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Miriam Linsenmeier

Researcher at ETH Zurich

Publications -  11
Citations -  208

Miriam Linsenmeier is an academic researcher from ETH Zurich. The author has contributed to research in topics: DEAD box & RNA. The author has an hindex of 4, co-authored 11 publications receiving 91 citations. Previous affiliations of Miriam Linsenmeier include University of California, Los Angeles.

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Journal ArticleDOI

Pat1 promotes processing body assembly by enhancing the phase separation of the DEAD-box ATPase Dhh1 and RNA.

TL;DR: It is shown that the PB component Pat1 antagonizes Not1 and promotes PB assembly via its direct interaction with Dhh1, thereby aiding the assembly of large multivalent mRNP granules that are PBs.
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Dynamics of Synthetic Membraneless Organelles in Microfluidic Droplets

TL;DR: The microfluidics approach represents an attractive platform to investigate the dynamics of compartmentalization in artificial cells in the absence and presence of network structures and shows that the characteristic time scale of phase separation decreases linearly with increasing the volume of the compartment.
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Microfluidic Shrinking Droplet Concentrator for Analyte Detection and Phase Separation of Protein Solutions.

TL;DR: A droplet microfluidic platform to increase the concentration of analytes in solution via reduction of the sample volume under well-defined conditions is developed and the droplet concentrator device, or DroMiCo, can quantify unlabeled proteins in nM concentrations and analyze multicomponent mixtures when coupled with a prefractionation step.
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Analysis of biomolecular condensates and protein phase separation with microfluidic technology.

TL;DR: The advantages of microfluidic technology for the analysis of several aspects of phase separation, including phase diagrams, dynamics of assembly and disassembly, rheological and surface properties, exchange of materials with the surrounding environment and the coupling between compartmentalization and biochemical reactions are described.
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Sequestration within biomolecular condensates inhibits Aβ-42 amyloid formation

TL;DR: It is demonstrated that biomolecular condensates could sequester aggregation-prone proteins and prevent aberrant aggregation events, despite the local increase in their concentration, since the heterogenous composition of the condensate could prevent the formation of ordered fibrillar aggregates.