The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Amino acid distributions around O-linked glycosylation sites
Open accessAbstract
To study the sequence requirements for addition of O-linked N-acetylgalactosamine to proteins, amino acid distributions around 174 O-glycosylation sites were compared with distributions around non-glycosylated sites. In comparison with non-glycosylated serine and threonine residues, the most prominent feature in the vicinity of O-glycosylated sites is a significantly increased frequency of proline residues, especially at positions -1 and +3 relative to the glycosylated residues. Alanine, serine and threonine are also significantly increased. The high serine and threonine content of O-glycosylated regions is due to the presence of clusters of several closely spaced glycosylated hydroxy amino acids in many O-glycosylated proteins. Such clusters can be predicted from the primary sequence in some cases, but there is no apparent possibility of predicting isolated O-glycosylation sites from primary sequence data.
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Cites
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The human LDL receptor: A cysteine-rich protein with multiple Alu sequences in its mRNA
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Self-citationHuman apolipoprotein E. The complete amino acid sequence
Rall, S. C., Weisgraber, K. H., & Mahley, R. W. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34702-1 · Cited by 741
Conformational preferences of amino acids in globular proteins
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The biochemistry of glycoproteins and proteoglycans
Summers, D. F. (1980) · Cell · doi:10.1016/0092-8674(80)90572-3 · Cited by 639
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The protein identification resource (PIR)
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Cited by
Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
Blom, N., Gammeltoft, S., & Brunak, S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3310 · Cited by 3,188
Blom, N., Sicheritz‐Pontén, T., Gupta, R., Gammeltoft, S., & Brunak, S. (2004) · PROTEOMICS · doi:10.1002/pmic.200300771 · Cited by 2,069
Bennett, E. P., Mandel, U., Clausen, H., Gerken, T. A., Fritz, T. A., & Tabak, L. A. (2012) · Glycobiology · doi:10.1093/glycob/cwr182 · Cited by 876
Julenius, K., Mølgaard, A., Gupta, R., & Brunak, S. (2005) · Glycobiology · doi:10.1093/glycob/cwh151 · Cited by 872
Molecular cloning of CD68, a human macrophage marker related to lysosomal glycoproteins
Holness, C., & Simmons, D. (1993) · Blood · doi:10.1182/blood.v81.6.1607.1607 · Cited by 733
Metadata
- Authors
- Wilson, I. B., Gavel, Y., & von Heijne, G.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1991-04-15
- Volume
- 275
- Issue
- 2
- Pages
- 529-534
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1870828328
- Cited by
- 281
- References
- 54
- FWCI
- 6.47
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Wilson, I. B., Gavel, Y., & von Heijne, G. (1991). Amino acid distributions around O-linked glycosylation sites. Biochemical Journal. https://doi.org/10.1042/bj2750529
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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.
