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Global view of human protein glycosylation pathways and functions
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Citations
Cites
ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES
Kornfeld, R., & Kornfeld, S. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.003215 · Cited by 4,906
Glycosylation in cancer: mechanisms and clinical implications
Pinho, S. S., & Reis, C. A. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3982 · Cited by 3,083
Pan-cancer analysis of whole genomes
The ICGC/TCGA Pan-Cancer Analysis of Whole Genomes Consortium, Aaltonen, L. A., Abascal, F., Abeshouse, A., Aburatani, H., Adams, D. J., Agrawal, N., Ahn, K. S., Ahn, S.-M., Aikata, H., et al. (2020) · Nature · doi:10.1038/s41586-020-1969-6 · Cited by 3,064
Glycosylation in Cellular Mechanisms of Health and Disease
Ohtsubo, K., & Marth, J. D. (2006) · Cell · doi:10.1016/j.cell.2006.08.019 · Cited by 2,788
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
Roles of N-Linked Glycans in the Endoplasmic Reticulum
Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037
Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
Vertebrate protein glycosylation: diversity, synthesis and function
Moremen, K. W., Tiemeyer, M., & Nairn, A. V. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3383 · Cited by 1,677
Newly identified loci that influence lipid concentrations and risk of coronary artery disease
Willer, C. J., Sanna, S., Jackson, A. U., Scuteri, A., Bonnycastle, L. L., Clarke, R., Heath, S. C., Timpson, N. J., Najjar, S. S., Stringham, H. M., et al. (2008) · Nature Genetics · doi:10.1038/ng.76 · Cited by 1,585
Order Out of Chaos: Assembly of Ligand Binding Sites in Heparan Sulfate
Esko, J. D., & Selleck, S. B. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135458 · Cited by 1,495
Research works printed but not linked: 8
- Roch, C., Kuhn, J., Kleesiek, K. & Götting, C. Differences in gene expression of human xylosyltransferases and determination of acceptor specificities for various proteoglycans. Biochem. Biophys. Res. Commun. 391, 685–691 (2010). · doi:10.1016/j.bbrc.2009.11.121
- Tsuji, S., Datta, A. K. & Paulson, J. C. Systematic nomenclature for sialyltransferases. Glycobiology 6, v–vii (1996). · DOI · Paper page
- El Qaidi, S. et al. NleB/SseK effectors from Citrobacter rodentium, Escherichia coli, and Salmonella enterica display distinct differences in host substrate specificity. J. Biol. Chem. 292, 11423–11430 (2017). · doi:10.1074/jbc.m117.790675
- Lee, S. H. et al. Core2 O-glycan structure is essential for the cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV during intestinal cell differentiation. J. Biol. Chem. 285, 37683–37692 (2010). · doi:10.1074/jbc.m110.162735
- Kitada, S. et al. Polypeptide N-acetylgalactosaminyl transferase 3 independently predicts high-grade tumours and poor prognosis in patients with renal cell carcinomas. Br. J. Cancer 109, 472–481 (2013). · doi:10.1038/bjc.2013.331
- Büll, C., Joshi, H. J., Clausen, H. & Narimatsu, Y. Cell-based glycan arrays — a practical guide to dissect the human glycome. STAR Protoc. 1, 100017 (2020). · doi:10.1016/j.xpro.2020.100017
- Naegeli, A. & Aebi, M. Current approaches to engineering N-linked protein glycosylation in bacteria. Methods Mol. Biol. 1321, 3–16 (2015). · doi:10.1007/978-1-4939-2760-9_1
- Ibrahim, A. M. S. et al. Acellular dermal matrices in breast surgery: a comprehensive review. Ann. Plast. Surg. 70, 732–738 (2013). · doi:10.1097/sap.0b013e31824b3d30
Cited by
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
Sies, H., Belousov, V. V., Chandel, N. S., Davies, M. J., Jones, D. P., Mann, G. E., Murphy, M. P., Yamamoto, M., & Winterbourn, C. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00456-z · Cited by 1,735
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
The Multifaceted Biology of PCSK9
Seidah, N. G., & Prat, A. (2022) · Endocrine Reviews · doi:10.1210/endrev/bnab035 · Cited by 232
Understanding the molecular diversity of synapses
van Oostrum, M., & Schuman, E. M. (2025) · Nature Reviews Neuroscience · doi:10.1038/s41583-024-00888-w · Cited by 49
Evolution of high-molecular-mass hyaluronic acid is associated with subterranean lifestyle
Zhao, Y., Zheng, Z., Zhang, Z., Xu, Y., Hillpot, E., Lin, Y. S., Zakusilo, F. T., Lu, J. Y., Ablaeva, J., Biashad, S. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43623-2 · Cited by 34
Metadata
- Authors
- Schjoldager, K. T., Narimatsu, Y., Joshi, H. J., & Clausen, H.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2020-10-21
- Volume
- 21
- Issue
- 12
- Pages
- 729-749
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W3094407181
- Cited by
- 1,309
- References
- 250
- FWCI
- 9.81
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
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- Schjoldager, K. T., Narimatsu, Y., Joshi, H. J., & Clausen, H. (2020). Global view of human protein glycosylation pathways and functions. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/s41580-020-00294-x
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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.
