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Ellen A. A. Nollen

Researcher at University of Groningen

Publications -  81
Citations -  5855

Ellen A. A. Nollen is an academic researcher from University of Groningen. The author has contributed to research in topics: Protein aggregation & Caenorhabditis elegans. The author has an hindex of 32, co-authored 75 publications receiving 4597 citations. Previous affiliations of Ellen A. A. Nollen include Northwestern University & University Medical Center Groningen.

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Tryptophan metabolism as a common therapeutic target in cancer, neurodegeneration and beyond

TL;DR: An overview of the physiological and pathophysiological roles of tryptophan metabolism is provided, focusing on the clinical potential and challenges associated with targeting this pathway.
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Chaperoning signaling pathways: Molecular chaperones as stress-sensing 'heat shock' proteins

TL;DR: Genetic and molecular interactions between heatshock proteins, their co-chaperones and components of signaling pathways suggest that crosstalk between these proteins can regulate proliferation and development by preventing or enhancing cell growth and cell death as the levels of heat shock proteins vary in response to environmental stress or disease.
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Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation

TL;DR: A screen identified 186 genes corresponding to five principal classes of polyglutamine regulators: genes involved in RNA metabolism, protein synthesis, protein folding, and protein degradation; and those involved in protein trafficking, proposing that each represents a molecular machine collectively comprising the protein homeostatic buffer that responds to the expression of damaged proteins to prevent their misfolding and aggregation.
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C-elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging

TL;DR: The processes and genes identified here present a framework for further study of the disease mechanism and provide candidate susceptibility genes and drug targets for Parkinson's disease and other α-synuclein related disorders.
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Polyglutamine protein aggregates are dynamic

TL;DR: Fluorescence imaging of living cells is used to show that polyglutamine protein aggregates are dynamic structures in which glutamine-rich proteins are tightly associated, but which exhibit distinct biophysical interactions.