Explore the words cloud of the Agglomerates project. It provides you a very rough idea of what is the project "Agglomerates" about.
The following table provides information about the project.
WEIZMANN INSTITUTE OF SCIENCE
|Coordinator Country||Israel [IL]|
|Total cost||2˙574˙819 €|
|EC max contribution||2˙574˙819 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2019-04-01 to 2024-03-31|
Take a look of project's partnership.
|1||WEIZMANN INSTITUTE OF SCIENCE||IL (REHOVOT)||coordinator||2˙574˙819.00|
Understanding how proteins respond to mutations is of paramount importance to biology and disease. While protein stability and misfolding have been instrumental in rationalizing the impact of mutations, we recently discovered that an alternative route is also frequent, where mutations at the surface of symmetric proteins trigger novel self-interactions that lead to infinite self-assembly. This mechanism can be involved in disease, as in sickle-cell anemia, but may also serve in adaptation. Importantly, it differs fundamentally from aggregation, because misfolding does not drive it. Thus, we term it “agglomeration”. The ease with which agglomeration can occur, even by single point mutations, shifts the paradigm of how quickly new protein assemblies can emerge, both in health and disease. This prompts us to determine the basic principles of protein agglomeration and explore its implications in cell physiology and human disease.
We propose an interdisciplinary research program bridging atomic and cellular scales to explore agglomeration in three aims: (i) Map the landscape of protein agglomeration in response to mutation in endogenous yeast proteins; (ii) Characterize how yeast physiology impacts agglomeration by changes in gene expression or cell state, and, conversely, how protein agglomerates impact yeast fitness. (iii) Analyze agglomeration in relation to human disease via two approaches. First, by predicting single nucleotide polymorphisms that trigger agglomeration, prioritizing them using knowledge from Aims 1 & 2, and characterizing them experimentally. Second, by providing a proof-of-concept that agglomeration can be exploited in drug design, whereby drugs induce its formation, like mutations can do.
Overall, through this research, we aim to establish agglomeration as a paradigm for protein assembly, with implications for our understanding of evolution, physiology, and disease.
Are you the coordinator (or a participant) of this project? Plaese send me more information about the "AGGLOMERATES" project.
For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.
Send me an email (firstname.lastname@example.org) and I put them in your project's page as son as possible.
Thanks. And then put a link of this page into your project's website.
The information about "AGGLOMERATES" are provided by the European Opendata Portal: CORDIS opendata.
The Enemy of the Good: Towards a Theory of Moral ProgressRead More
Discovery and Characterization of Hydrogen-Based High-Temperature SuperconductorsRead More
Towards Realistic Modelling of Nucleosome Organization Inside Functional Chromatin DomainsRead More