The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
A New Strategy for Identification of N-Glycosylated Proteins and Unambiguous Assignment of Their Glycosylation Sites Using HILIC Enrichment and Partial Deglycosylation
Abstract
Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site. In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96). After hydrolysis with these enzymes, a single N-acetylglucosamine (GlcNAc) residue remains linked to the asparagine residue. The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence. We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
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
Anderson, N. L., & Anderson, N. G. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r200007-mcp200 · Cited by 4,414
Cited by
Protein Analysis by Shotgun/Bottom-up Proteomics
Zhang, Y., Fonslow, B. R., Shan, B., Baek, M.-C., & Yates, J. R. (2013) · Chemical Reviews · doi:10.1021/cr3003533 · Cited by 1,491
Interpreting the protein language using proteomics
Jensen, O. N. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1939 · Cited by 502
Self-citationMass spectrometry approaches to glycomic and glycoproteomic analyses
Ruhaak, L. R., Xu, G., Li, Q., Goonatilleke, E., & Lebrilla, C. B. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00732 · Cited by 395
Zhao, Y., & Jensen, O. N. (2009) · PROTEOMICS · doi:10.1002/pmic.200900398 · Cited by 384
Self-citationHigh-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
Alley, W. R., Mann, B. F., & Novotny, M. V. (2013) · Chemical Reviews · doi:10.1021/cr3003714 · Cited by 310
Determination of glycosylation sites and site-specific heterogeneity in glycoproteins
An, H. J., Froehlich, J. W., & Lebrilla, C. B. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.07.022 · Cited by 280
Gu, Y., Liu, Y., Fu, L., Zhai, L., Zhu, J., Han, Y., Jiang, Y., Zhang, Y., Zhang, P., Jiang, Z., et al. (2019) · Nature Medicine · doi:10.1038/s41591-018-0309-y · Cited by 266
Mucin‐type O‐glycosylation – putting the pieces together
Jensen, P. H., Kolarich, D., & Packer, N. H. (2010) · The FEBS Journal · doi:10.1111/j.1742-4658.2009.07429.x · Cited by 252
Glycoproteomics: A Balance between High-Throughput and In-Depth Analysis
Yang, Y., Franc, V., & Heck, A. J. R. (2017) · Trends in Biotechnology · doi:10.1016/j.tibtech.2017.04.010 · Cited by 122
Ahmad Izaham, A. R., Ang, C.-S., Nie, S., Bird, L. E., Williamson, N. A., & Scott, N. E. (2021) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00565 · Cited by 62
Hoffman, M. D., Walsh, G. M., Rogalski, J. C., & Kast, J. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800230-mcp200 · Cited by 41
Metadata
- Authors
- Hägglund, P., Bunkenborg, J., Elortza, F., Jensen, O. N., & Roepstorff, P.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2004-04-10
- Volume
- 3
- Issue
- 3
- Pages
- 556-566
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- OpenAlex
- W2066144238
- Cited by
- 460
- References
- 1
- FWCI
- 6.67
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.