Search Results - "Trinkaus, Victoria A."

In situ architecture of neuronal α-Synuclein inclusions by Trinkaus, Victoria A., Riera-Tur, Irene, Martínez-Sánchez, Antonio, Bäuerlein, Felix J. B., Guo, Qiang, Arzberger, Thomas, Baumeister, Wolfgang, Dudanova, Irina, Hipp, Mark S., Hartl, F. Ulrich, Fernández-Busnadiego, Rubén

“…The molecular architecture of α-Synuclein (α-Syn) inclusions, pathognomonic of various neurodegenerative disorders, remains unclear. α-Syn inclusions were long…”
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The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model by Yuste-Checa, Patricia, Trinkaus, Victoria A., Riera-Tur, Irene, Imamoglu, Rahmi, Schaller, Theresa F., Wang, Huping, Dudanova, Irina, Hipp, Mark S., Bracher, Andreas, Hartl, F. Ulrich

“…Spreading of aggregate pathology across brain regions acts as a driver of disease progression in Tau-related neurodegeneration, including Alzheimer’s disease…”
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The AAA+ chaperone VCP disaggregates Tau fibrils and generates aggregate seeds in a cellular system by Saha, Itika, Yuste-Checa, Patricia, Da Silva Padilha, Miguel, Guo, Qiang, Körner, Roman, Holthusen, Hauke, Trinkaus, Victoria A., Dudanova, Irina, Fernández-Busnadiego, Rubén, Baumeister, Wolfgang, Sanders, David W., Gautam, Saurabh, Diamond, Marc I., Hartl, F. Ulrich, Hipp, Mark S.

“…Amyloid-like aggregates of the microtubule-associated protein Tau are associated with several neurodegenerative disorders including Alzheimer’s disease. The…”
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The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends by Schneider, Matthias M., Gautam, Saurabh, Herling, Therese W., Andrzejewska, Ewa, Krainer, Georg, Miller, Alyssa M., Trinkaus, Victoria A., Peter, Quentin A. E., Ruggeri, Francesco Simone, Vendruscolo, Michele, Bracher, Andreas, Dobson, Christopher M., Hartl, F. Ulrich, Knowles, Tuomas P. J.

“…Molecular chaperones contribute to the maintenance of cellular protein homoeostasis through assisting de novo protein folding and preventing amyloid formation…”
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NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62 by Furthmann, Nikolas, Bader, Verian, Angersbach, Lena, Blusch, Alina, Goel, Simran, Sánchez-Vicente, Ana, Krause, Laura J., Chaban, Sarah A., Grover, Prerna, Trinkaus, Victoria A., van Well, Eva M., Jaugstetter, Maximilian, Tschulik, Kristina, Damgaard, Rune Busk, Saft, Carsten, Ellrichmann, Gisa, Gold, Ralf, Koch, Arend, Englert, Benjamin, Westenberger, Ana, Klein, Christine, Jungbluth, Lisa, Sachse, Carsten, Behrends, Christian, Glatzel, Markus, Hartl, F. Ulrich, Nakamura, Ken, Christine, Chadwick W., Huang, Eric J., Tatzelt, Jörg, Winklhofer, Konstanze F.

“…NEMO is a ubiquitin-binding protein which regulates canonical NF-κB pathway activation in innate immune signaling, cell death regulation and host-pathogen…”
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