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Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes

We provide detailed datasets from our analysis of proteins that are identified in human liver, lung, kidney and intestine microsomes by MS-based proteomics. Also included is a set of CYP450 enzymes and microsomal glutathione-S-transferase (MGSTs) activities in human liver microsomes. The data presen...

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Detalles Bibliográficos
Autores principales: Song, Wei, Yu, Longjiang, Peng, Zhihong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996730/
https://www.ncbi.nlm.nih.gov/pubmed/29900246
http://dx.doi.org/10.1016/j.dib.2018.03.124
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author Song, Wei
Yu, Longjiang
Peng, Zhihong
author_facet Song, Wei
Yu, Longjiang
Peng, Zhihong
author_sort Song, Wei
collection PubMed
description We provide detailed datasets from our analysis of proteins that are identified in human liver, lung, kidney and intestine microsomes by MS-based proteomics. Also included is a set of CYP450 enzymes and microsomal glutathione-S-transferase (MGSTs) activities in human liver microsomes. The data presented in this paper support the research article “Targeted label-free approach for quantification of epoxide hydrolase and glutathione transferases in microsomes” (Song et al., 2015) [1]. We expect that the data will contribute to the study of metabolism enzymes.
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spelling pubmed-59967302018-06-13 Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes Song, Wei Yu, Longjiang Peng, Zhihong Data Brief Proteomics and Biochemistry    We provide detailed datasets from our analysis of proteins that are identified in human liver, lung, kidney and intestine microsomes by MS-based proteomics. Also included is a set of CYP450 enzymes and microsomal glutathione-S-transferase (MGSTs) activities in human liver microsomes. The data presented in this paper support the research article “Targeted label-free approach for quantification of epoxide hydrolase and glutathione transferases in microsomes” (Song et al., 2015) [1]. We expect that the data will contribute to the study of metabolism enzymes. Elsevier 2018-03-30 /pmc/articles/PMC5996730/ /pubmed/29900246 http://dx.doi.org/10.1016/j.dib.2018.03.124 Text en © 2018 The Authors. Published by Elsevier Inc. 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 Proteomics and Biochemistry   
Song, Wei
Yu, Longjiang
Peng, Zhihong
Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
title Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
title_full Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
title_fullStr Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
title_full_unstemmed Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
title_short Dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
title_sort dataset from proteomic analysis of human liver, lung, kidney and intestine microsomes
topic Proteomics and Biochemistry   
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996730/
https://www.ncbi.nlm.nih.gov/pubmed/29900246
http://dx.doi.org/10.1016/j.dib.2018.03.124
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