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Soluble ErbB-1

Known as: sEGFR, sErbB-1, EGFR-ECD 
Soluble epidermal growth factor receptor is encoded by the human EGFR gene. This protein may be involved in the regulation of epidermal growth factor… 
National Institutes of Health

Related topics

Related topics

23 relations
Cell Differentiation processCell Growth RegulationCell ProliferationCell-Cell Adhesion Process

Papers overview

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Highly Cited
2012
Highly Cited
2012
Correlations between tear cytokines, chemokines, and soluble receptors and clinical severity of dry eye disease.
PURPOSE To determine cytokine and chemokine concentrations in the tears of patients with dry eye disease (DED) and analyze the… 
Highly Cited
2008
Highly Cited
2008
Immunopurification and mass spectrometric quantification of the active form of a chimeric therapeutic antibody in human serum.
In this study, we show that liquid chromatography coupled with tandem mass spectrometry provides a sensitive, specific, and… 
Highly Cited
2008
Highly Cited
2008
A polymorphism of EGFR extracellular domain is associated with progression free-survival in metastatic colorectal cancer patients receiving cetuximab-based treatment
BackgroundCetuximab, a monoclonal antibody targeting Epidermal Growth Factor Receptor (EGFR), is currently used in metastatic… 
Highly Cited
2008
Highly Cited
2008
Shedding of epidermal growth factor receptor is a regulated process that occurs with overexpression in malignant cells.
Highly Cited
2005
Highly Cited
2005
Directed evolution of the epidermal growth factor receptor extracellular domain for expression in yeast
The extracellular domain of epidermal growth factor receptor (EGFR‐ECD) has been engineered through directed evolution and yeast… 
Highly Cited
2003
Highly Cited
2003
Soluble epidermal growth factor receptor (sEGFR/sErbB1) as a potential risk, screening, and diagnostic serum biomarker of epithelial ovarian cancer.
Epithelial ovarian cancer (EOC) is the leading cause of death from gynecologic malignancies in the United States, for which risk… 
Highly Cited
2000
Highly Cited
2000
Real-time kinetic studies on the interaction of transforming growth factor alpha with the epidermal growth factor receptor extracellular domain reveal a conformational change model.
Transforming growth factor alpha (TGF-alpha), epidermal growth factor (EGF), and related factors mediate their biological effects… 
Highly Cited
2000
Highly Cited
2000
The Asn-420-linked Sugar Chain in Human Epidermal Growth Factor Receptor Suppresses Ligand-independent Spontaneous Oligomerization
To elucidate a role(s) of Asn-linked sugar chain(s) in the function of epidermal growth factor receptor (EGFR), a series of the… 
Highly Cited
1998
Highly Cited
1998
Disulfide Bond Structure of Human Epidermal Growth Factor Receptor*
The extracellular domain of the human epidermal growth factor receptor (sEGFR) consists of 621 amino acid residues, including 50… 
Highly Cited
1997
Highly Cited
1997
Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor.
We studied the dimerization of the recombinant soluble extracellular domain of the epidermal growth factor receptor (sEGFR) in… 
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