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FADD the bad in head and neck cancer
It has been known for many years that the protein Fas-associated death domain (FADD) is an essential protein forming the apical portion of the extrinsic apoptosis pathway that permits association of death receptors, e.g., CD95, DR4, DR5 with pro-caspases 8 and 10, thereby facilitating caspase activa...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Landes Bioscience
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909546/ https://www.ncbi.nlm.nih.gov/pubmed/23974629 http://dx.doi.org/10.4161/cbt.26151 |
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author | Dent, Paul |
author_facet | Dent, Paul |
author_sort | Dent, Paul |
collection | PubMed |
description | It has been known for many years that the protein Fas-associated death domain (FADD) is an essential protein forming the apical portion of the extrinsic apoptosis pathway that permits association of death receptors, e.g., CD95, DR4, DR5 with pro-caspases 8 and 10, thereby facilitating caspase activation (e.g., ref. 1, and references therein). It is also known that FADD can recruit other proteins to regulate NFκB and MAPK pathways which in turn can promote proliferation and cell cycle progression. In NSCLC high expression of FADD has been associated with shorter survival times and lymph node metastasis or oral cancer and worse survival, and the present manuscript in head and neck cancer demonstrates similar findings with respect to lymph node metastasis and survival.(2)(,)(3) |
format | Online Article Text |
id | pubmed-3909546 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-39095462014-02-10 FADD the bad in head and neck cancer Dent, Paul Cancer Biol Ther Commentary It has been known for many years that the protein Fas-associated death domain (FADD) is an essential protein forming the apical portion of the extrinsic apoptosis pathway that permits association of death receptors, e.g., CD95, DR4, DR5 with pro-caspases 8 and 10, thereby facilitating caspase activation (e.g., ref. 1, and references therein). It is also known that FADD can recruit other proteins to regulate NFκB and MAPK pathways which in turn can promote proliferation and cell cycle progression. In NSCLC high expression of FADD has been associated with shorter survival times and lymph node metastasis or oral cancer and worse survival, and the present manuscript in head and neck cancer demonstrates similar findings with respect to lymph node metastasis and survival.(2)(,)(3) Landes Bioscience 2013-09-01 2013-08-15 /pmc/articles/PMC3909546/ /pubmed/23974629 http://dx.doi.org/10.4161/cbt.26151 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Commentary Dent, Paul FADD the bad in head and neck cancer |
title | FADD the bad in head and neck cancer |
title_full | FADD the bad in head and neck cancer |
title_fullStr | FADD the bad in head and neck cancer |
title_full_unstemmed | FADD the bad in head and neck cancer |
title_short | FADD the bad in head and neck cancer |
title_sort | fadd the bad in head and neck cancer |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3909546/ https://www.ncbi.nlm.nih.gov/pubmed/23974629 http://dx.doi.org/10.4161/cbt.26151 |
work_keys_str_mv | AT dentpaul faddthebadinheadandneckcancer |