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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,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
F1000Research
2016
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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. |
format | Online Article Text |
id | pubmed-5017282 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | F1000Research |
record_format | MEDLINE/PubMed |
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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