γ-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase
By Chang-Yuan Ni, M. Murphy, T. Golde, G. Carpenter. Science, 2001
848 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/37f9039530e9550e235b1fd2391286207be018ac
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Citations in the corpus
- The epidermal growth factor receptor family: Biology driving targeted therapeutics (2008, background): “Full-length EGFR, ErbB2, and ErbB3 as well as truncated constitutively active ErbB2 and truncated C-terminal ErbB4 (s80, E4ICD) have been found in the nucleus of cells [62-70].”
- Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1 (2002, background): “Beside the Notch-1±4 receptors (De Strooper et al., 1999; Mizutani et al., 2001; Saxena et al., 2001), several other type I TM proteins have been identi®ed as substrates for PS-dependent endoproteolysis, including the Alzheimer's disease (AD)-associated b-amyloid protein precursor (bAPP) (De Stroope”
- The Epidermal Growth Factor Receptor Pathway: A Model for Targeted Therapy (2006, background): “Members of this receptor family that have been found in the nucleus include HER-2 (32), HER-3 (33, 34), the truncated COOH-terminal portion of HER-4 (35), and, more recently, a truncated constitutively active form of HER-2 (6).”
- ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. (2006, background): “A further variation on this scenario has been reported for an ErbB4 receptor isoform where ligand-induced ectodomain cleavage is not only required to facilitate the release and translocation to the nucleus of the ErbB intracellular domain but is also necessary for the generation of the appropriate s”