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Mandy Koopman

Researcher at University Medical Center Groningen

Publications -  15
Citations -  294

Mandy Koopman is an academic researcher from University Medical Center Groningen. The author has contributed to research in topics: Caenorhabditis elegans & Medicine. The author has an hindex of 6, co-authored 10 publications receiving 217 citations.

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A screening-based platform for the assessment of cellular respiration in Caenorhabditis elegans

TL;DR: A detailed protocol to optimize and measure respiration in C. elegans with the XF96 respirometer is provided, including the interpretation of parameters and results.
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Cellular Regulation of Amyloid Formation in Aging and Disease.

TL;DR: Different aspects of the involvement ofAmyloid-forming proteins in disease, mechanisms of toxicity, structural features, and biological functions of amyloids are reviewed, as well as the cellular mechanisms that modulate and regulate protein aggregation, including the presence of enhancers and suppressors of aggregation, are reviewed.
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Massively parallel C. elegans tracking provides multi-dimensional fingerprints for phenotypic discovery

TL;DR: The Wide Field-of-View Nematode Tracking Platform (WF-NTP) is described, which enables massively parallel data acquisition and automated multi-parameter behavioural profiling of thousands of worms simultaneously and shows that the sensitivity and reproducibility of behavioural assays is very greatly increased.
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Assessing motor-related phenotypes of Caenorhabditis elegans with the wide field-of-view nematode tracking platform.

TL;DR: A protocol for the implementation of the improved wide field-of-view nematode tracking platform (WF-NTP), which enables the simultaneous analysis of hundreds of worms with respect to multiple behavioral parameters and is compared with other existing worm trackers, including those having high spatial resolution.
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Identification of an evolutionary conserved structural loop that is required for the enzymatic and biological function of tryptophan 2,3-dioxygenase.

TL;DR: Compared multiple different CRISPR/Cas9-induced tdo-2 deletion mutants and identified a motif of three amino acids (PLD) that is required for the enzymatic conversion of tryptophan to N-formylkynurenine that will aid in the design of novel inhibitors to treat diseases in which the TDO enzyme is overexpressed or hyperactive.