z-logo
open-access-imgOpen Access
A biosensor for the activity of the “sheddase” TACE (ADAM17) reveals novel and cell type–specific mechanisms of TACE activation
Author(s) -
Douglas A. Chapnick,
Eric Bunker,
Xuedong Liu
Publication year - 2015
Publication title -
science signaling
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.659
H-Index - 154
eISSN - 1937-9145
pISSN - 1945-0877
DOI - 10.1126/scisignal.2005680
Subject(s) - microbiology and biotechnology , förster resonance energy transfer , extracellular , cleavage (geology) , mapk/erk pathway , kinase , cytoskeleton , signal transduction , chemistry , disintegrin , cell , metalloproteinase , biology , biochemistry , enzyme , fluorescence , paleontology , physics , quantum mechanics , fracture (geology)
A FRET-based sensor reports the spatiotemporal dynamics of the protease TACE in live cells.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom