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Cover Picture: Activity‐Based Near‐Infrared Fluorescent Probe for LMP7: A Chemical Proteomics Tool for the Immunoproteasome in Living Cells (ChemBioChem 13/2012)
Author(s) -
Sharma Lalit Kumar,
Lee NaRa,
Jang Eun Ryoung,
Lei Beilei,
Zhan ChangGuo,
Lee Wooin,
Kim KyungBo
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201290053
Subject(s) - fluorescence , protein subunit , chemistry , cover (algebra) , biophysics , proteomics , nanotechnology , microbiology and biotechnology , biochemistry , biology , materials science , physics , mechanical engineering , quantum mechanics , engineering , gene
The cover picture shows a fluorescent image of the immunoproteasome captured in living cells by using LKS01‐B650, an immunoproteasome‐selective activity‐based fluorescent probe. The image at the bottom shows the binding mode of LKS01‐B650 to the β5i‐catalytic subunit of the immunoproteasome. Considering recent studies that suggest an important role of the immunoproteasome in multiple disease states, this imaging probe could help us to understand immunoproteasome functions better and to explore its therapeutic potential. On p. 1899 ff. , W. Lee, K.‐B. Kim et al. describe the structure‐based design, synthesis and characterization of a near‐infra‐red fluorescent probe that targets the immunoproteasome subunit β5i. Cell‐based binding studies, in‐gel fluorescence and competition assays all clearly demonstrate the ability of this probe to visualize the immunoproteasome catalytic subunit LMP7/β5i in living cells, thus providing a valuable tool for immunoproteasome biology. The cover picture was prepared by Chitra Saini.