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Cited by 600

The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.

The Glycosylphosphatidylinositol Anchor: A Complex Membrane-Anchoring Structure for Proteins

Open access
Paulick, Margot G., Bertozzi, Carolyn R.·2008·Biochemistry
DOI 10.1021/bi8006324
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Abstract

Positioned at the C-terminus of many eukaryotic proteins, the glycosylphosphatidylinositol (GPI) anchor is a posttranslational modification that anchors the modified protein in the outer leaflet of the cell membrane. The GPI anchor is a complex structure comprising a phosphoethanolamine linker, glycan core, and phospholipid tail. GPI-anchored proteins are structurally and functionally diverse and play vital roles in numerous biological processes. While several GPI-anchored proteins have been characterized, the biological functions of the GPI anchor have yet to be elucidated at a molecular level. This review discusses the structural diversity of the GPI anchor and its putative cellular functions, including involvement in lipid raft partitioning, signal transduction, targeting to the apical membrane, and prion disease pathogenesis. We specifically highlight studies in which chemically synthesized GPI anchors and analogues have been employed to study the roles of this unique posttranslational modification.

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Metadata

Authors
Paulick, M. G., & Bertozzi, C. R.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2008-06-17
Volume
47
Issue
27
Pages
6991-7000
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi8006324
OpenAlex
W2050606799
Cited by
600
References
50
FWCI
14.15
Type
journal article
Language
en
Open access
hybrid

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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.