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The dataset of proteins specifically interacted with activated TICAM-1
The presented data are related with our paper entitled “14-3-3-zeta participates in TLR3-mediated TICAM-1 signal-platform formation” (Funami et al., 2016) [1]. These data show the proteins which specifically bind to the activated (oligomerized) TICAM-1. Fifty-three proteins were identified as specif...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949732/ https://www.ncbi.nlm.nih.gov/pubmed/27508220 http://dx.doi.org/10.1016/j.dib.2016.06.030 |
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author | Funami, Kenji Matsumoto, Misako Oshiumi, Hiroyuki Obuse, Chikashi Seya, Tsukasa |
author_facet | Funami, Kenji Matsumoto, Misako Oshiumi, Hiroyuki Obuse, Chikashi Seya, Tsukasa |
author_sort | Funami, Kenji |
collection | PubMed |
description | The presented data are related with our paper entitled “14-3-3-zeta participates in TLR3-mediated TICAM-1 signal-platform formation” (Funami et al., 2016) [1]. These data show the proteins which specifically bind to the activated (oligomerized) TICAM-1. Fifty-three proteins were identified as specifically interacted with oligomerized TICAM-1. Mutant TICAM-1 cannot form the active oligomer, so the proteins interacted with mutant TICAM-1 are dispensable for TICAM-1-signaling. Among 53 proteins, 14-3-3-zeta specifically interacts with oligomerized TICAM-1 to corroborate TICAM-1 signalosome. |
format | Online Article Text |
id | pubmed-4949732 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-49497322016-08-09 The dataset of proteins specifically interacted with activated TICAM-1 Funami, Kenji Matsumoto, Misako Oshiumi, Hiroyuki Obuse, Chikashi Seya, Tsukasa Data Brief Data Article The presented data are related with our paper entitled “14-3-3-zeta participates in TLR3-mediated TICAM-1 signal-platform formation” (Funami et al., 2016) [1]. These data show the proteins which specifically bind to the activated (oligomerized) TICAM-1. Fifty-three proteins were identified as specifically interacted with oligomerized TICAM-1. Mutant TICAM-1 cannot form the active oligomer, so the proteins interacted with mutant TICAM-1 are dispensable for TICAM-1-signaling. Among 53 proteins, 14-3-3-zeta specifically interacts with oligomerized TICAM-1 to corroborate TICAM-1 signalosome. Elsevier 2016-06-28 /pmc/articles/PMC4949732/ /pubmed/27508220 http://dx.doi.org/10.1016/j.dib.2016.06.030 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Data Article Funami, Kenji Matsumoto, Misako Oshiumi, Hiroyuki Obuse, Chikashi Seya, Tsukasa The dataset of proteins specifically interacted with activated TICAM-1 |
title | The dataset of proteins specifically interacted with activated TICAM-1 |
title_full | The dataset of proteins specifically interacted with activated TICAM-1 |
title_fullStr | The dataset of proteins specifically interacted with activated TICAM-1 |
title_full_unstemmed | The dataset of proteins specifically interacted with activated TICAM-1 |
title_short | The dataset of proteins specifically interacted with activated TICAM-1 |
title_sort | dataset of proteins specifically interacted with activated ticam-1 |
topic | Data Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4949732/ https://www.ncbi.nlm.nih.gov/pubmed/27508220 http://dx.doi.org/10.1016/j.dib.2016.06.030 |
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