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Michael Ameismeier

Researcher at Ludwig Maximilian University of Munich

Publications -  11
Citations -  1158

Michael Ameismeier is an academic researcher from Ludwig Maximilian University of Munich. The author has contributed to research in topics: Eukaryotic Small Ribosomal Subunit & Ribosome. The author has an hindex of 6, co-authored 8 publications receiving 563 citations. Previous affiliations of Michael Ameismeier include Center for Integrated Protein Science Munich.

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Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2.

TL;DR: Structural characterization of the inhibitory mechanism of Nsp1 may aid structure-based drug design against SARS-CoV-2 and effectively blocks retinoic acid–inducible gene I–dependent innate immune responses that would otherwise facilitate clearance of the infection.
Posted ContentDOI

Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2

TL;DR: It is shown that Nsp1 from SARS-CoV-2 binds to 40S and 80S ribosomes, resulting in shutdown of capped mRNA translation both in vitro and in cells, which effectively blocks RIG-I-dependent innate immune responses that would otherwise facilitate clearance of the infection.
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Visualizing late states of human 40S ribosomal subunit maturation.

TL;DR: Cryo-electron microscopy structures of late-stage human 40S assembly intermediates are presented, representing one state reconstituted in vitro and five native states that range from nuclear to late cytoplasmic.
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Symbiosis induces widespread changes in the proteome of the model cnidarian Aiptasia.

TL;DR: This work utilized label‐free liquid chromatography electrospray‐ionization tandem mass spectrometry to analyze the effects of symbiosis on the proteomes of symbiotic and aposymbiotic Aiptasia, and identified and obtained relative quantification of more than 3,300 proteins in 1,578 protein clusters.
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90S pre-ribosome transformation into the primordial 40S subunit

TL;DR: These studies reveal how a cast of molecular players act to coordinate the compositional and structural changes that transform the 90S preribosome into a pre-40S subunit and clarify the principles of assembly and remodeling of large ribonucleoproteins.