The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.
Open accessAbstract
The soluble, calcium-binding protein calreticulin shares high sequence homology with calnexin, a transmembrane chaperone of glycoprotein folding. Our experiments demonstrated that calreticulin, like calnexin, associated transiently with numerous newly synthesized proteins in the endoplasmic reticulum. The population of proteins that bound to calreticulin was partially overlapping with those that bound to calnexin. Hemagglutinin (HA) of influenza virus was shown to associate with both calreticulin and calnexin. Using HA as a model substrate, it was found that both calreticulin- and calnexin-bound HA corresponded primarily to incompletely disulfide-bonded folding intermediates and conformationally trapped forms. Binding of all substrates was oligosaccharide-dependent and required the trimming of glucose residues from asparagine-linked core glycans by glucosidases I and II. In vitro, alpha-mannosidase digestion of calreticulin-bound HA indicated that calreticulin was specific for monoglucosylated glycans. Thus, calreticulin appeared to be a lectin with similar oligosaccharide specificity as its membrane-bound homologue, calnexin. Both are therefore likely to play an important role in glycoprotein maturation and quality control in the endoplasmic reticulum.
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Cites
ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES
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Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
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Self-citationHow N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.
Helenius, A. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.3.253 · Cited by 623
Self-citationAssociation of folding intermediates of glycoproteins with calnexin during protein maturation
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Self-citationCalnexin: a membrane-bound chaperone of the endoplasmic reticulum
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Cited by
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
Self-citationAsano, N., Nash, R. J., Molyneux, R. J., & Fleet, G. W. J. (2000) · Tetrahedron: Asymmetry · doi:10.1016/s0957-4166(00)00113-0 · Cited by 1,015
Calreticulin: one protein, one gene, many functions
Michalak, M., Corbett, E. F., Mesaeli, N., Nakamura, K., & Opas, M. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440281 · Cited by 830
Protein Glucosylation and Its Role in Protein Folding
Parodi, A. J. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.69 · Cited by 658
ER chaperone functions during normal and stress conditions
Ma, Y., & Hendershot, L. M. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2003.08.007 · Cited by 440
Metadata
- Authors
- Peterson, J. R., Ora, A., Van, P. N., & Helenius, A.
- Venue
- Molecular Biology of the Cell
- Published
- 1995-09
- Volume
- 6
- Issue
- 9
- Pages
- 1173-1184
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- OpenAlex
- W2051690692
- Cited by
- 275
- References
- 54
- FWCI
- 9.05
- Type
- journal article
- Language
- en
- Open access
- green
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- Peterson, J. R., Ora, A., Van, P. N., & Helenius, A. (1995). Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins. Molecular Biology of the Cell. https://doi.org/10.1091/mbc.6.9.1173
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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.
