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Nina Morgner

Researcher at Goethe University Frankfurt

Publications -  84
Citations -  3757

Nina Morgner is an academic researcher from Goethe University Frankfurt. The author has contributed to research in topics: Membrane protein & Mass spectrometry. The author has an hindex of 30, co-authored 75 publications receiving 3266 citations. Previous affiliations of Nina Morgner include University of Freiburg & University of Oxford.

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Structures of SAS-6 Suggest Its Organization in Centrioles

TL;DR: The x-ray structure of the amino-terminal domain of SAS-6 is determined from zebrafish, and it is shown that recombinant SAS- 6 self-associates in vitro into assemblies that resemble cartwheel centers, consistent with the notion that centriole formation in vivo depends on the interactions that define the self-assemblies observed here.
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Mass spectrometry of intact V-type ATPases reveals bound lipids and the effects of nucleotide binding.

TL;DR: It is shown that rotary adenosine triphosphatases (ATPases)/synthases from Thermus thermophilus and Enterococcus hirae can be maintained intact with membrane and soluble subunit interactions preserved in vacuum and can link specific lipid and nucleotide binding with distinct regulatory roles.
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Symmetry and electronic structure of noble-metal nanoparticles and the role of relativity.

TL;DR: High resolution UV-photoelectron spectra of cold mass selected Cun, Agn, and Aun- with n=53-58 show that only Cu55- and Ag55- exhibit highly degenerate states, a direct consequence of their icosahedral symmetry, as confirmed by density functional theory calculations.
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The influence of densely organized maltose shells on the biological properties of poly(propylene imine) dendrimers: new effects dependent on hydrogen bonding.

TL;DR: Improved improvements will initiate the development of the next platform of glycodendrimers in which apparently contrary properties can be combined, and this will enable, for example, therapeutic products such as more efficient and less toxic antiamyloid agents to be synthesized.