SUMmOning up SUMOylation sites
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چکیده
Fluorescence resonance energy transfer (FRET) is a popular and powerful technique for measuring protein interactions. Recently, many photoactivatable fluorescent proteins that can be induced to change their emission properties after exposure to a particular light source have been developed and are finding useful biological applications. Day and colleagues combine these two techniques into a method they call photoquenching FRET (PQ-FRET). This method can be used to simultaneously measure protein mobility, exchange within macromolecular complexes and interactions with other proteins. They demonstrate its use by studying the interaction of nuclear proteins HP1α and C/EBPα in areas of heterochromatin. Article p519
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Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
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