EGF receptor ligands.

By Raymond C. Harris, E. Chung, R. Coffey. Experimental Cell Research, 2003

849 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/599df2ce12bf8bff7fc43ef42a25deec906a0f56

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. N. Hynes
2. S. Eguchi
3. H. Ohtsu
4. P. Dempsey
5. C. Blobel
6. M. Lemmon
7. Gwen Macdonald
8. D. Leahy

In Oncology

1. N. Hynes
2. S. Eguchi
3. H. Ohtsu
4. P. Dempsey
5. C. Blobel
6. Gwen Macdonald
7. D. Leahy
8. Ping Wee

In Radiology, Nuclear Medicine and Imaging

1. N. Hynes
2. C. Blobel
3. Gwen Macdonald
4. M. Sliwkowski
5. J. Baselga
6. M. Lacouture

Citations in the corpus

• ErbB receptors and signaling pathways in cancer. (2009, background): “receptor activation [2], could be another mechanism promoting resistance.”
• ADAMs: key components in EGFR signalling and development (2005, background): “ADAMs as molecular signalling switches All EGFR ligands are made as membrane-anchored precursors that can be proteolytically released from cells (reviewed in Ref”
• Satellite glial cells in sensory ganglia: from form to function. (2005, background): “Transforming growth factor a (TGF-a) is a member of the epidermal growth factor (EGF) family of growth factors [66].”
• Insight into nanoparticle cellular uptake and intracellular targeting (2014, neutral): “The small molecules and monoclonal antibodies have been used as EGFR-targeting ligands; for examples, epidermal growth factor (EGF), transforming growth factor-α (TGF-α), heparin binding EGF-like growth factor, epigen, betacelluin, and epiregulin [117].”
• Regulation of intestinal epithelial permeability by tight junctions (2012, background): “Transforming growth factor-a (TGF-a) is a member of the EGF family and is synthesized as a transmembrane precursor with EGF structural units in the extracellular domain [147].”
• ERBB receptors and cancer: the complexity of targeted inhibitors (2005, background): “ERBB-receptor transactivation in cancer The EGF family of growth factors are produced as transmembrane precursors that can be cleaved by cell-surface proteases (reviewed in Ref”
• Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, background): “EGF, TGF-α, and amphiregulin are specific ligands only for the EGFR [98].”
• ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. (2006, background): “Importantly, all EGF ligand family members are made as inactive transmembrane precursors that can undergo ectodomain proteolytic cleavage to release mature active growth factor (40, 44).”
• An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors. (2003, background): “All EGFR ligands are expressed as type I integral membrane proteins (Harris et al., 2003) and are proteolytically processed to yield the 49–85 amino acid mature growth factor that consists largely of the EGF-like domain (Harris et al., 2003).”
• Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands (2004, background): “Ligands of the EGFR comprise a family of structurally and functionally related integral membrane proteins that can be proteolytically processed and released from cells (Harris et al., 2003).”