The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
Golgi Glycosylation
Open accessAbstract
Glycosylation is a very common modification of protein and lipid, and most glycosylation reactions occur in the Golgi. Although the transfer of initial sugar(s) to glycoproteins or glycolipids occurs in the ER or on the ER membrane, the subsequent addition of the many different sugars that make up a mature glycan is accomplished in the Golgi. Golgi membranes are studded with glycosyltransferases, glycosidases, and nucleotide sugar transporters arrayed in a generally ordered manner from the cis-Golgi to the trans-Golgi network (TGN), such that each activity is able to act on specific substrate(s) generated earlier in the pathway. The spectrum of glycosyltransferases and other activities that effect glycosylation may vary with cell type, and thus the final complement of glycans on glycoconjugates is variable. In addition, glycan synthesis is affected by Golgi pH, the integrity of Golgi peripheral membrane proteins, growth factor signaling, Golgi membrane dynamics, and cellular stress. Knowledge of Golgi glycosylation has fostered the development of assays to identify mechanisms of intracellular vesicular trafficking and facilitated glycosylation engineering of recombinant glycoproteins.
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Cites
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
Cantarel, B. L., Coutinho, P. M., Rancurel, C., Bernard, T., Lombard, V., & Henrissat, B. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn663 · Cited by 5,972
Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints
Zielinska, D. F., Gnad, F., Wiśniewski, J. R., & Mann, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.012 · Cited by 902
Fringe is a glycosyltransferase that modifies Notch
Moloney, D. J., Panin, V. M., Johnston, S. H., Chen, J., Shao, L., Wilson, R., Wang, Y., Stanley, P., Irvine, K. D., Haltiwanger, R. S., et al. (2000) · Nature · doi:10.1038/35019000 · Cited by 852
Self-citationAn evolving view of the eukaryotic oligosaccharyltransferase
Kelleher, D. J., & Gilmore, R. (2006) · Glycobiology · doi:10.1093/glycob/cwj066 · Cited by 528
Ju, T., & Cummings, R. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262438199 · Cited by 487
Longman, C. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg307 · Cited by 416
An investigation of the role of transmembrane domains in Golgi protein retention.
Munro, S. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00151.x · Cited by 391
Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides
Rabouille, C., Hui, N., Hunte, F., Kieckbusch, R., Berger, E. G., Warren, G., & Nilsson, T. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.4.1617 · Cited by 365
Rumi Is a CAP10 Domain Glycosyltransferase that Modifies Notch and Is Required for Notch Signaling
Acar, M., Jafar-Nejad, H., Takeuchi, H., Rajan, A., Ibrani, D., Rana, N. A., Pan, H., Haltiwanger, R. S., & Bellen, H. J. (2008) · Cell · doi:10.1016/j.cell.2007.12.016 · Cited by 306
Protein quality control in the ER: The recognition of misfolded proteins
Määttänen, P., Gehring, K., Bergeron, J. J. M., & Thomas, D. Y. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2010.03.006 · Cited by 284
Cited by
Glycosylation in health and disease
Reily, C., Stewart, T. J., Renfrow, M. B., & Novak, J. (2019) · Nature Reviews Nephrology · doi:10.1038/s41581-019-0129-4 · Cited by 2,075
Precision mapping of the human O‐GalNAc glycoproteome through SimpleCell technology
Steentoft, C., Vakhrushev, S. Y., Joshi, H. J., Kong, Y., Vester‐Christensen, M. B., Schjoldager, K. T. G., Lavrsen, K., Dabelsteen, S., Pedersen, N. B., Marcos‐Silva, L., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.79 · Cited by 1,408
Suppression of Exosomal PD-L1 Induces Systemic Anti-tumor Immunity and Memory
Poggio, M., Hu, T., Pai, C.-C., Chu, B., Belair, C. D., Chang, A., Montabana, E., Lang, U. E., Fu, Q., Fong, L., et al. (2019) · Cell · doi:10.1016/j.cell.2019.02.016 · Cited by 1,376
Glycosylation: mechanisms, biological functions and clinical implications
He, M., Zhou, X., & Wang, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01886-1 · Cited by 499
Golgi Bypass: Skirting Around the Heart of Classical Secretion
Grieve, A. G., & Rabouille, C. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005298 · Cited by 357
Metadata
- Authors
- Stanley, P.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-03-02
- Volume
- 3
- Issue
- 4
- Pages
- a005199-a005199
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W4245814297
- Cited by
- 455
- References
- 70
- Type
- posted content
- Language
- en
- Open access
- bronze
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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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