Expertises
Alpha-Synuclein
Alpha-Synuclein
Proteins
Membranes
Amyloid
Evaporation
Rats
Fluorescence
Evaporation
Cells
Membranes
Visualization
Electrons
Molecules
Neurons
Parkinson Disease
Neurons
Biological Materials
Deposits
Synucleins
Cells
Synucleins
Polymorphism
Proteins
Proteins
Visualization
Proteins
Communication
Seeds
Agglomeration
Death
Glass
Fluorescence Spectrometry
Chemical Analysis
Growth
Rats
Proteins
Microscopic Examination
Thin Films
Neurons
Intrinsically Disordered Proteins
Energy Transfer
Communication
Thin Films
Conformations
Seed
Experiments
Membranes
Animal Communication
Molecules
Granulocytes
Cells
Verbonden aan
Publicaties
Recent
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. (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
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. -. Poster session presented at 9th European Biophysics Congress, EBSA 2013, Lisbon, Portugal.
Sidhu, A., Segers-Nolten, G. M. J., & Subramaniam, V. (2013). Self-assembled amyloid nanostructures as scaffolds for creating photonic and electronic assemblies. -. Poster session presented at MESA+ Meeting 2013, Enschede, Netherlands.
Segers-Nolten, G. M. J. (2013). Facilities at MESA+ BioNanoLab. -. Poster session presented at MESA+ Meeting 2013, Enschede, Netherlands.
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Contactgegevens
Bezoekadres
Universiteit Twente
Faculteit Technische Natuurwetenschappen
Horst Complex
(gebouwnr. 20), kamer ZH156
De Horst 2
7522LW Enschede
Postadres
Universiteit Twente
Faculteit Technische Natuurwetenschappen
Horst Complex
ZH156
Postbus 217
7500 AE Enschede
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