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Cited by 296

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

Enzymatic conversion of proteins to glycoproteins.

Open access
Pless, D D, Lennarz, W J·1977·Proceedings of the National Academy of Sciences

Abstract

The enzymatic transfer of the oligosaccharide moiety from an oligosaccharide-lipid to denatured forms of three secretory proteins--ovalbumin, alpha-lactalbumin, and ribonuclease A--has been demonstrated utilizing a membrane fraction from hen oviduct. Based on a survey of 10 proteins denatured by sulfitolysis, the presence of the tripeptide sequence -Asn-X-Thr-Ser- (X represents a variable amino acid) appears to be necessary but not sufficient for the protein to serve as acceptor in vitro. The results of this investigation also suggest that unfolding of the polypeptide chain is required in order to expose sites for carbohydrate attachment.

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Crossref · 10.1073/pnas.74.1.134

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Metadata

Authors
Pless, D. D., & Lennarz, W. J.
Venue
Proceedings of the National Academy of Sciences
Published
1977-01
Volume
74
Issue
1
Pages
134-138
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2030070992
Cited by
296
References
19
FWCI
8.29
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Enzymatic conversion of proteins to glycoproteins. https://app.cochat.ai/papers/10.1073/pnas.74.1.134
The paper
Pless, D. D., & Lennarz, W. J. (1977). Enzymatic conversion of proteins to glycoproteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.74.1.134

Data sources

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.