Evidence map›Paper›PMID 18557633›Full record

ReviewBiochemistry2008

The glycosylphosphatidylinositol anchor: a complex membrane-anchoring structure for proteins.

Margot G Paulick, Carolyn R Bertozzi

Abstract readReview
In one paragraph

Review in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 258 papers.

0numbers the graph read from it
0cells of the map it votes in
258citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

258 citing papers in PubMed.

  1. Trial
  2. Defining cell surface and glycosylated RNAs.Trends in genetics : TIG · 2026
    Review
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198 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Margot G PaulickDepartment of Chemistry, University of California, Berkeley, California 94720, USA.
Carolyn R Bertozzi

Funding

Investigations of Golgi EnzymesR01GM059907 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 1999 to 2016
$5.9M
Howard Hughes Medical InstituteNIGMS NIH HHS GM59907NIGMS NIH HHS R01 GM059907
6 · The paper itself

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.

Indexed as

AcetylcholinesteraseErythrocytesGlycosylphosphatidylinositolsHumansMembrane ProteinsModels, BiologicalPeptidesAcetylcholinesteraseGlycosylphosphatidylinositolsMembrane ProteinsPeptides

Identifiers

PMID18557633
PMCPMC2663890

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.