期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 20, 页码 7554-7559出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0401835101
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资金
- NCI NIH HHS [R37 CA042471, R01 CA042471, CA42471] Funding Source: Medline
- NIAID NIH HHS [AI40127, AI43726, R01 AI040127] Funding Source: Medline
- NIGMS NIH HHS [GM038608, R01 GM038608] Funding Source: Medline
Transient or reversible protein-protein interactions are commonly used to ensure efficient targeting of signaling enzymes to their cellular substrates. These interactions include direct binding to substrate, interaction with an accessory or scaffold protein, and positioning at subcellular locations in proximity to substrates. The existence of specialized targeting mechanisms raises the possibility of designing inhibitors that do not block enzyme activity per se, but rather interfere with targeting of the enzyme to one or more of its substrates within the cell. Here, we identify small organic molecules that specifically block targeting of the protein phosphatase calcineurin to its substrate nuclear factor of activated T cells (NFAT, also termed NFATc) and show that they are effective inhibitors of calcineurin-NFAT signaling.
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