๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Combining Mass Spectrometry and Peptide Arrays to Profile the Specificities of Histone Deacetylases

โœ Scribed by Zachary A. Gurard-Levin; Joohoon Kim; Milan Mrksich


Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
588 KB
Volume
10
Category
Article
ISSN
1439-4227

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Application of mass spectrometry to the
โœ Michael A. Freitas; Amy R. Sklenar; Mark R. Parthun ๐Ÿ“‚ Article ๐Ÿ“… 2004 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 393 KB ๐Ÿ‘ 1 views

## Abstract The core histones are the primary protein component of chromatin, which is responsible for the packaging of eukaryotic DNA. The NH~2~โ€terminal tail domains of the core histones are the sites of numerous postโ€translational modifications that have been shown to play an important role in t

The combined use of enzymatic hydrolysis
โœ R. Self; A. Parente ๐Ÿ“‚ Article ๐Ÿ“… 1983 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 440 KB ๐Ÿ‘ 2 views

Oligopeptides subjected to partial enzyme hydrolysis provide mixtures of sub-peptides which optimize amino acid sequence determination by fast atom bombardment mass spectrometry. The digestion mixture can be sampled directly; there is no interference from the enzyme. Complete sequences were obtained

Application of Liquid Chromatography/Mas
โœ Nana Kawasaki; Miyako Ohta; Sumiko Hyuga; Masashi Hyuga; Takao Hayakawa ๐Ÿ“‚ Article ๐Ÿ“… 2000 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 186 KB

## High -performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) and liquid chromatography with tandem mass spectrometry (LC/MS/MS) were applied to the analysis of the site-specific carbohydrate heterogeneity in erythropoietin (EPO) used as a model of the sialylate

The relative influence of phosphorylatio
โœ Jan Gropengiesser; Balamurugan T. Varadarajan; Heike Stephanowitz; Eberhard Krau ๐Ÿ“‚ Article ๐Ÿ“… 2009 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 171 KB

## Abstract Qualitative and quantitative analysis of postโ€translational protein modifications by mass spectrometry is often hampered by changes in the ionization/detection efficiencies caused by amino acid modifications. This paper reports a comprehensive study of the influence of phosphorylation a