Detection of programmed cell death using fluorescence energy transfer | Zendy

Xiang Xu | Zendy

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Detection of programmed cell death using fluorescence energy transfer

Author(s) -

Xiang Xu

Publication year - 1998

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/26.8.2034

Subject(s) - förster resonance energy transfer , green fluorescent protein , biology , cleavage (geology) , fluorescence , protease , programmed cell death , peptide , yellow fluorescent protein , microbiology and biotechnology , caspase , biophysics , biochemistry , apoptosis , enzyme , gene , physics , paleontology , quantum mechanics , fracture (geology)

Fluorescence energy transfer (FRET) can be generated when green fluorescent protein (GFP) and blue fluorescent protein (BFP) are covalently linked together by a short peptide. Cleavage of this linkage by protease completely eliminates FRET effect. Caspase-3 (CPP32) is an important cellular protease activated during programmed cell death. An 18 amino acid peptide containing CPP32 recognition sequence, DEVD, was used to link GFP and BFP together. CPP32 activation can be monitored by FRET assay during the apoptosis process.

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