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
Items 201–235 of 235
Regulation of a COPII component by cytosolic O‐glycosylation during mitosis
Dudognon, P., Maeder-Garavaglia, C., Carpentier, J., & Paccaud, J. (2004) · FEBS Letters · doi:10.1016/s0014-5793(04)00109-7 · Cited by 61
Banerjee, S., Robbins, P. W., & Samuelson, J. C. (2008) · Glycobiology · doi:10.1093/glycob/cwn107 · Cited by 61
Sensory experience and the formation of a computational map of auditory space in the brain
King, A. J. (1999) · BioEssays · doi:10.1002/(sici)1521-1878(199911)21:11 · Cited by 61
Skorobogatko, Y. V., Deuso, J., Adolf-Bergfoyle, J., Nowak, M. G., Gong, Y., Lippa, C. F., & Vosseller, K. (2010) · Amino Acids · doi:10.1007/s00726-010-0645-9 · Cited by 60
Yao, P. J., & Coleman, P. D. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00547-3 · Cited by 57
Post‐translational modification by O‐GlcNAc: Another way to change protein function
Kudlow, J. E. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20926 · Cited by 57
The cytoskeletal protein talin is O-glycosylated.
Hagmann, J., Grob, M., & Burger, M. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49729-9 · Cited by 54
The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc
Wells, L., Slawson, C. M., & Hart, G. W. (2010) · Amino Acids · doi:10.1007/s00726-010-0709-x · Cited by 54
Self-citationSchultz, J., & Pils, B. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03322-7 · Cited by 53
Ataxin-10 Interacts with O-Linked β-N-Acetylglucosamine Transferase in the Brain
März, P., Stetefeld, J., Bendfeldt, K., Nitsch, C., Reinstein, J., Shoeman, R. L., Dimitriades‐Schmutz, B., Schwager, M., Leiser, D., Özcan, S., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601563200 · Cited by 49
Wu, W., Pasternack, L. B., Huang, D., Koeller, K. M., Lin, C., Seitz, O., & Wong, C. (1999) · Journal of the American Chemical Society · doi:10.1021/ja983474v · Cited by 48
O-Linked N -Acetylglucosaminylation of Sp1 Inhibits the Human Immunodeficiency Virus Type 1 Promoter
Jochmann, R., Thurau, M., Jung, S., Hofmann, C., Naschberger, E., Kremmer, E., Harrer, T., Miller, M., Schaft, N., & Stürzl, M. (2009) · Journal of Virology · doi:10.1128/jvi.01384-08 · Cited by 48
Robles‐Flores, M., Meléndez, L., García, W., et al. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.07.011 · Cited by 44
Identification of O‐GlcNAc Sites on Proteins
Whelan, S. A., & Hart, G. W. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)15008-9 · Cited by 43
Self-citationPlakoglobin Is O-Glycosylated Close to the N-terminal Destruction Box
Hatsell, S. J., Medina, L., Merola, J., Haltiwanger, R. S., & Cowin, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301346200 · Cited by 40
O‐Linked GlcNAc in serotype‐2 adenovirus fibre
Caillet‐Boudin, M., Strecker, G., & Michalski, J. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15008.x · Cited by 40
Regulation of Dauer Formation by O-GlcNAcylation in Caenorhabditis elegans
Lee, J., Kim, K.-Y., Lee, J., & Paik, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.022665 · Cited by 38
Regulation of the Inositol 1,4,5-Trisphosphate Receptor Type I by O -GlcNAc Glycosylation
Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., & Ehrlich, B. E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2069-07.2007 · Cited by 38
THE BIOSYNTHESIS OF HYALURONIC ACID BY GROUP A STREPTOCOCCUS
Dorfman, A., Roseman, S., Moses, F. E., et al. (1955) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70995-2 · Cited by 38
Elevation of nucleocytoplasmic β-N-acetylglucosaminidase (O-GlcNAcase) activity in thyroid cancers
Krześlak, A. (2010) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000387 · Cited by 37
The tumor suppressor HIC1 (hypermethylated in cancer 1) is O ‐GlcNAc glycosylated
Lefebvre, T., Pinte, S., Guérardel, C., Deltour, S., Martin, N., Slomianny, M., Michalski, J., & Leprince, D. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04316.x · Cited by 35
Hu, P., Berkowitz, P., Madden, V. J., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511702200 · Cited by 35
Tuning the conformation properties of a peptide by glycosylation and phosphorylation
Liang, F., Chen, R. P. ‐., Lin, C., Huang, K., & Chan, S. I. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.168 · Cited by 35
O-GlcNAc level variations are associated with the development of skeletal muscle atrophy
Cieniewski‐Bernard, C., Mounier, Y., Michalski, J., & Bastide, B. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00865.2005 · Cited by 35
Detection and Analysis of Proteins Modified by O‐Linked N‐Acetylglucosamine
Zachara, N. E., Cole, R. N., Hart, G. W., et al. (2001) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps1208s25 · Cited by 35
Self-citationComprehensive glycan analysis of recombinant Aspergillus niger endo-polygalacturonase C
Woosley, B. D., Xie, M., Wells, L., Orlando, R., Garrison, D., King, D. A., & Bergmann, C. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.02.002 · Cited by 33
Matthews, J. A., Acevedo-Duncan, M. E., & Potter, R. L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.11.001 · Cited by 32
Analytical Methods for the Study of O-GlcNAc Glycoproteins and Glycopeptides
Greis, K. D., & Hart, G. W. (2003) · Humana Press eBooks · doi:10.1385/0-89603-355-4:19 · Cited by 30
Self-citationIsolation and further characterization of bovine brain hexosaminidase C
Overdijk, B., Kroef, W. M. J. V. D., Steijn, G. J. V., et al. (1981) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(81)90052-8 · Cited by 29
Inhibition of phospholipase C‐β1‐mediated signaling by O‐GlcNAc modification
Kim, Y. H., Song, M., Oh, Y., Heo, K., Choi, J., Park, J., Kim, S., Lim, S., Kwon, H.-W., Ryu, S. H., et al. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20609 · Cited by 26
Nucleocytoplasmic Glycosylation, O-GlcNAc: Identification and Site Mapping
Zachara, N. E., Cheung, W. D., & Hart, G. W. (2004) · Humana Press eBooks · doi:10.1385/1-59259-816-1:175 · Cited by 26
Self-citationO-GlcNAcylation, an original modulator of contractile activity in striated muscle
Cieniewski‐Bernard, C., Montel, V., Stevens, L., & Bastide, B. (2009) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-010-9201-1 · Cited by 23
High-sensitivity FAB-MS strategies for O-GlcNAc characterization
Reason, A. J., Blench, I., Haltiwanger, R. S., et al. (1991) · Glycobiology · doi:10.1093/glycob/1.6.585 · Cited by 20
Jones, S. P. (2005) · Circulation Research · doi:10.1161/01.res.0000168039.61228.67 · Cited by 13
Fine-Tuning ER-β Structure with PTMs
Hart, G. W., & Sakabe, K. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.09.001 · Cited by 7
Self-citation
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
