Evidence map›Paper›PMID 11208140›Full record

ReviewTraffic (Copenhagen, Denmark)2000

Folding of viral envelope glycoproteins in the endoplasmic reticulum.

I Braakman, E van Anken

Open access · bronzeAbstract readReview
In one paragraph

Review in Traffic (Copenhagen, Denmark), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

44 citing papers in PubMed, 94 citations in OpenAlex.

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  15. Iminosugars: Promising therapeutics for influenza infection.Critical reviews in microbiology · 2017
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  19. Efficient method to optimize antibodies using avian leukosis virus display and eukaryotic cells.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
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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 at 2 institutions in 1 country.

I BraakmanDepartment of Bio-Organic Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, The Netherlands. braakman@chem.uu.nl
E van Anken
Academic Medical Center · NLUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Viral glycoproteins fold and oligomerize in the endoplasmic reticulum of the host cell. They employ the cellular machinery and receive assistance from cellular folding factors. During the folding process, they are retained in the compartment and their structural quality is checked by the quality control system of the endoplasmic reticulum. A special characteristic that distinguishes viral fusion proteins from most cellular proteins is the extensive conformational change they undergo during fusion of the viral and cellular membrane. Many viral proteins fold in conjunction with and dependent on a viral partner protein, sometimes even synthesized from the same mRNA. Relevant for folding is that viral glycoproteins from the same or related virus families may consist of overlapping sets of domain modules. The consequences of these features for viral protein folding are at the heart of this review.

Indexed as

Protein FoldingAnimalsCalcium-Binding ProteinsCalnexinCalreticulinCystineEndoplasmic ReticulumEvolution, MolecularGlycosylationHemagglutinin Glycoproteins, Influenza VirusHumansMolecular ChaperonesProtein ConformationProtein Processing, Post-TranslationalRibonucleoproteinsStructure-Activity RelationshipCalcium-Binding ProteinsCalnexinCalreticulinCystineHemagglutinin Glycoproteins, Influenza VirusMolecular ChaperonesRibonucleoproteinsViral Envelope ProteinsViral Fusion Proteins

Identifiers

PMID11208140
PMCPMC7190097
OpenAlexW2047151337

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.