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Items: 5

1.

Quantitative comparison of IMAC and TiO2 surfaces used in the study of regulated, dynamic protein phosphorylation.

Liang X, Fonnum G, Hajivandi M, Stene T, Kjus NH, Ragnhildstveit E, Amshey JW, Predki P, Pope RM.

J Am Soc Mass Spectrom. 2007 Nov;18(11):1932-44. Epub 2007 Aug 14.

2.

Quantitative analysis of global phosphorylation changes with high-resolution tandem mass spectrometry and stable isotopic labeling.

Kweon HK, Andrews PC.

Methods. 2013 Jun 15;61(3):251-9. doi: 10.1016/j.ymeth.2013.04.010. Epub 2013 Apr 21. Review.

3.

Phosphoproteomics by mass spectrometry and classical protein chemistry approaches.

Salih E.

Mass Spectrom Rev. 2005 Nov-Dec;24(6):828-46. Review.

PMID:
15538747
4.

Hydrophilic interaction chromatography for fractionation and enrichment of the phosphoproteome.

McNulty DE, Annan RS.

Methods Mol Biol. 2009;527:93-105, x. doi: 10.1007/978-1-60327-834-8_8. Review.

PMID:
19241008
5.

Versatile nanocomposites in phosphoproteomics: a review.

Najam-ul-Haq M, Jabeen F, Hussain D, Saeed A, Musharraf SG, Huck CW, Bonn GK.

Anal Chim Acta. 2012 Oct 17;747:7-18. doi: 10.1016/j.aca.2012.08.004. Epub 2012 Aug 21. Review.

PMID:
22986130
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