University of Twente
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dr. G.M.J. Segers - Nolten (Ine)

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Expertises

Alpha-Synuclein
Proteins
Dna
Amyloid
Granulocytes
Coloring Agents
Molecules
Proteins
Dna

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Publicaties

Recent
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]. DOI: 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. DOI: 10.1021/acs.jpclett.8b00092
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. DOI: 10.1021/acschemneuro.6b00287
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2016). Conformational Compatibility Is Essential for Heterologous Aggregation of α-Synuclein. ACS chemical neuroscience, 7(6), 719-727. DOI: 10.1021/acschemneuro.5b00322
Kumar, P., Segers-Nolten, I. M. J., Schilderink, N., Subramaniam, V., & Huber, M. (2015). Parkinson's protein α-synuclein binds efficiently and with a novel conformation to two natural membrane mimics. PLoS ONE, 10(11), [e0142795]. DOI: 10.1371/journal.pone.0142795
Hashemi Shabestari, M., Kumar, P., Segers-Nolten, I. M. J., Claessens, M. M. A. E., van Rooijen, B. D., Subramaniam, V., & Huber, M. (2015). Three Long-Range Distance Constraints and an Approach Towards a Model for the α-Synuclein-Fibril Fold. Applied Magnetic Resonance, 46(4), 369-388. DOI: 10.1007/s00723-014-0622-7
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2015). Disease related point mutations and solution conditions determine fibrillization behavior of alpha-synuclein. -.
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2014). Solution conditions define morphological homogeneity of alpha-synuclein fibrils. Biochimica et biophysica acta : proteins and proteomics, 1844, 2127-2134. DOI: 10.1016/j.bbapap.2014.09.007
Shabestari, M. H., Kumar, P., Segers-Nolten, G. M. J., Claessens, M. M. A. E., van Rooijen, B., Subramaniam, V., & Huber, M. (2014). Long-Range Distance Constraints for the Fibril Fold of Parkinson's Protein Alpha-Synuclein. Biophysical journal, 106(2, suppl. 1), 269a-. DOI: 10.1016/j.bpj.2013.11.1576
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2014). Functionalizing amyloid fibrils to create hybrid metal-protein bionanostructures. -.
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2014). Functionalizing amyloid fibrils to create hybrid metal-protein bionanostructures. -.
Zijlstra, N., Segers-Nolten, G. M. J., Claessens, M. M. A. E., Blum, C., & Subramaniam, V. (2013). Shining light on amyloid protein aggregates: Single-molecule photobleaching of sub-stoichiometrically labeled alpha-synuclein oligomers reveals molecular composition. Microscopy and analysis (E MEA edition), (7), 24-24.
Zijlstra, N., Segers-Nolten, G. M. J., Claessens, M. M. A. E., Blum, C., & Subramaniam, V. (2013). Shining light on amyloid protein aggregates: Single-molecule photobleaching of sub-stoichiometrically labeled alpha-synuclein oligomers reveals the aggregation number. -.
Zijlstra, N., Segers-Nolten, G. M. J., Claessens, M. M. A. E., Blum, C., & Subramaniam, V. (2013). Shining light on amyloid protein aggregates: Single-molecule photobleaching of sub-stoichiometrically labeled alpha-synuclein oligomers reveals the aggregation number. -.
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2013). Self-assembled amyloid nanostructures as scaffolds for creating photonic and electronic assemblies. -.
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2013). Self assembled amyloid nanostructures as scaffold for creating photonic and electronic assemblies. -.
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2013). Insights into solvent dependent alpha-synuclein fibrillization using hi-resolution AFM. -.
Segers-Nolten, G. M. J. (2013). Facilities at MESA+ BioNanoLab. -.

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Universiteit Twente
Faculteit Technische Natuurwetenschappen
Horst - Zuidhorst (gebouwnr. 28), kamer 156
De Horst 2
7522LW  Enschede

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Universiteit Twente
Faculteit Technische Natuurwetenschappen
Horst - Zuidhorst  156
Postbus 217
7500 AE Enschede

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