dr. G.M.J. Segers - Nolten (Ine) | Universiteit Twente

Medicine & Life Sciences

# Alpha-Synuclein
# Amyloid
# Amyloid Beta-Protein (40-42)
# Synucleins
# Thioflavin T

Chemistry

# Amyloid Fibril
# Protein

Engineering & Materials Science

# Molecules

Semerdzhiev, S. A. , Fakhree, M. A. A. , Segers-Nolten, I. , Blum, C. , & Claessens, M. M. A. E. (2022). Interactions between SARS-CoV-2 N-Protein and α-Synuclein Accelerate Amyloid Formation. ACS chemical neuroscience, 13(1), 143-150. https://doi.org/10.1021/acschemneuro.1c00666

Molenaar, R. , Chatterjee, S., Kamphuis, B. , Segers-Nolten, I. M. J. , Claessens, M. M. A. E. , & Blum, C. (2021). Nanoplastic sizes and numbers: Quantification by single particle tracking. Environmental Science: Nano, 8(3), 723-730. https://doi.org/10.1039/d0en00951b

Vaneyck, J. , Segers-Nolten, I. , Broersen, K. , & Claessens, M. M. A. E. (2021). Cross-seeding of alpha-synuclein aggregation by amyloid fibrils of food proteins. Journal of biological chemistry, 296, [100358]. https://doi.org/10.1016/J.JBC.2021.100358

Marczynski, M., Rickert, C. A. , Semerdzhiev, S. A. , Van Dijk, W. R. , Segers-Nolten, I. M. J. , Claessens, M. M. A. E., & Lieleg, O. (2019). α-Synuclein Penetrates Mucin Hydrogels despite Its Mucoadhesive Properties. Biomacromolecules, 20(12), 4332-4344. https://doi.org/10.1021/acs.biomac.9b00905

Sidhu, A. , Vaneyck, J. , Blum, C. , Segers-Nolten, I. , & Subramaniam, V. (2018). Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in α-synuclein fibrils. Amyloid, 25(3), 189-196. https://doi.org/10.1080/13506129.2018.1517736

Hassink, G. C. , Raiss, C. C. , Segers-Nolten, I. M. J. , van Wezel, R. J. A. , Subramaniam, V. , le Feber, J. , & Claessens, M. M. A. E. (2018). Exogenous α-synuclein hinders synaptic communication in cultured cortical primary rat neurons. PLoS ONE, 13(3), [e0193763]. https://doi.org/10.1371/journal.pone.0193763

Fakhree, M. A. A. , Nolten, I. S. , Blum, C. , & Claessens, M. M. A. E. (2018). Different Conformational Subensembles of the Intrinsically Disordered Protein α-Synuclein in Cells. Journal of physical chemistry letters, 9(6), 1249-1253. https://doi.org/10.1021/acs.jpclett.8b00092

Segers-Nolten, I. , Van Raaij, M. , & Subramaniam, V. (2017). 2.19 Biophysical analysis of amyloid formation. In P. Ducheyne (Ed.), Comprehensive Biomaterials II: Biologically inspired and biomolecular materials (Vol. 2, pp. 438-451). Elsevier. https://doi.org/10.1016/B978-0-08-100691-7.00155-5

Sidhu, A. , Segers-Nolten, G. M. J., Raussens, V. , Claessens, M. M. A. E. , & Subramaniam, V. (2017). Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation. ACS chemical neuroscience, 8(3), 538-547. https://doi.org/10.1021/acschemneuro.6b00287

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g.m.j.segers-nolten@utwente.nl

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Universiteit Twente
Faculty of Science and Technology
Horst Complex (gebouwnr. 20), kamer ZH156
De Horst 2
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