Evidence map›Paper›PMID 9371730›Full record

ArticleThe Biochemical journal1997

Glycosyl-phosphatidylinositol anchor attachment in a yeast in vitro system.

T L Doering, R Schekman

Abstract read
In one paragraph

Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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.

T L DoeringDepartment of Molecular and Cell Biology, Barker Hall, Howard Hughes Research Institute, University of California, Berkeley, CA 94720-3202, USA.
R Schekman

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast mating pheromone precursor prepro-alpha factor was fused to C-terminal signals for glycosyl-phosphatidylinositol (GPI) anchor attachment, based on the sequence of the Saccharomyces cerevisiae protein Gas1p. Maturation of fusion proteins expressed in vivo required the presence of both a functional GPI attachment site and the synthesis of GPI precursors. Constructs were translated in vitro for use in cell-free studies of glycolipid attachment. The radiolabelled polypeptides were post-translationally translocated into yeast microsomes, where at least one third of the molecules received a GPI anchor. This approach offers distinct advantages over anchor attachment reactions that require co-translational translocation of secretory peptide substrates.

Indexed as

Saccharomyces cerevisiae ProteinsBiological TransportCell-Free SystemFungal ProteinsGlycosylphosphatidylinositolsMembrane GlycoproteinsProtein PrecursorsRecombinant Fusion ProteinsResearch DesignSaccharomyces cerevisiaeFungal ProteinsGAS1 protein, S cerevisiaeGlycosylphosphatidylinositolsMembrane GlycoproteinsMF(ALPHA)1 protein, S cerevisiaeProtein PrecursorsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID9371730
PMCPMC1218970

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.