@article{Molden2014,
	title = {Middle-down and top-down mass spectrometric analysis of co-occurring histone modification},
	issn = {1934-3663},
	url = {http://doi.wiley.com/10.1002/0471140864nhttp://www.ncbi.nlm.nih.gov/pubmed/18429326nhttp://www.ncbi.nlm.nih.gov/pubmed/18429317},
	doi = {10.1002/0471140864},
	abstract = {Histones are chromatin proteins that are highly modified with many different types of post-translational modifications. These modifications act in concert to regulate a number of chromatin-related processes. However, identification and quantification of co-occurring histone post-translational modifications is challenging because there are many potential combinations of modifications and because the commonly used strategy of fragmenting proteins using trypsin or an alternative protease prior to LC-MS/MS analysis results in the loss of connectivity between modifications on different peptides. In this unit, mass spectrometric methods to analyze combinatorial histone modifications on histone tails (middle-down mass spectrometry) and on intact histones (top-down mass spectrometry) are described.},
	number = {78},
	journal = {Current protocols in protein science},
	author = {Molden, Rosalynn C. and Garcia, Benjamin A.},
	year = {2014},
	pmid = {18429317},
	note = {ISBN: 0471140864},
	keywords = {\#nosource},
	pages = {Unit 23.7},
}

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