Absolute and Site-Specific Quantification of Protein Phosphorylation Using Integrated Elemental and Molecular Mass Spectrometry:  Its Potential To Assess Phosphopeptide Enrichment Procedures

2008 ◽  
Vol 80 (5) ◽  
pp. 1777-1787 ◽  
Author(s):  
Ana Pereira Navaza ◽  
Jorge Ruiz Encinar ◽  
Montserrat Carrascal ◽  
Joaquín Abián ◽  
Alfredo Sanz-Medel
Keyword(s):  
Mass Spectrometry ◽  
Protein Phosphorylation ◽  
Molecular Mass ◽  
Phosphopeptide Enrichment ◽  
Site Specific ◽  
Molecular Mass Spectrometry

scholarly journals Extensive non-canonical phosphorylation in human cells revealed using strong-anion exchange-mediated phosphoproteomics

2017 ◽  
Author(s):  
Gemma Hardman ◽  
Simon Perkins ◽  
Zheng Ruan ◽  
Natarajan Kannan ◽  
Philip Brownridge ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Phosphorylation ◽  
Anion Exchange ◽  
Human Cell ◽  
Cell Biology ◽  
Human Cells ◽  
Phosphopeptide Enrichment ◽  
Cell Extracts ◽  
Strong Anion Exchange ◽  
Acid Labile

Protein phosphorylation is a ubiquitous post-translational modification (PTM) that regulates all aspects of life. To date, investigation of human cell signalling has focussed on canonical phosphorylation of serine (Ser), threonine (Thr) and tyrosine (Tyr) residues. However, mounting evidence suggests that phosphorylation of histidine also plays a central role in regulating cell biology. Phosphoproteomics workflows rely on acidic conditions for phosphopeptide enrichment, which are incompatible with the analysis of acid-labile phosphorylation such as histidine. Consequently, the extent of non-canonical phosphorylation is likely to be under-estimated. We report an Unbiased Phosphopeptide enrichment strategy based on Strong Anion Exchange (SAX) chromatography (UPAX), which permits enrichment of acid-labile phosphopeptides for characterisation by mass spectrometry. Using this approach, we identify extensive and positional phosphorylation patterns on histidine, arginine, lysine, aspartate and glutamate in human cell extracts, including 310 phosphohistidine and >1000 phospholysine sites of protein modification. Remarkably, the extent of phosphorylation on individual non-canonical residues vastly exceeds that of basal phosphotyrosine. Our study reveals the previously unappreciated diversity of protein phosphorylation in human cells, and opens up avenues for exploring roles of acid-labile phosphorylation in any proteome using mass spectrometry.

Use of molecular mass spectrometry in studying composition of dispersion media in lubricating greases

1978 ◽  
Vol 14 (9) ◽  
pp. 699-702
Author(s):  
L. N. Sosulina ◽  
L. I. Nazarova ◽  
E. M. Nikonorov ◽  
T. G. Zubkevich
Keyword(s):  
Mass Spectrometry ◽  
Molecular Mass ◽  
Molecular Mass Spectrometry ◽  
Dispersion Media

Use of elemental and molecular-mass spectrometry to assess the toxicological effects of inorganic mercury in the mouse Mus musculus

2014 ◽  
Vol 406 (24) ◽  
pp. 5853-5865 ◽  
Author(s):  
Miguel Ángel García-Sevillano ◽  
Tamara García-Barrera ◽  
Francisco Navarro ◽  
Jürgen Gailer ◽  
José Luiz Gómez-Ariza
Keyword(s):  
Mass Spectrometry ◽  
Molecular Mass ◽  
Mus Musculus ◽  
Inorganic Mercury ◽  
Toxicological Effects ◽  
Molecular Mass Spectrometry

Atomic (HPLC-ICP-MS) and molecular mass spectrometry (ESI-Q-TOF) to study cis-platin interactions with serum proteins

2008 ◽  
Vol 23 (3) ◽  
pp. 378-384 ◽  
Author(s):  
Diego Esteban-Fernández ◽  
M. Montes-Bayón ◽  
E. Blanco González ◽  
M. M. Gómez Gómez ◽  
M. A. Palacios ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Mass ◽  
Serum Proteins ◽  
Icp Ms ◽  
Molecular Mass Spectrometry

Imaging by Elemental and Molecular Mass Spectrometry Reveals the Uptake of an Arsenolipid in the Brain of Drosophila melanogaster

2016 ◽  
Vol 88 (10) ◽  
pp. 5258-5263 ◽  
Author(s):  
Ann-Christin Niehoff ◽  
Jacqueline Schulz ◽  
Jens Soltwisch ◽  
Sören Meyer ◽  
Hans Kettling ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Drosophila Melanogaster ◽  
Molecular Mass ◽  
Molecular Mass Spectrometry ◽  
The Brain
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