Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle
The proteomic data presented in this article provide supporting information to the related research article ''Proteomic analysis of the sarcolemma-enriched fraction from dystrophic mdx-4cv skeletal muscle'' (Murphy et al., 2018) [1]. In the associated research article, the sarcol...
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doaj-686337b532d44df898f90643bea1a5d32020-11-25T01:17:50ZengElsevierData in Brief2352-34092018-04-0117980993Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscleSandra Murphy0Margit Zweyer1Michael Henry2Paula Meleady3Rustam R. Mundegar4Dieter Swandulla5Kay Ohlendieck6Department of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, IrelandInstitute of Physiology II, University of Bonn, D-53115 Bonn, GermanyNational Institute for Cellular Biotechnology, Dublin City University, Dublin 9, IrelandNational Institute for Cellular Biotechnology, Dublin City University, Dublin 9, IrelandInstitute of Physiology II, University of Bonn, D-53115 Bonn, GermanyInstitute of Physiology II, University of Bonn, D-53115 Bonn, GermanyDepartment of Biology, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland; Corresponding author.The proteomic data presented in this article provide supporting information to the related research article ''Proteomic analysis of the sarcolemma-enriched fraction from dystrophic mdx-4cv skeletal muscle'' (Murphy et al., 2018) [1]. In the associated research article, the sarcolemma from normal versus dystrophic skeletal muscle was analyzed by mass spectrometry-based proteomics. Sarcolemma vesicles were enriched by a lectin agglutination method and then analyzed by liquid chromatography tandem mass spectrometry. Here we provide additional datasets on proteins with decreased versus increased abundance in dystrophin-deficient muscle plasma membranes.http://www.sciencedirect.com/science/article/pii/S2352340918301367 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Sandra Murphy Margit Zweyer Michael Henry Paula Meleady Rustam R. Mundegar Dieter Swandulla Kay Ohlendieck |
spellingShingle |
Sandra Murphy Margit Zweyer Michael Henry Paula Meleady Rustam R. Mundegar Dieter Swandulla Kay Ohlendieck Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle Data in Brief |
author_facet |
Sandra Murphy Margit Zweyer Michael Henry Paula Meleady Rustam R. Mundegar Dieter Swandulla Kay Ohlendieck |
author_sort |
Sandra Murphy |
title |
Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle |
title_short |
Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle |
title_full |
Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle |
title_fullStr |
Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle |
title_full_unstemmed |
Subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle |
title_sort |
subproteomic profiling of sarcolemma from dystrophic mdx-4cv skeletal muscle |
publisher |
Elsevier |
series |
Data in Brief |
issn |
2352-3409 |
publishDate |
2018-04-01 |
description |
The proteomic data presented in this article provide supporting information to the related research article ''Proteomic analysis of the sarcolemma-enriched fraction from dystrophic mdx-4cv skeletal muscle'' (Murphy et al., 2018) [1]. In the associated research article, the sarcolemma from normal versus dystrophic skeletal muscle was analyzed by mass spectrometry-based proteomics. Sarcolemma vesicles were enriched by a lectin agglutination method and then analyzed by liquid chromatography tandem mass spectrometry. Here we provide additional datasets on proteins with decreased versus increased abundance in dystrophin-deficient muscle plasma membranes. |
url |
http://www.sciencedirect.com/science/article/pii/S2352340918301367 |
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