Several methods are used to identify protein phosphorylation sites. We report a novel electrospray-based method for the determination of phosphorylation sites by mass spectrometry, using two different declustering potential values. This method allows one to obtain, with a single liquid chromatography/mass spectrometry (LC/MS) run, the pattern with either the phosphorylated or the unphosphorylated species of a protein tryptic digest, that can be further analyzed by tracing back the origin of each HPO3-deprived form using the capabilities of tandem mass spectrometers
AbstractA procedure for determining the extent of phosphorylation at individual sites of multiply ph...
Tyrosine hydroxylase (TH) is involved in the biosynthesis of catecholamines and is activated by phos...
Protein phosphorylation is a reversible post-translational modification crucial in the control of nu...
Protein phosphorylation - dephosphorylation plays a very important role in signal transduction in bi...
A new, multidimensional electrospray MS-based strategy for phosphopeptide mapping is described which...
A methodology for the rapid and quantitative analysis of phosphorylation sites in proteins is presen...
Phosphopeptides in a complex mixture were identified using conventional triple quadrupole neutral lo...
Since the emergence of proteomics, much attention has been paid to the development of new technologi...
The reversible phosphorylation of proteins plays a major role in many vital cellular processes by mo...
<p>The MS/MS spectra correspond to phosphopeptides with the following mass-to-charge (<i>m/z</i>) ra...
Multisite protein phosphorylation appears to be quite common. Nevertheless our understanding of howm...
<p>Mass spectra and accurate amino acid sequence of the selected protein are analyzed by FindMod too...
ABSTRACT A mechanistic understanding of signaling networks requires identification and analysis of p...
In the present work mass spectrometric approaches are described for the identification of phosphoryl...
This chapter discusses the analysis of the in vivo phosphorylation states of proteins by fast atom b...
AbstractA procedure for determining the extent of phosphorylation at individual sites of multiply ph...
Tyrosine hydroxylase (TH) is involved in the biosynthesis of catecholamines and is activated by phos...
Protein phosphorylation is a reversible post-translational modification crucial in the control of nu...
Protein phosphorylation - dephosphorylation plays a very important role in signal transduction in bi...
A new, multidimensional electrospray MS-based strategy for phosphopeptide mapping is described which...
A methodology for the rapid and quantitative analysis of phosphorylation sites in proteins is presen...
Phosphopeptides in a complex mixture were identified using conventional triple quadrupole neutral lo...
Since the emergence of proteomics, much attention has been paid to the development of new technologi...
The reversible phosphorylation of proteins plays a major role in many vital cellular processes by mo...
<p>The MS/MS spectra correspond to phosphopeptides with the following mass-to-charge (<i>m/z</i>) ra...
Multisite protein phosphorylation appears to be quite common. Nevertheless our understanding of howm...
<p>Mass spectra and accurate amino acid sequence of the selected protein are analyzed by FindMod too...
ABSTRACT A mechanistic understanding of signaling networks requires identification and analysis of p...
In the present work mass spectrometric approaches are described for the identification of phosphoryl...
This chapter discusses the analysis of the in vivo phosphorylation states of proteins by fast atom b...
AbstractA procedure for determining the extent of phosphorylation at individual sites of multiply ph...
Tyrosine hydroxylase (TH) is involved in the biosynthesis of catecholamines and is activated by phos...
Protein phosphorylation is a reversible post-translational modification crucial in the control of nu...