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Proteomic Profiling of Potential E6AP Substrates via Ubiquitin-based Photo-Crosslinking Assisted Affinity Enrichment.
Chembiochem
January 2025
Departments of Biology and Chemistry, Konstanz Research School Chemical Biology, University of Konstanz, Universitätsstraße 10, 78467, Konstanz, Germany.
The ubiquitin (Ub) ligase E6AP, encoded by the UBE3A gene, has been causally associated with human diseases including cervical cancer and Angelman syndrome, a neurodevelopmental disorder. Yet, our knowledge about disease-relevant substrates of E6AP is still limited, presumably because at least some of these interactions are rather transient, a phenomenon observed for many enzyme-substrate interactions. Here, we introduce a novel approach to trap such potential transient interactions by combining a stable E6AP-Ub conjugate mimicking the active state of this enzyme with photo-crosslinking (PCL) followed by affinity enrichment coupled to mass spectrometry (AE-MS).
View Article and Find Full Text PDFDevelopment of nucleus-targeted histone-tail-based photoaffinity probes to profile the epigenetic interactome in native cells.
Nat Commun
January 2025
School of Food and Biological Engineering, Engineering Research Center of Bio-process, Ministry of Education, Key Laboratory of Animal Source of Anhui Province, Hefei University of Technology, Hefei, 230009, China.
Dissection of the physiological interactomes of histone post-translational modifications (hPTMs) is crucial for understanding epigenetic regulatory pathways. Peptide- or protein-based histone photoaffinity tools expanded the ability to probe the epigenetic interactome, but in situ profiling in native cells remains challenging. Here, we develop a nucleus-targeting histone-tail-based photoaffinity probe capable of profiling the hPTM-mediated interactomes in native cells, by integrating cell-permeable and nuclear localization peptide modules into an hPTM peptide equipped with a photoreactive moiety.
View Article and Find Full Text PDFA propofol binding site in the voltage sensor domain mediates inhibition of HCN1 channel activity.
Sci Adv
January 2025
Department of Anesthesiology, Washington University School of Medicine, St. Louis, MO 63110, USA.
Article Synopsis
- HCN ion channels play a key role in cellular activity and pain perception, with propofol acting as an analgesic by inhibiting their function.
- Researchers used a propofol analog to pinpoint binding sites on the human HCN1 isoform, revealing a specific pocket formed by certain residues in the channel.
- Mutations in this binding pocket affect propofol's ability to modulate HCN1 currents, highlighting its specific binding mechanism and offering insights for developing targeted HCN channel modulators.
CD63 as novel target for nanoemulsion-based F MRI imaging and drug delivery to activated cardiac fibroblasts.
Theranostics
January 2025
Department of Molecular Cardiology, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University Düsseldorf, Düsseldorf, Germany.
Cardiac fibroblasts are activated following myocardial infarction (MI) and cardiac fibrosis is a major driver of the growing burden of heart failure. A non-invasive targeting method for activated cardiac fibroblasts would be advantageous because of their importance for imaging and therapy. Targeting was achieved by linking a 7-amino acid peptide (EP9) to a perfluorocarbon-containing nanoemulsion (PFC-NE) for visualization by F-combined with H-MRI.
View Article and Find Full Text PDFA subcellular selective APEX2-based proximity labeling used for identifying mitochondrial G-quadruplex DNA binding proteins.
Nucleic Acids Res
January 2025
Laboratory of Chemical Biology and State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, 5625 Renmin Street, Changchun, Jilin 130022, P. R. China.
G-quadruplexes (G4s), as an important type of non-canonical nucleic acid structure, have received much attention because of their regulations of various biological processes in cells. Identifying G4s-protein interactions is essential for understanding G4s-related biology. However, current strategies for exploring G4 binding proteins (G4BPs) include pull-down assays in cell lysates or photoaffinity labeling, which are lack of sufficient spatial specificity at the subcellular level.
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