Dr. T. (Tessa) Sinnige

Dr. T. (Tessa) Sinnige

Universitair docent
Membrane Biochemistry & Biophysics
030 253 2092
t.sinnige1@uu.nl

Publicaties

2023

Wetenschappelijke publicaties

Elenbaas, B. O. W., Kremsreiter, S. M., Khemtemourian, L., Killian, J. A., & Sinnige, T. (2023). Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage. BBA Advances, 3, [100083]. https://doi.org/10.1016/j.bbadva.2023.100083

2022

Wetenschappelijke publicaties

Elenbaas, B. O. W., Khemtemourian, L., Killian, J. A., & Sinnige, T. (2022). Membrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation. Biochemistry, 61(14), 1465-1472. https://doi.org/10.1021/acs.biochem.2c00184
Sinnige, T. (2022). Molecular mechanisms of amyloid formation in living systems. Chemical Science, 13(24), 7080-7097. https://doi.org/10.1039/d2sc01278b

2021

Wetenschappelijke publicaties

Molenkamp, J., den Outer, A., van Schijndel, V., & Sinnige, T. (2021). Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans. Journal of visualized experiments : JoVE, 178, 1-13. [e63365]. https://doi.org/10.3791/63365
Hardenberg, M. C., Sinnige, T., Casford, S., Dada, S. T., Poudel, C., Robinson, E. A., Fuxreiter, M., Kaminski, C. F., Kaminski Schierle, G. S., Nollen, E. A. A., Dobson, C. M., & Vendruscolo, M. (2021). Observation of an α-synuclein liquid droplet state and its maturation into Lewy body-like assemblies. Journal of Molecular Cell Biology, 13(4), 282-294. https://doi.org/10.1093/jmcb/mjaa075
Perni, M., van der Goot, A., Limbocker, R., van Ham, T. J., Aprile, F. A., Xu, C. K., Flagmeier, P., Thijssen, K., Sormanni, P., Fusco, G., Chen, S. W., Challa, P. K., Kirkegaard, J. B., Laine, R. F., Ma, K. Y., Müller, M. B. D., Sinnige, T., Kumita, J. R., Cohen, S. I. A., ... Dobson, C. M. (2021). Comparative Studies in the A30P and A53T α-Synuclein C. elegans Strains to Investigate the Molecular Origins of Parkinson's Disease. Frontiers in Cell and Developmental Biology, 9, 1-10. [552549]. https://doi.org/10.3389/fcell.2021.552549
Sinnige, T., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Morimoto, R. I. (2021). Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans. Proceedings of the National Academy of Sciences of the United States of America, 118(11), 1-7. [e2021888118]. https://doi.org/10.1073/pnas.2021888118

2020

Wetenschappelijke publicaties

Sinnige, T., Yu, A., & Morimoto, R. I. (2020). Challenging Proteostasis: Role of the Chaperone Network to Control Aggregation-Prone Proteins in Human Disease. In M. L. Mendillo, D. Pincus, & R. Scherz-Shouval (Eds.), HSF1 and Molecular Chaperones in Biology and Cancer (1 ed., pp. 53-68). (Advances in Experimental Medicine and Biology; Vol. 1243). Springer Cham. https://doi.org/10.1007/978-3-030-40204-4_4
Sinnige, T., Stroobants, K., Dobson, C. M., & Vendruscolo, M. (2020). Biophysical studies of protein misfolding and aggregation in in vivo models of Alzheimer's and Parkinson's diseases. Quarterly Reviews of Biophysics, 53, 1-43. [e10]. https://doi.org/10.1017/S0033583520000025

2019

Wetenschappelijke publicaties

Sinnige, T., Ciryam, P., Casford, S., Dobson, C. M., De Bono, M., & Vendruscolo, M. (2019). Expression of the amyloid-β peptide in a single pair of C. elegans sensory neurons modulates the associated behavioural response. PLoS One, 14(5), [e0217746]. https://doi.org/10.1371/journal.pone.0217746
Huang, C., Wagner-Valladolid, S., Stephens, A. D., Jung, R., Poudel, C., Sinnige, T., Lechler, M. C., Schörit, N., Lu, M., Laine, R. F., Michel, C. H., Vendruscolo, M., Kaminski, C. F., Schierle, G. S. K., & David, D. C. (2019). Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in caenorhabditis elegans. eLife, 8, [e43059]. https://doi.org/10.7554/eLife.43059
Laine, R. F., Sinnige, T., Ma, K. Y., Haack, A. J., Poudel, C., Gaida, P., Curry, N., Perni, M., Nollen, E. A. A., Dobson, C. M., Vendruscolo, M., Kaminski Schierle, G. S., & Kaminski, C. F. (2019). Fast Fluorescence Lifetime Imaging Reveals the Aggregation Processes of α-Synuclein and Polyglutamine in Aging Caenorhabditis elegans. ACS Chemical Biology, 14(7), 1628-1636. https://doi.org/10.1021/acschembio.9b00354

2018

Wetenschappelijke publicaties

de Agrela Pinto, C., Mance, D., Sinnige, T., Daniëls, M., Weingarth, M., & Baldus, M. (2018). Formation of the β-barrel assembly machinery complex in lipid bilayers as seen by solid-state NMR. Nature Communications, 9(1), [4135]. https://doi.org/10.1038/s41467-018-06466-w
Baker, L. A., Sinnige, T., Schellenberger, P., De Keyzer, J., Siebert, C. A., Driessen, A. J. M., Baldus, M., & Grünewald, K. (2018). Combined 1 H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments. Structure, 26(1), 161-170.e3. https://doi.org/10.1016/j.str.2017.11.011

2015

Wetenschappelijke publicaties

Mance, D., Sinnige, T., Kaplan, M., Narasimhan, S., Daniëls, M., Houben, K., Baldus, M., & Weingarth, M. (2015). An Efficient Labelling Approach to Harness Backbone and Side-Chain Protons in 1H-Detected Solid-State NMR Spectroscopy. Angewandte Chemie - International Edition, 54(52), 15799-15803. https://doi.org/10.1002/anie.201509170
Sinnige, T., Weingarth, M., Daniels, M., Boelens, R., Bonvin, A. M. J. J., Houben, K., & Baldus, M. (2015). Conformational Plasticity of the POTRA 5 Domain in the Outer Membrane Protein Assembly Factor BamA. Structure, 23(7), 1317-1324. https://doi.org/10.1016/j.str.2015.04.014
Baker, L. A., Folkers, G. E., Sinnige, T., Houben, K., Kaplan, M., van der Cruijsen, E. A. W., & Baldus, M. (2015). Magic-Angle-Spinning Solid-State NMR of Membrane Proteins. Methods in Enzymology, 557, 307-328. https://doi.org/10.1016/bs.mie.2014.12.023
Sinnige, T., Houben, K., Pritisanac, I., Renault, M., Boelens, R., & Baldus, M. (2015). Insight into the conformational stability of membrane-embedded BamA using a combined solution and solid-state NMR approach. Journal of Biomolecular NMR, 61(3-4), 321-32. https://doi.org/10.1007/s10858-014-9891-6

2014

Wetenschappelijke publicaties

Sinnige, T., Weingarth, M., Renault, M., Baker, L., Tommassen, J., & Baldus, M. (2014). Solid-State NMR studies of full-length BamA in lipid bilayers suggest limited overall POTRA mobility. Journal of Molecular Biology, 426(9), 2009-2021. https://doi.org/10.1016/j.jmb.2014.02.007
Sinnige, T., Daniëls, M., Baldus, M., & Weingarth, M. (2014). Proton clouds to measure long-range contacts between nonexchangeable side chain protons in solid-state NMR. Journal of the American Chemical Society, 136(12), 4452-4455. https://doi.org/10.1021/ja412870m
Sinnige, T. (2014). Plasticity of the β-barrel assembly machinery investigated by NMR. [Doctoral thesis 1 (Research UU / Graduation UU), Utrecht University]. Utrecht University.
https://dspace.library.uu.nl/bitstream/handle/1874/297597/Sinnige.pdf?sequence=1

Overige resultaten

Sinnige, T., Houben, K., Weingarth, M., Baker, L., Boelens, R., & Baldus, M. (2014). Protein Plasticity and Protein-Lipid Interactions of the Beta-Barrel Assembly Machinery. Biophysical Journal, 106(2), 47A-47A. https://doi.org/10.1016/j.bpj.2013.11.339

2011

Wetenschappelijke publicaties

Karagoz, E., dos santos Duarte, A., Ippel, H., Uetrecht, C., Sinnige, T., Van Rosmalen, M., Hausmann, J., Heck, A. J. R., Boelens, R., & Rüdiger, S. G. D. (2011). N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proceedings of the National Academy of Sciences of the United States of America, 108(2), 580-585. https://doi.org/10.1073/pnas.1011867108
Karagöz, G. E., Sinnige, T., Hsieh, O., & Rüdiger, S. G. D. (2011). Expressed protein ligation for a large dimeric protein. Protein Engineering, Design & Selection, 24(6), 495-501. https://doi.org/10.1093/protein/gzr007

2010

Wetenschappelijke publicaties

Sinnige, T., Karagöz, G. E., & Rüdiger, S. G. D. (2010). Protein folding and chaperones. In Encyclopedia of life sciences Wiley.