The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Analysis of Posttranslational Modifications of Proteins by Tandem Mass Spectrometry: Mass Spectrometry For Proteomics Analysis
Open accessAbstract
Protein activity and turnover is tightly and dynamically regulated in living cells. Whereas the three-dimensional protein structure is predominantly determined by the amino acid sequence, posttranslational modification (PTM) of proteins modulates their molecular function and the spatial-temporal distribution in cells and tissues. Most PTMs can be detected by protein and peptide analysis by mass spectrometry (MS), either as a mass increment or a mass deficit relative to the nascent unmodified protein. Tandem mass spectrometry (MS/MS) provides a series of analytical features that are highly useful for the characterization of modified proteins via amino acid sequencing and specific detection of posttranslationally modified amino acid residues. Large-scale, quantitative analysis of proteins by MS/MS is beginning to reveal novel patterns and functions of PTMs in cellular signaling networks and biomolecular structures.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Electrospray Ionization for Mass Spectrometry of Large Biomolecules
Fenn, J. B., Mann, M., Meng, C. K., Wong, S. F., & Whitehouse, C. M. (1989) · Science · doi:10.1126/science.2675315 · Cited by 7,634
Mass spectrometry-based proteomics
Aebersold, R., & Mann, M. (2003) · Nature · doi:10.1038/nature01511 · Cited by 6,955
Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B., Parker, K., Hattan, S., Khainovski, N., Pillai, S., Dey, S., Daniels, S., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400129-mcp200 · Cited by 4,401
Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370
Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., & Gygi, S. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832254100 · Cited by 1,733
Proteomic Analysis of in Vivo Phosphorylated Synaptic Proteins
Collins, M. O., Yu, L., Coba, M. P., Husi, H., Campuzano, I., Blackstock, W. P., Choudhary, J. S., & Grant, S. G. N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411220200 · Cited by 320
Weighing in on ubiquitin: the expanding role of mass-spectrometry-based proteomics
Kirkpatrick, D. S., Denison, C., & Gygi, S. P. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-750 · Cited by 209
Cited by
Post-translational modifications in proteins: resources, tools and prediction methods
Ramazi, S., & Zahiri, J. (2021) · Database · doi:10.1093/database/baab012 · Cited by 772
Analysis of protein carbonylation — pitfalls and promise in commonly used methods
Rogowska-Wrzesinska, A., Wojdyla, K., Nedić, O., Baron, C. P., & Griffiths, H. R. (2014) · Free Radical Research · doi:10.3109/10715762.2014.944868 · Cited by 65
Allgoewer, K., Wu, S., Choi, H., & Vogel, C. (2023) · Molecular Omics · doi:10.1039/d2mo00258b · Cited by 5
Metadata
- Authors
- Larsen, M. R., Trelle, M. B., Thingholm, T. E., & Jensen, O. N.
- Venue
- BioTechniques
- Publisher
- Informa UK Limited
- Published
- 2006-06
- Volume
- 40
- Issue
- 6
- Pages
- 790-798
- ISSN
- 0736-6205 (ISSN-L)
- 1940-9818
- OpenAlex
- W2132500972
- Cited by
- 251
- References
- 7
- FWCI
- 4.88
- Type
- journal article
- Language
- en
- Open access
- gold
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Analysis of Posttranslational Modifications of Proteins by Tandem Mass Spectrometry: Mass Spectrometry For Proteomics Analysis. https://app.cochat.ai/papers/10.2144/000112201
- The paper
- Larsen, M. R., Trelle, M. B., Thingholm, T. E., & Jensen, O. N. (2006). Analysis of Posttranslational Modifications of Proteins by Tandem Mass Spectrometry: Mass Spectrometry For Proteomics Analysis. BioTechniques. https://doi.org/10.2144/000112201
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
