Publication | Closed Access
A Fluorescent Reporter of the Phosphorylation Status of the Substrate Protein STAT3
11
Citations
20
References
2011
Year
Ein reversibler Biosensor gibt Auskunft über den Phosphorylierungszustand des Volllängen-Substratproteins STAT3, indem er genetisch 7-Hydroxycumarin in dessen Phosphotyrosin-Bindetasche einbaut (siehe Bild). Eine starke Zunahme der Fluoreszenz mit charakteristischen Emissions- und Anregungseigenschaften tritt bei Phosphorylierung von STAT3 in vitro und endogen in Zellkernextrakten auf. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
| Year | Citations | |
|---|---|---|
1994 | 820 | |
1998 | 787 | |
2005 | 663 | |
2001 | 591 | |
2003 | 547 | |
2001 | 456 | |
2006 | 319 | |
Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Bruce J. Mayer, Peter K. Jackson, Richard A. Van Etten, Molecular and Cellular Biology Abl Sh2 DomainMolecular RegulationMolecular BiologyCytoskeletonImpair Phosphotyrosine Binding | 1992 | 291 |
2005 | 219 | |
2003 | 213 |
Page 1
Page 1