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Atomic force microscopy (AFM) has recently received increasing interest in molecular biology. This technique allows quick and reliable detection of biomolecules. However, studying RNA-protein complexes using AFM poses significant challenges.

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Multidrug resistance-associated protein 2 (MRP2) is an ATP-powered exporter important for maintaining liver homeostasis and a potential contributor to chemotherapeutic resistance. Using cryogenic electron microscopy (cryo-EM), we determine the structures of human MRP2 in three conformational states: an autoinhibited state, a substrate-bound pre-translocation state, and an ATP-bound post-translocation state. In the autoinhibited state, the cytosolic regulatory (R) domain plugs into the transmembrane substrate-binding site and extends into the cytosol to form a composite ATP-binding site at the surface of nucleotide-binding domain 2.

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Evaluation of minced beef quality fortified with edible microalgae species during cryogenic storage.

Food Res Int

January 2025

Chemistry of Natural Compounds Department, National Research Centre, 33 El-Behouth St, Dokki-Giza 12622, Egypt. Electronic address:

The aim of this study is to evaluate the effect of some microalgae species adding with different forms on minced beef meat shelf life during cryogenic storage for 13 days. Chlorella vulgaris and Arthrospira platensis are chosen because of their safety and high nutritional value. Microalgae nanoparticles with their different forms have been prepared by using emulsification solvent evaporation method.

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The textural properties of synthetic and natural clays in the sodium form and exchanged with tetramethylammonium cations (TMA) were characterized using N and Ar physisorption isotherms at cryogenic temperatures. Specific surface areas and micro/mesoporous volumes were determined using the BET and the models. The analysis requires the use of reference isotherms measured at the same temperature on the surface of non-porous materials with an identical chemical composition.

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Extracellular vesicles (EVs) in cerebrospinal fluid (CSF) represent a valuable source of biomarkers for central nervous system (CNS) diseases, offering new pathways for diagnosis and monitoring. However, existing methods for isolating EVs from CSF often prove to be labor-intensive and reliant on specialized equipment, hindering their clinical application. In this study, we present a novel, clinically compatible method for isolating EVs from CSF.

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