The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability
Open accessAbstract
The folding energetics of the mono-N-glycosylated adhesion domain of the human immune cell receptor cluster of differentiation 2 (hCD2ad) were studied systematically to understand the influence of the N-glycan on the folding energy landscape. Fully elaborated N-glycan structures accelerate folding by 4-fold and stabilize the β-sandwich structure by 3.1 kcal/mol, relative to the nonglycosylated protein. The N-glycan's first saccharide unit accounts for the entire acceleration of folding and for 2/3 of the native state stabilization. The remaining third of the stabilization is derived from the next 2 saccharide units. Thus, the conserved N-linked triose core, ManGlcNAc 2 , improves both the kinetics and the thermodynamics of protein folding. The native state stabilization and decreased activation barrier for folding conferred by N-glycosylation provide a powerful and potentially general mechanism for enhancing folding in the secretory pathway.
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Cites
Intracellular Functions of N-Linked Glycans
Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405
N-linked oligosaccharides as outfitters for glycoprotein folding, form and function
Mitra, N., Sinha, S., Ramya, T. N. C., & Surolia, A. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.01.003 · Cited by 302
An Adaptable Standard for Protein Export from the Endoplasmic Reticulum
Wiseman, R. L., Powers, E. T., Buxbaum, J. N., Kelly, J. W., & Balch, W. E. (2007) · Cell · doi:10.1016/j.cell.2007.10.025 · Cited by 155
Self-citationArulanandam, A. R., Withka, J. M., Wyss, D. F., Wagner, G., Kister, A., Pallai, P., Recny, M. A., & Reinherz, E. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.24.11613 · Cited by 85
Cited by
The endoplasmic reticulum: structure, function and response to cellular signaling
Schwarz, D. S., & Blower, M. D. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2052-6 · Cited by 1,613
Mechanisms and principles of N-linked protein glycosylation
Schwarz, F., & Aebi, M. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.005 · Cited by 695
Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation
Yuzwa, S. A., Shan, X., Macauley, M. S., Clark, T., Skorobogatko, Y., Vosseller, K., & Vocadlo, D. J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.797 · Cited by 611
Prebiotic Peptides: Molecular Hubs in the Origin of Life
Frenkel-Pinter, M., Samanta, M., Ashkenasy, G., & Leman, L. J. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00664 · Cited by 354
N-Linked Protein Glycosylation in the Endoplasmic Reticulum
Breitling, J., & Aebi, M. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013359 · Cited by 332
Metadata
- Authors
- Hanson, S. R., Culyba, E. K., Hsu, T.-L., Wong, C.-H., Kelly, J. W., & Powers, E. T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-03-03
- Volume
- 106
- Issue
- 9
- Pages
- 3131-3136
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1987419931
- Cited by
- 236
- References
- 4
- FWCI
- 4.92
- Type
- journal article
- Language
- en
- Open access
- green
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