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Secreted LGALS3BP facilitates distant metastasis of breast cancer.
Breast Cancer Res
January 2025
College of Pharmacy, Seoul National University, Seoul, 08826, South Korea.
Background: Patients with estrogen receptor (ER)-positive breast cancer (BC) can be treated with endocrine therapy targeting ER, however, metastatic recurrence occurs in 25% of the patients who have initially been treated. Secreted proteins from tumors play important roles in cancer metastasis but previous methods for isolating secretory proteins had limitations in identifying novel targets.
Methods: We applied an in situ secretory protein labeling technique using TurboID to analyze secretome from tamoxifen-resistant (TAMR) BC.
A Single Bioorthogonal Reaction for Multiplex Cell Surface Protein Labeling.
J Am Chem Soc
January 2025
Institute of Molecular Physiology, Shenzhen Bay Laboratory, Shenzhen 518132, China.
Small-molecule fluorophores are invaluable tools for fluorescence imaging. However, means for their covalent conjugation to the target proteins limit applications in multicolor imaging. Here, we identify 2-[(alkylhio)(ryl)ethylene]alononitrile (TAMM) molecules reacting with 1,2-aminothiol at a labeling rate over 10 M s through detailed mechanistic investigation.
View Article and Find Full Text PDFSingle-cell synaptome mapping: its technical basis and applications in critical period plasticity research.
Front Neural Circuits
December 2024
Department of Cellular Neuropathology, Brain Research Institute, Niigata University, Niigata, Japan.
Our brain adapts to the environment by optimizing its function through experience-dependent cortical plasticity. This plasticity is transiently enhanced during a developmental stage, known as the "critical period," and subsequently maintained at lower levels throughout adulthood. Thus, understanding the mechanism underlying critical period plasticity is crucial for improving brain adaptability across the lifespan.
View Article and Find Full Text PDFSelective labeling of tyrosine residues in proteins: insights from PTAD labeling and tandem mass spectrometry analysis.
Mol Omics
December 2024
Department of Chemistry and Biochemistry, University of Texas at Arlington, Box 19065, 700 Planetarium Place, Room 130, Arlington, TX 76019, USA.
Designing reagents for protein labeling is crucial for investigating cellular events and developing new therapeutics. Historically, much effort has been focused on labeling lysine and arginine residues due to their abundance on the protein periphery. The chemo-selectivity of these reagents is a challenging yet crucial parameter for deciphering properties specifically associated with the targeted amino acid.
View Article and Find Full Text PDFIntracellular Photocatalytic Proximity Labeling (iPPL) for Dynamic Analysis of Chromatin-Binding Proteins Targeting Histone H3.
ACS Chem Biol
December 2024
Laboratory for Chemistry and Life Science, Institute of Integrated Research, Institute of Science Tokyo, Yokohama 226-8501, Japan.
We demonstrated a novel approach for protein-protein interaction (PPI) profiling of histone H3 using intracellular photocatalytic-proximity labeling (iPPL). This approach identified that the combination of acriflavine as a photocatalyst and 1-methyl-4-arylurazol (MAUra) as a protein labeling agent was the most efficient strategy to proceed the protein proximity labeling reaction. Furthermore, the identification of the labeled amino acids in histone H3 interacting proteins, histone lysine -methyltransferase EZH2, showed that the amino acid in EZH2 within a few nanometers from histone H3 is labeled by iPPL.
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