Abstract

As the human genome comes close to being completely identified, attention is turning to protein characterization, because the proteins are the substances actually involved in physiological processes, individually, posttranslationally modified and/or as part of complexes. State-of-the-art protein identification is based on mass spectrometric characterization of proteolytic peptides, either through peptide mapping data or through sequence tag data, combined with data base searching. In addition to protein identification, identification of post-translational modifications and sites of modification are extremely important aspects of protein characterization. Phosphorylation of proteins controls basic cellular processes and determination of the state of phosphorylation of a protein and the specific sites of phosphorylation provides important information that can be used for proposing mechanistic hypotheses, as well as for understanding the processes involved. We are actively developing and applying mass spectrometry-based methods for the characterization of phosphoproteins.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Intramural Research (Z01)
Project #
1Z01ES050171-04
Application #
6838404
Study Section
(LSB)
Project Start
Project End
Budget Start
Budget End
Support Year
4
Fiscal Year
2003
Total Cost
Indirect Cost

  Institution

Name
U.S. National Inst of Environ Hlth Scis
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

Terajima, Masahiko; Perdivara, Irina; Sricholpech, Marnisa et al. (2014) Glycosylation and cross-linking in bone type I collagen. J Biol Chem 289:22636-47
Perdivara, Irina; Yamauchi, Mitsuo; Tomer, Kenneth B (2013) Molecular Characterization of Collagen Hydroxylysine O-Glycosylation by Mass Spectrometry: Current Status. Aust J Chem 66:760-769
Perdivara, Irina; Perera, Lalith; Sricholpech, Marnisa et al. (2013) Unusual fragmentation pathways in collagen glycopeptides. J Am Soc Mass Spectrom 24:1072-81
Sricholpech, Marnisa; Perdivara, Irina; Yokoyama, Megumi et al. (2012) Lysyl hydroxylase 3-mediated glucosylation in type I collagen: molecular loci and biological significance. J Biol Chem 287:22998-3009
Perdivara, Irina; Peddada, Shyamal D; Miller, Frederick W et al. (2011) Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes. J Proteome Res 10:2969-78
Merrick, B Alex; Dhungana, Suraj; Williams, Jason G et al. (2011) Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3. Mol Cell Proteomics 10:M110.006007
Deterding, Leesa J; Williams, Jason G; Humble, Margaret M et al. (2011) CD34 Antigen: Determination of Specific Sites of Phosphorylation In Vitro and In Vivo. Int J Mass Spectrom 301:12-21
Gates, Matthew B; Tomer, Kenneth B; Deterding, Leesa J (2010) Comparison of metal and metal oxide media for phosphopeptide enrichment prior to mass spectrometric analyses. J Am Soc Mass Spectrom 21:1649-59
Lardinois, Olivier M; Chatterjee, Saurabh; Mason, Ronald P et al. (2010) Biotinylated analogue of the spin-trap 5,5-dimethyl-1-pyrroline-N-oxide for the detection of low-abundance protein radicals by mass spectrometry. Anal Chem 82:9155-8
Ye, Wenjie; Sangaiah, R; Degen, Diana E et al. (2009) Iminohydantoin lesion induced in DNA by peracids and other epoxidizing oxidants. J Am Chem Soc 131:6114-23

Showing the most recent 10 out of 53 publications