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Marija Rankovic

Researcher at Max Planck Society

Publications -  11
Citations -  793

Marija Rankovic is an academic researcher from Max Planck Society. The author has contributed to research in topics: Transcription (biology) & Chemistry. The author has an hindex of 5, co-authored 8 publications receiving 450 citations.

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RNA polymerase II clustering through carboxy-terminal domain phase separation

TL;DR: It is reported that human and yeast CTDs undergo cooperative liquid phase separation, with the shorter yeast CTD forming less-stable droplets and that CTD phosphorylation liberates Pol II enzymes from hubs for promoter escape and transcription elongation.
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Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates.

TL;DR: It is shown that RNA induces cooperative liquid–liquid phase separation of the SARS-CoV-2 nucleocapsid protein, which generates high-density protein/RNA condensates that recruit the RNA-dependent RNA polymerase complex of SARS, providing a mechanism for efficient transcription of viral RNA.
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Interplay between tau and α-synuclein liquid-liquid phase separation.

TL;DR: In this article, the interaction of α-synuclein with tau and its consequences on tau LLPS was investigated, and it was shown that α-Synuclein has a low propensity for self-coacervation and RNA-mediated LLPS at pH 7.4.
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Upregulated levels and pathological aggregation of abnormally phosphorylated Tau-protein in children with neurodevelopmental disorders

TL;DR: It is suggested that Tau might play a previously underestimated role in neurodevelopmental disorders and regression in children, as well as several neurological conditions and diseases in an early life stage with upregulated levels or even pathological aggregation of abnormally phosphorylated Tau protein.
Posted ContentDOI

Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates

TL;DR: It is shown that RNA induces cooperative liquid-liquid phase separation of the SARS-CoV-2 nucleocapsid protein, which generates high-density protein/RNA condensates that recruit the RNA-dependent RNA polymerase complex of SARS, providing a mechanism for efficient transcription of viral RNA.