A fluorescent reporter of the phosphorylation status of the substrate protein STAT3.

A fluorescent reporter of the phosphorylation status of the substrate protein STAT3.
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DOI:
10.1002/anie.201102923
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发表时间:
2011-09-05
影响因子:
16.6
通讯作者:
Wang, Lei
Wang, Lei
中科院分区:
化学1区
文献类型:
--
作者:
Lacey, Vanessa K.;Parrish, Angela R.;Han, Shuliang;Shen, Zhouxin;Briggs, Steven P.;Ma, Yuguo;Wang, Lei

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The ability to monitor phosphorylation events can provide valuable information pertaining to signal transduction regulation and for developing effective therapeutics targeted at aberrant kinase activities.[1] Kinase activity can be optically reported using sensors based on short peptides or domains resembling amino acids near the phosphorylation site of a substrate protein. Of these, peptide-based reporters exhibit large fluorescence changes from small molecule fluorophores chemically attached to the peptide sensor,[2] but introducing these reporters into cells is challenging. Protein-based reporters contain genetically appended fluorescent proteins and have revealed novel spatiotemporal information regarding kinases in living cells despite their moderate signal changes.[3] Nonetheless, the subcellular location, trafficking and lifetime of a full-length substrate protein cannot be faithfully replicated by comparatively simplified peptide or domain sensor elements.[4] Moreover, many kinases derive substrate specificity using distal residues in addition to those proximal
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