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EGF receptor ligands: recent advances

Seven ligands bind to and activate the mammalian epidermal growth factor (EGF) receptor (EGFR/ERBB1/HER1): EGF, transforming growth factor-alpha (TGFA), heparin-binding EGF-like growth factor (HBEGF), betacellulin (BTC), amphiregulin (AREG), epiregulin (EREG), and epigen (EPGN). Of these, EGF, TGFA,...

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Detalles Bibliográficos
Autores principales: Singh, Bhuminder, Carpenter, Graham, Coffey, Robert J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: F1000Research 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5017282/
https://www.ncbi.nlm.nih.gov/pubmed/27635238
http://dx.doi.org/10.12688/f1000research.9025.1
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author Singh, Bhuminder
Carpenter, Graham
Coffey, Robert J.
author_facet Singh, Bhuminder
Carpenter, Graham
Coffey, Robert J.
author_sort Singh, Bhuminder
collection PubMed
description Seven ligands bind to and activate the mammalian epidermal growth factor (EGF) receptor (EGFR/ERBB1/HER1): EGF, transforming growth factor-alpha (TGFA), heparin-binding EGF-like growth factor (HBEGF), betacellulin (BTC), amphiregulin (AREG), epiregulin (EREG), and epigen (EPGN). Of these, EGF, TGFA, HBEGF, and BTC are thought to be high-affinity ligands, whereas AREG, EREG, and EPGN constitute low-affinity ligands. This focused review is meant to highlight recent studies related to actions of the individual EGFR ligands, the interesting biology that has been uncovered, and relevant advances related to ligand interactions with the EGFR.
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spelling pubmed-50172822016-09-14 EGF receptor ligands: recent advances Singh, Bhuminder Carpenter, Graham Coffey, Robert J. F1000Res Review Seven ligands bind to and activate the mammalian epidermal growth factor (EGF) receptor (EGFR/ERBB1/HER1): EGF, transforming growth factor-alpha (TGFA), heparin-binding EGF-like growth factor (HBEGF), betacellulin (BTC), amphiregulin (AREG), epiregulin (EREG), and epigen (EPGN). Of these, EGF, TGFA, HBEGF, and BTC are thought to be high-affinity ligands, whereas AREG, EREG, and EPGN constitute low-affinity ligands. This focused review is meant to highlight recent studies related to actions of the individual EGFR ligands, the interesting biology that has been uncovered, and relevant advances related to ligand interactions with the EGFR. F1000Research 2016-09-08 /pmc/articles/PMC5017282/ /pubmed/27635238 http://dx.doi.org/10.12688/f1000research.9025.1 Text en Copyright: © 2016 Singh B et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Singh, Bhuminder
Carpenter, Graham
Coffey, Robert J.
EGF receptor ligands: recent advances
title EGF receptor ligands: recent advances
title_full EGF receptor ligands: recent advances
title_fullStr EGF receptor ligands: recent advances
title_full_unstemmed EGF receptor ligands: recent advances
title_short EGF receptor ligands: recent advances
title_sort egf receptor ligands: recent advances
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5017282/
https://www.ncbi.nlm.nih.gov/pubmed/27635238
http://dx.doi.org/10.12688/f1000research.9025.1
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