Evidence map›Paper›PMID 2954653›Full record

ArticleCell1987

A short sequence in the COOH-terminus makes an adenovirus membrane glycoprotein a resident of the endoplasmic reticulum.

S Pääbo, B M Bhat, W S Wold, P A Peterson

Open access · greenAbstract read
In one paragraph

Article in Cell, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
17.5field-weighted citation impact, top 1% of its field
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

89 citing papers in PubMed, 201 citations in OpenAlex.

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29 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

4 authors at 3 institutions in 3 countries.

S Pääbo
B M Bhat
W S Wold
P A Peterson
Saint Louis University · USMax Planck Society · DEUppsala University · SE

Funding

ADENOVIRUS TWO CODED EARLY GLYCOPROTEINR01CA024710 · NCI · SAINT LOUIS UNIVERSITY · PI WOLD, WILLIAM SM · 1985 to 1997
–
NCI NIH HHS CA 24710
6 · The paper itself

Abstract

The E19 protein of adenoviruses is a transmembrane protein that abrogates the intracellular transport of class I antigens by forming complexes with them in the ER. We show here that the E19 protein is retained in the ER even in the absence of class I antigens. To define the region conferring residency in the ER, we examined two mutant forms of the viral protein. A 5 amino acid extension of the 15-membered cytoplasmic tail of the protein reduces its interaction with class I antigens but does not change its intracellular distribution. Shortening the tail to 7 amino acids also diminishes the affinity for class I antigens; however, this mutant E19 protein becomes transported to the cell surface. Thus, we concluded that a small stretch of amino acids exposed on the cytoplasmic side of the ER membrane is responsible for the retention of the E19 protein in the ER.

Indexed as

Adenovirus Early ProteinsAdenoviruses, HumanAntigens, Viral, TumorEndoplasmic ReticulumFlow CytometryFluorescent Antibody TechniqueHeLa CellsHumansMutationOncogene Proteins, ViralAdenovirus Early ProteinsAntigens, Viral, TumorOncogene Proteins, Viral

Identifiers

PMID2954653
PMCPMC7133293
OpenAlexW2009075135

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.