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Related Concept Videos

Selectins01:25

Selectins

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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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The JAK-STAT Signaling Pathway01:20

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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
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T Cell Activation and Clonal Selection

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T cells are integral to our adaptive immune system, recognizing and effectively responding to foreign antigens. T cell activation and clonal selection are pivotal in orchestrating this immune response. This article elucidates these mechanisms, detailing the roles of cluster of differentiation (CD) markers, major histocompatibility complex (MHC) molecules, costimulatory signals, and the process of clonal selection.
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Related Experiment Video

Updated: Jan 10, 2026

Isolation Protocol of Mouse Monocyte-derived Dendritic Cells and Their Subsequent In Vitro Activation with Tumor Immune Complexes
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Covalent Activation of the C-type Lectin DC-SIGN.

Jonathan Lefèbre1,2,3, Maurice Besch1,2,3, Noémi Csorba4,5,6

  • 1Department of Pharmaceutical Sciences, University of Vienna, Josef-Holaubek-Platz 2, Vienna, 1090, Austria.

Angewandte Chemie (International Ed. in English)
|November 25, 2025
PubMed
Summary

Researchers developed novel covalent compounds to modulate DC-SIGN function, a key immune receptor. These activators enhance ligand binding and offer a new therapeutic strategy for C-type lectin modulation.

Keywords:
Covalent inhibitionDC‐SIGNFragment‐based drug designGlycobiologyProtein activation

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Area of Science:

  • Immunology
  • Structural Biology
  • Medicinal Chemistry

Background:

  • Dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) is a C-type lectin receptor on antigen-presenting cells, vital for pathogen recognition and immune responses.
  • The unique, shallow carbohydrate-binding site of DC-SIGN poses challenges for developing effective ligand-based therapeutics.
  • Modulating DC-SIGN function is a promising avenue for immune system therapies.

Purpose of the Study:

  • To explore covalent modification of DC-SIGN as a strategy to modulate its function.
  • To identify potent activators of DC-SIGN through fragment-based screening.
  • To elucidate the structural mechanisms underlying DC-SIGN activation by novel covalent compounds.

Main Methods:

  • Screening of a lysine-targeted electrophilic fragment library against DC-SIGN.
  • Orthogonal functional assays to identify DC-SIGN activators.
  • Structural analysis using NMR spectroscopy, mass spectrometry, and computational modeling.

Main Results:

  • Two potent DC-SIGN activators were identified from the fragment library.
  • Both compounds enhanced DC-SIGN's affinity for monosaccharide ligands.
  • Distinct activation mechanisms were revealed: one induced oligomerization, the other covalently modified lysine K373 within the binding site.

Conclusions:

  • Lysine-targeted covalent compounds represent a novel and effective strategy for modulating DC-SIGN function.
  • These findings have implications for the development of therapeutics targeting DC-SIGN and other C-type lectins.
  • The identified compounds provide valuable tools for further research into C-type lectin receptor biology.