The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Vertebrate protein glycosylation: diversity, synthesis and function
Open accessAbstract
Protein glycosylation is a ubiquitous post-translational modification found in all domains of life. Despite their significant complexity in animal systems, glycan structures have crucial biological and physiological roles, from contributions in protein folding and quality control to involvement in a large number of biological recognition events. As a result, they impart an additional level of 'information content' to underlying polypeptide structures. Improvements in analytical methodologies for dissecting glycan structural diversity, along with recent developments in biochemical and genetic approaches for studying glycan biosynthesis and catabolism, have provided a greater understanding of the biological contributions of these complex structures in vertebrates.
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Cites
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
Order Out of Chaos: Assembly of Ligand Binding Sites in Heparan Sulfate
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Role of Glycosylation in Development
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Brefeldin A Acts to Stabilize an Abortive ARF–GDP–Sec7 Domain Protein Complex
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Regulation of Notch Signaling by O-Linked Fucose
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Rumi Is a CAP10 Domain Glycosyltransferase that Modifies Notch and Is Required for Notch Signaling
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Cited by
Protein Glycosylation in Cancer
Stowell, S. R., Ju, T., & Cummings, R. D. (2015) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012414-040438 · Cited by 873
Chromatin modifications as determinants of muscle stem cell quiescence and chronological aging
Liu, L., Cheung, T. H., Charville, G. W., Hurgo, B. M. C., Leavitt, T., Shih, J., Brunet, A., & Rando, T. A. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.05.043 · Cited by 544
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
Nanotechnology for protein delivery: Overview and perspectives
Yu, M., Wu, J., Shi, J., & Farokhzad, O. C. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.10.012 · Cited by 410
The Challenge and Promise of Glycomics
Cummings, R. D., & Pierce, J. M. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.12.010 · Cited by 400
Metadata
- Authors
- Moremen, K. W., Tiemeyer, M., & Nairn, A. V.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-06-22
- Volume
- 13
- Issue
- 7
- Pages
- 448-462
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2018042261
- Cited by
- 1,677
- References
- 9
- FWCI
- 4.59
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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