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Kirstin Rau

Researcher at Max Delbrück Center for Molecular Medicine

Publications -  5
Citations -  983

Kirstin Rau is an academic researcher from Max Delbrück Center for Molecular Medicine. The author has contributed to research in topics: Interactome & Random hexamer. The author has an hindex of 5, co-authored 5 publications receiving 896 citations. Previous affiliations of Kirstin Rau include Max Planck Society.

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Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers

TL;DR: It is shown that the high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers, and that engineered eUBX polypeptides can induce cell death, providing a rationale for developing anti-cancer polyPEptide inhibitors that may target p97 activity.
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DULIP: A Dual Luminescence-Based Co-Immunoprecipitation Assay for Interactome Mapping in Mammalian Cells

TL;DR: DULIP is a sensitive and reliable method of great utility for systematic interactome research that can be applied for interaction screening and validation of PPIs in mammalian cells and permits the specific analysis of mutation-dependent binding patterns.
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LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.

TL;DR: A double‐readout bioluminescence‐based two‐hybrid technology, termed LuTHy, is presented, which provides two quantitative scores in one experimental procedure when testing binary interactions, and is broadly applicable for detecting the effects of small molecules or disease‐causing mutations on PPIs.
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Development and application of a DNA microarray-based yeast two-hybrid system

TL;DR: A novel Y2H interaction screening procedure using DNA microarrays for high-throughput quantitative PPI detection and it is shown that this parallelized screening procedure and the global inspection of Y2h interaction data are uniquely suited to define specific PPI patterns and their alteration by disease-causing mutations in huntingtin and ataxin-1.