Tuomas Knowles

Nov 20, 2024 | nature.com | Dhiman Ghosh |Matthias Schneider |Dzmitry Ashkinadze |Harindranath Kadavath |Peter Güntert |Georg Krainer | +4 more

AbstractThe complex kinetics of disease-related amyloid aggregation of proteins such as α-Synuclein (α-Syn) in Parkinson’s disease and Aβ42 in Alzheimer’s disease include primary nucleation, amyloid fibril elongation and secondary nucleation. The latter can be a key accelerator of the aggregation process. It has been demonstrated that the chaperone domain BRICHOS can interfere with the secondary nucleation process of Aβ42.

Sep 25, 2024 | biorxiv.org | Tuomas Knowles |Yihan Yao |Nadia Aicha Erkamp |Tomas Sneideris

AbstractThyroid hormones are produced by the thyroid gland and are essential for regulating metabolism, growth and development. Maintenance of circulating thyroid hormone levels within an appropriate range is thus a prerequisite for health. In vivo, this objective is, at least in part, facilitated through an extracellular storage depot of thyroglobulin, the glycoprotein precursor for thyroid hormones, in the thyroid follicular lumen.

Sep 13, 2023 | biorxiv.org | Zenon Toprakcioglu |Akhila Jayaram |Tuomas Knowles

AbstractThe aggregation of the amyloid-β (Aβ) peptides (Aβ42/Aβ40) into toxic amyloid fibrils and plaques is one of the molecular hallmarks in dementia and Alzheimers disease (AD). While the molecular mechanisms behind this aggregation process are not fully known, it has been shown that some biomolecules can accelerate this process while others can inhibit amyloid formation. Lipids, which are ubiquitously found in cell membranes, play a pivotal role in protein aggregation.

Jun 6, 2023 | pubs.rsc.org | Sara Linse |Tuomas Knowles

Amyloids and protein aggregation Sara Linse a  and  Tuomas Knowles b   Abstract A general discovery in protein science in the past few decades has been the finding that a number of unrelated proteins and peptides all have a marked propensity to form amyloid fibrils in vivo and in vitro. These structures have become known as the pathological hallmark of some of the most prevalent neurodegenerative diseases.

Apr 12, 2023 | biorxiv.org | Alyssa Miller |Sean Chia |Tuomas Knowles |Ewa Klimont

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