Rebecca Sternke-Hoffmann
Affiliations: | Institut für Physikalische Biologie | Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Nordrhein-Westfalen, Germany |
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Publications
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Sternke-Hoffmann R, Sun X, Menzel A, et al. (2024) Phase Separation and Aggregation of α-Synuclein Diverge at Different Salt Conditions. Biorxiv : the Preprint Server For Biology |
Sternke-Hoffmann R, Pauly T, Norrild RK, et al. (2023) Widespread amyloidogenicity potential of multiple myeloma patient-derived immunoglobulin light chains. Bmc Biology. 21: 21 |
Wang H, Wu J, Sternke-Hoffmann R, et al. (2022) Multivariate effects of pH, salt, and Zn ions on Aβ fibrillation. Communications Chemistry. 5: 171 |
Pauly T, Zhang T, Sternke-Hoffmann R, et al. (2022) Differentiation of subnucleus-sized oligomers and nucleation-competent assemblies of the Aβ peptide. Biophysical Journal. 122: 269-278 |
Bavinton CE, Sternke-Hoffmann R, Yamashita T, et al. (2022) Rationally designed helical peptidomimetics disrupt α-synuclein fibrillation. Chemical Communications (Cambridge, England). 58: 5132-5135 |
Dupré M, Duchateau M, Sternke-Hoffmann R, et al. (2021) Sequencing of Antibody Light Chain Proteoforms from Patients with Multiple Myeloma. Analytical Chemistry |
Sternke-Hoffmann R, Boquoi A, Lopez Y Niedenhoff D, et al. (2020) Biochemical and biophysical characterisation of immunoglobulin free light chains derived from an initially unbiased population of patients with light chain disease. Peerj. 8: e8771 |
Sternke-Hoffmann R, Peduzzo A, Bolakhrif N, et al. (2020) The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of -Synuclein Amyloid Fibril Formation. International Journal of Molecular Sciences. 21 |
Sneideris T, Sakalauskas A, Sternke-Hoffmann R, et al. (2019) The Environment Is a Key Factor in Determining the Anti-Amyloid Efficacy of EGCG. Biomolecules. 9 |