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Global profiling of protein-DNA and protein-nucleosome binding affinities using quantitative mass spectrometry.
Nat. Commun. 9:1653 (2018)
Interaction proteomics studies have provided fundamental insights into multimeric biomolecular assemblies and cell-scale molecular networks. Significant recent developments in mass spectrometry-based interaction proteomics have been fueled by rapid advances in label-free, isotopic, and isobaric quantitation workflows. Here, we report a quantitative protein-DNA and protein-nucleosome binding assay that uses affinity purifications from nuclear extracts coupled with isobaric chemical labeling and mass spectrometry to quantify apparent binding affinities proteome-wide. We use this assay with a variety of DNA and nucleosome baits to quantify apparent binding affinities of monomeric and multimeric transcription factors and chromatin remodeling complexes.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Times Cited
Scopus
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Cited By
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12.353
2.912
26
36
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Special Publikation
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Randomized Controlled-trial; Chronic Tic Disorders; Parkinsons-disease; Health-care; Tourette-syndrome; Behavior-therapy; Neurological Disorders; Huntington Disease; Batten-disease; Virtual Visits
Language
english
Publication Year
2018
HGF-reported in Year
2018
ISSN (print) / ISBN
2041-1723
e-ISSN
2041-1723
Journal
Nature Communications
Quellenangaben
Volume: 9,
Issue: 1,
Article Number: 1653
Publisher
Nature Publishing Group
Publishing Place
London
Reviewing status
Peer reviewed
Institute(s)
Institute of Functional Epigenetics (IFE)
POF-Topic(s)
30203 - Molecular Targets and Therapies
Research field(s)
Helmholtz Diabetes Center
PSP Element(s)
G-502800-001
WOS ID
WOS:000430798100009
Scopus ID
85046093524
PubMed ID
29695722
Erfassungsdatum
2018-07-12