The DOI matches its Crossref record; 235 of the 235 references it cites were found in a registry or an index.
Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease
Open accessAbstract
O-GlcNAcylation is the addition of β-D-N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not discovered until the early 1980s and still remains difficult to detect and quantify. Nonetheless, O-GlcNAc is highly abundant and cycles on proteins with a timescale similar to protein phosphorylation. O-GlcNAc occurs in organisms ranging from some bacteria to protozoans and metazoans, including plants and nematodes up the evolutionary tree to man. O-GlcNAcylation is mostly on nuclear proteins, but it occurs in all intracellular compartments, including mitochondria. Recent glycomic analyses have shown that O-GlcNAcylation has surprisingly extensive cross talk with phosphorylation, where it serves as a nutrient/stress sensor to modulate signaling, transcription, and cytoskeletal functions. Abnormal amounts of O-GlcNAcylation underlie the etiology of insulin resistance and glucose toxicity in diabetes, and this type of modification plays a direct role in neurodegenerative disease. Many oncogenic proteins and tumor suppressor proteins are also regulated by O-GlcNAcylation. Current data justify extensive efforts toward a better understanding of this invisible, yet abundant, modification. As tools for the study of O-GlcNAc become more facile and available, exponential growth in this area of research will eventually take place.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“there seems to be a limited number of forms of intracellular glycosylation, with a single modi fi cation ( O -GlcNAc) numerically dominating the scene (647 -648).”
From Biological roles of glycans (2017) · cites this paper as [648]
Experimental — accuracy not yet measured
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
The protein kinase complement of the human genome
Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
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
Cycling of O-linked β-N-acetylglucosamine on nucleocytoplasmic proteins
Hart, G. W., Housley, M. P., & Slawson, C. (2007) · Nature · doi:10.1038/nature05815 · Cited by 1,418
Self-citationLarge-scale characterization of HeLa cell nuclear phosphoproteins
Beausoleil, S. A., Jedrychowski, M. P., Schwartz, D., Elias, J. E., Villén, J., Li, J., Cohn, M. A., Cantley, L. C., & Gygi, S. P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404720101 · Cited by 1,376
Du, X.-L., Edelstein, D., Rossetti, L., Fantus, I. G., Goldberg, H. J., Ziyadeh, F. N., Wu, J., & Brownlee, M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.22.12222 · Cited by 1,152
Torres, C., & Hart, G. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43295-9 · Cited by 1,132
Self-citationMarshall, S., Bacote, V., & Traxinger, R. R. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67706-9 · Cited by 1,049
Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc
Wells, L., Vosseller, K., & Hart, G. W. (2001) · Science · doi:10.1126/science.1058714 · Cited by 959
Self-citationProtein phosphatase 1 – targeted in many directions
Cohen, P. T. W. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.241 · Cited by 922
Research works printed but not linked: 12
- 10.1074/mcp.M400024-MCP200 · DOI
- 10.1074/jbc.M806199200 · DOI
- 10.1074/jbc.M808890200 · DOI
- Zachara NE, 2004, Methods Mol. Biol., 284, 175
- Greis KD, 1998, Methods Mol. Biol., 76, 19
- 10.1126/scisignal.2000526 · DOI
- Omary MB, 1998, Subcell. Biochem., 31, 105
- 10.1074/jbc.M406481200 · DOI
- 10.1161/CIRCRESAHA.108.184978 · DOI · Paper page
- 10.1210/en.140.3.1151 · DOI
- Kroner Z., 2009, Altern. Med. Rev., 14, 373
- 10.1074/jbc.271.46.28741 · DOI · Paper page
Cited by
Sorted by citations
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Identification of bioactive metabolites using activity metabolomics
Rinschen, M. M., Ivanisevic, J., Giera, M., & Siuzdak, G. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0108-4 · Cited by 1,008
TETonic shift: biological roles of TET proteins in DNA demethylation and transcription
Pastor, W. A., Aravind, L., & Rao, A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3589 · Cited by 897
Ruan, H.-B., Han, X., Li, M.-D., Singh, J. P., Qian, K., Azarhoush, S., Zhao, L., Bennett, A. M., Samuel, V. T., Wu, J., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.07.006 · Cited by 296
Phosphoproteomics in the Age of Rapid and Deep Proteome Profiling
Riley, N. M., & Coon, J. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04123 · Cited by 265
Metadata
- Authors
- Hart, G. W., Slawson, C., Ramirez-Correa, G., & Lagerlof, O.
- Affiliations
- Johns Hopkins University (US)
- Departments of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205;, cslawso1@jhmi.edu, gramire2@jhmi.edu, olof.lagerlof@gmail.com
- Departments of Biological Chemistry and Pediatrics, Johns Hopkins University, School of Medicine, Baltimore, Maryland 21205;
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2011-07-07
- Volume
- 80
- Issue
- 1
- Pages
- 825-858
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- PMC
- PMC3294376
- OpenAlex
- W2140409722
- Cited by
- 1,317
- References
- 235
- Citations by year
- 2026: 65 · 2025: 75 · 2024: 88 · 2023: 73 · 2022: 92 · 2021: 121 · 2020: 83 · 2019: 78 · 2018: 90 · 2017: 87 · 2016: 88 · 2015: 91 · 2014: 122 · 2013: 95 · 2012: 53
- FWCI
- 8.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- ScholarWorks @ UTRGV (The University of Texas Rio Grande Valley) (submittedVersion)
- Funders
- National Institutes of Health (4r33dk071280-03)
- National Cancer Institute (R01CA42486, R01CA042486)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK061671, R33-DK-071280, R24DK084949, P30DK079637, R33 DK071280-04, R01-DK61671)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R37HD013563)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- O-GlcNAcylation, protein phosphorylation, post-translational modification, O-GlcNAc transferase, O-GlcNAcase, protein glycosylation, nutrient sensing, stress sensing, signal transduction, transcriptional regulation, cytoskeleton, mitochondria, insulin resistance, glucotoxicity, diabetes mellitus, neurodegenerative diseases, oncoprotein, tumor suppressor proteins, chronic disease
- MeSH terms
- Acetylglucosamine, Animals, Chronic Disease, Diabetes Mellitus, Glycosylation, Humans, Models, Molecular, Neoplasms, Phosphorylation, Protein Conformation, Transcription, Genetic, Molecular Structure, Signal Transduction, N-Acetylglucosaminyltransferases, Neurodegenerative Diseases
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
