2024

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29.08.2024

PRDM16-DT is a novel lncRNA that regulates astrocyte function in Alzheimer’s disease

Authors Schröder S, Fuchs U, Gisa V, Pena T, Krüger DM, Hempel N, Burkhardt S, Salinas G, Schütz AL, Delalle I, Sananbenesi F, Fischer A Journal Acta Neuropahologica Citation Acta Neuropathol. 2024 Aug 29;148(1):32. Abstract Astrocytes provide crucial support for neurons, contributing to synaptogenesis, synaptic maintenance, and neurotransmitter recycling. Under
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27.08.2024

The amyloid oligomer modulator anle138b has disease modifying effects in a human IAPP transgenic mouse model of type 2 diabetes mellitus (hIAPP Ob/Ob mice)

Authors Albariqi MMA, Baauw SMG, Fens SPJP, Versteeg S, Ryazanov S, Leonov A, Willemen HLDM, Stathonikos N, Seychell RM, El Saghir A, Gerritsen B, Khemtemourian L, Vassallo N, Giese A, Eijkelkamp N, Griesinger C, Höppener JWM Journal BioRxiv Citation bioRxiv 2024.08.27.609850. Abstract Cytotoxic aggregates of human islet amyloid polypeptide (hIAPP)
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24.08.2024

TOM-TIM23 supercomplex formation

Authors Jain N, Gomkale R, Rehling P Journal Methods in Enzymology Citation Methods Enzymol. 2024;707:3-22. Abstract Mitochondria import the vast majority of proteins from the cytosol. Protein translocation machineries in outer and inner membranes facilitate precursor recognition and transport. Most mitochondrial proteins utilize N-terminal presequences as targeting signals that eventually
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22.08.2024

Optical control of pH via chromoselective photodosimetry

Authors Chaudhuri A, Eijsink LE, Simeth NA Journal Chemical Communications (Cambridge) Citation Chem Commun (Camb). 2024 Aug 22. Abstract The dynamic regulation of pH via an external stimulus is an attractive technique to gate chemical transformations. Applying photons of different energy, we preferentially address either a photoacid or a photobase
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Illustration of the protein folding helper complexes in bullet shape (blue) and football shape (red) in their natural environment surrounded by a variety of different proteins. Foreground: High-resolution structure of the protein folding helper complex in cross-section. A protein to be folded is visible inside (yellow). Illustration: Jonathan Wagner, MPI of Biochemistry

22.08.2024

Protein folding helpers in their natural environment

Scientists from Martinsried and Göttingen have analyzed protein folding helpers, so-called chaperonin complexes, in their natural environment using cryo-electron tomography.   Cryo-electron tomography, or cryo-ET for short, can be used to visualize and analyze cellular structures in their natural environment. Researchers at the Max Planck Institute of Biochemistry (MPIB) in
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22.08.2024

Signatures of hierarchical temporal processing in the mouse visual system

Authors Rudelt L, González Marx D, Spitzner FP, Cramer B, Zierenberg J, Priesemann V. Journal PLoS Computational Biology Citation PLoS Comput Biol. 2024 Aug 22;20(8):e1012355. Abstract A core challenge for the brain is to process information across various timescales. This could be achieved by a hierarchical organization of temporal processing
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22.08.2024

Empirical Optimal Transport under Estimated Costs: Distributional Limits and Statistical Applications

Authors Hundrieser S, Mordant G. Weitkamp CA, Munk A Journal Stochastic Processes and their Applications Citation Stochastic Processes and their Applications 178 (2024) 104462. Abstract Optimal transport (OT) based data analysis is often faced with the issue that the underlying cost function is (partially) unknown. This is addressed in this
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Illustration of the protein folding helper complexes in bullet shape (blue) and football shape (red) in their natural environment surrounded by a variety of different proteins. Foreground: High-resolution structure of the protein folding helper complex in cross-section. A protein to be folded is visible inside (yellow). Illustration: Jonathan Wagner, MPI of Biochemistry

21.08.2024

Protein folding helpers in their natural environment

Scientists from Martinsried and Göttingen have analyzed protein folding helpers, so-called chaperonin complexes, in their natural environment using cryo-electron tomography.   Cryo-electron tomography, or cryo-ET for short, can be used to visualize and analyze cellular structures in their natural environment. Researchers at the Max Planck Institute of Biochemistry (MPIB) in
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21.08.2024

Genomic and biological panoramas of non-muscle actinopathies

Authors Di Donato N, NMA Consortium, Thom A, Rump A, Greve JN, Kropp M, Cadiñanos J, Calabro S, Cathey S, Chung B, Cope H, Costales M, Cuvertino S, Dinkel P, Erripi K, Fry AE, Garavelli L, Guan K, Hoffjan S, Janzarik WG, Koenig M, Kreimer I, Kuenzel K, Mancini G,
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