Identification of histidine phosphorylations in proteins using mass spectrometry and affinity-based techniques (Q33289833)

25 July 2017

title

Identification of histidine phosphorylations in proteins using mass spectrometry and affinity-based techniques (English)

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25 July 2017

Andrew R S Ross

1

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25 July 2017

language of work or name

English

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publication date

1 January 2007

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25 July 2017

number of pages

24

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inferred from page(s)

published in

Methods in Enzymology

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25 July 2017

volume

423

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25 July 2017

page(s)

549-572

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describes a project that uses

25 July 2017

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Mass spectrometry-based proteomics

1 reference

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Involvement of the carboxy-terminal residue in the active site of the histidine-containing protein, HPr, of the phosphoenolpyruvate:sugar phosphotransferase system of Escherichia coli

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Metal-affinity separations: a new dimension in protein processing

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Enzyme I of the phosphoenolpyruvate:sugar phosphotransferase system. In vitro intragenic complementation: the roles of Arg126 in phosphoryl transfer and the C-terminal domain in dimerization.

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Phosphoric acid as a matrix additive for MALDI MS analysis of phosphopeptides and phosphoproteins.

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Phosphoproteins analysis in plants: a proteomic approach

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Open tubular immobilized metal ion affinity chromatography combined with MALDI MS and MS/MS for identification of protein phosphorylation sites

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Protein kinases and phosphatases that act on histidine, lysine, or arginine residues in eukaryotic proteins: a possible regulator of the mitogen-activated protein kinase cascade

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The bacterial phosphoenolpyruvate: glycose phosphotransferase system

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Substitution of aspartate and glutamate for active center histidines in the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system maintain phosphotransfer potential.

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Identifiers

DOI

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25 July 2017

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