvagnion, Ricardo Gaspar, Emma Sparr, Michele Vendruscolo, Tuomas P. J. Knowles, Sara Linse, Christopher M. Dobson - National Academy of Sciences, Proceedings of the National Academy of Sciences 2014 cited by 687

  6. Galectin-3, a novel endogenous TREM2 ligand, detrimentally regulates inflammatory response in Alzheimer’s disease

    Authors: Antonio Boza‐Serrano, Rocío Ruiz, Raquel Sánchez‐Varo, Juan García‐Revilla, Yiyi Yang, Itzia Jiménez-Ferrer, Agnes Paulus, Malin Wennström, Anna Vilalta, David H. Allendorf, José Carlos Dávila, John Stegmayr, Sebastián Jiménez, María Angustias Roca-Ceballos, Victoria Navarro, Maria Swanberg, Christine L. Hsieh, Luís Miguel Real, Elisabet Englund, Sara Linse, Hakon Leffler, Ulf J. Nilsson, Guy C. Brown, Antonia Gutiérrez, Javier Vitórica, José L. Venero, Tomas Deierborg - Acta Neuropathologica 2019 cited by 370

  7. Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide

    Authors: Thomas C. T. Michaels, Anđela Šarić, Samo Curk, Katja Bernfur, Paolo Arosio, Georg Meisl, Alexander J. Dear, Samuel I. A. Cohen, Christopher M. Dobson, Michele Vendruscolo, Sara Linse, Tuomas P. J. Knowles - Nature Chemistry 2020 cited by 343

  8. Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

    Authors: Sara Linse, Tom Scheidt, Katja Bernfur, Michele Vendruscolo, Christopher M. Dobson, Samuel I. A. Cohen, Eimantas Šileikis, Martin Lundqvist, Fang Qian, Tiernan T. O’Malley, Thierry Bussière, Paul H. Weinreb, Catherine K. Xu, Georg Meisl, Sean R. A. Devenish, Tuomas P. J. Knowles, Oskar Hansson - Nature Structural & Molecular Biology 2020 cited by 197

  9. Secondary nucleation in amyloid formation

    Authors: Mattias Törnquist, Thomas C. T. Michaels, Kalyani Sanagavarapu, Xiaoting Yang, Georg Meisl, Samuel I. A. Cohen, Tuomas P. J. Knowles, Sara Linse - Chemical Communications 2018 cited by 482

  10. Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

    Authors: Michael T. Colvin, Robert Silvers, Qing Zhe Ni, Thach V. Can, Ivan V. Sergeyev, Mélanie Rosay, K. J. Donovan, Brian Michael, Joseph S. Wall, Sara Linse, Robert G. Griffin - Journal of the American Chemical Society 2016 cited by 824

  11. Amyloid formation as a protein phase transition

    Authors: Thomas C. T. Michaels, Daoyuan Qian, Anđela Šarić, Michele Vendruscolo, Sara Linse, Tuomas P. J. Knowles - Nature Reviews Physics 2023 cited by 164

  12. Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

    Authors: Georg Meisl, Xiaoting Yang, Erik Hellstrand, Birgitta Frohm, Julius B. Kirkegaard, Samuel I. A. Cohen, Christopher M. Dobson, Sara Linse, Tuomas P. J. Knowles - National Academy of Sciences, Proceedings of the National Academy of Sciences 2014 cited by 513

  13. Acceleration of α-Synuclein Aggregation by Exosomes

    Authors: Marie Grey, Christopher J.R. Dunning, Ricardo Gaspar, Carl Grey, Patrik Brundin, Emma Sparr, Sara Linse - Journal of Biological Chemistry 2014 cited by 377

  14. Methods for the detection and analysis of protein–protein interactions

    Authors: Tord Berggård, Sara Linse, Peter James - PROTEOMICS 2007 cited by 713

  15. A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

    Authors: Samuel I. A. Cohen, Paolo Arosio, Jenny Presto, Firoz Roshan Kurudenkandy, Henrik Biverstål, Lisa Dolfe, Christopher J.R. Dunning, Xiaoting Yang, Birgitta Frohm, Michele Vendruscolo, Jan Johansson, Christopher M. Dobson, André Fisahn, Tuomas P. J. Knowles, Sara Linse - Nature Structural & Molecular Biology 2015 cited by 424

  16. Secondary nucleation of monomers on fibril surface dominatesα-synuclein aggregation and provides autocatalytic amyloid amplification

    Authors: Ricardo Gaspar, Georg Meisl, Alexander K. Buell, Laurence J. Young, Clemens F. Kaminski, Tuomas P. J. Knowles, Emma Sparr, Sara Linse - Quarterly Reviews of Biophysics 2017 cited by 262

  17. Kinetic diversity of amyloid oligomers

    Authors: Alexander J. Dear, Thomas C. T. Michaels, Georg Meisl, David Klenerman, Si Wu, Sarah Perrett, Sara Linse, Christopher M. Dobson, Tuomas P. J. Knowles - National Academy of Sciences, Proceedings of the National Academy of Sciences 2020 cited by 186

  18. Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes

    Authors: Johnny Habchi, Sean Chia, Céline Galvagnion, Thomas C. T. Michaels, Mathias M. J. Bellaiche, Francesco Simone Ruggeri, Michele Sanguanini, Ilaria Idini, Janet R. Kumita, Emma Sparr, Sara Linse, Christopher M. Dobson, Tuomas P. J. Knowles, Michele Vendruscolo - Nature Chemistry 2018 cited by 255

  19. Identification of on- and off-pathway oligomers in amyloid fibril formation

    Authors: Alexander J. Dear, Georg Meisl, Anđela Šarić, Thomas C. T. Michaels, Magnus Kjærgaard, Sara Linse, Tuomas P. J. Knowles - Chemical Science 2020 cited by 122

  20. Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

    Authors: Paolo Arosio, Thomas C. T. Michaels, Sara Linse, Cecilia Månsson, Cecilia Emanuelsson, Jenny Presto, Jan Johansson, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles - Nature Communications 2016 cited by 266

  21. Secondary nucleation and elongation occur at different sites on Alzheimer’s amyloid-β aggregates

    Authors: Tom Scheidt, Urszula Łapińska, Janet R. Kumita, Daniel R. Whiten, David Klenerman, Mark R. Wilson, Samuel I. A. Cohen, Sara Linse, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles, Paolo Arosio - Science Advances 2019 cited by 162

  22. Uncovering the universality of self-replication in protein aggregation and its link to disease

    Authors: Georg Meisl, Catherine K. Xu, Jonathan D. Taylor, Thomas C. T. Michaels, Aviad Levin, Daniel E. Otzen, David Klenerman, Stephen Matthews, Sara Linse, Maria Andreasen, Tuomas P. J. Knowles - Science Advances 2022 cited by 59

  23. The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils

    Authors: Dev Thacker, Kalyani Sanagavarapu, Birgitta Frohm, Georg Meisl, Tuomas P. J. Knowles, Sara Linse - National Academy of Sciences, Proceedings of the National Academy of Sciences 2020 cited by 100

  24. Amyloid β-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process

    Authors: Erik Hellstrand, Barry Boland, Dominic M. Walsh, Sara Linse - ACS Chemical Neuroscience 2009 cited by 391