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Front Cover: Comparative gel‐based proteomic analysis of chemically crosslinked complexes in dystrophic skeletal muscle
Author(s) -
Murphy Sandra,
Zweyer Margit,
Mundegar Rustam R.,
Swandulla Dieter,
Ohlendieck Kay
Publication year - 2018
Publication title -
electrophoresis
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201870111
Subject(s) - sarcolemma , skeletal muscle , proteome , cytoskeleton , dystrophin , muscular dystrophy , gene isoform , chemistry , tandem mass spectrometry , front cover , actin , proteomics , biology , biochemistry , anatomy , mass spectrometry , chromatography , cover (algebra) , cell , genetics , gene , mechanical engineering , engineering
DOI: 10.1002/elps.201800028 The cover picture shows the bioanalytical combination of gel electrophoretic shift analysis and chemical cross linking/mass spectrometry (XL/MS) to evaluate proteome‐wide changes in protein interaction patterns in normal wild type versus dystrophic mdx‐4cv skeletal muscle. Contractile fibres were histologically stained using haematoxylin and eosin. The background shows the immunofluorescence microscopical labelling of the dystrophin isoform Dp427‐M in the muscle sarcolemma. The almost complete absence of this membrane cytoskeletal protein is the primary abnormality that causes X‐linked muscular dystrophy.