相关实验视频

Updated: Jun 17, 2025

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
10:05

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Published on: January 16, 2017

12.8K

亲介素-1α的近距离标记揭示了进化保守的核相互作用

Rose Wellens1,2,3, Victor S Tapia1,2,3, Paula I Seoane1,2,3

  • 1Division of Neuroscience, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, M13 9PT, UK.

Nature communications
|August 8, 2024
PubMed
概括

介质蛋白-1α (IL-1α) 具有涉及酸转移酶的核作用,通过近距离标记揭示出来. 进化表明,在不同物种中,IL-1α核定位的收性损失,保持了基酸转移酶结合.

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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

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Intravital Imaging of Neutrophil Priming Using IL-1β Promoter-driven DsRed Reporter Mice

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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