Evidence map›Paper›PMID 11559835›Full record

ArticleJournal of virology2001

Arginine-glycine-aspartic acid motif is critical for human parechovirus 1 entry.

Y Boonyakiat, P J Hughes, F Ghazi, G Stanway

Abstract read
In one paragraph

Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.2field-weighted citation impact, top 19% 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

32 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Review
  6. Polarized Entry of Human Parechoviruses in the Airway Epithelium.Frontiers in cellular and infection microbiology · 2018
    Article
  7. Article
  8. Structure of deformed wing virus, a major honey bee pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  17. Review
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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

4 authors at 1 institution in 1 country.

Y BoonyakiatDepartment of Biological Sciences, John Tabor Laboratories, University of Essex, Colchester CO4 3SQ, United Kingdom.
P J Hughes
F Ghazi
G Stanway
University of Essex · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The human parechovirus 1 RGD motif in VP1 was studied by mutagenesis. An RGD-to-RGE change gave only revertant viruses with a restored RGD, while deletion of GD was lethal and nonrevertable. Mutations at the +1 and +2 positions had some effect on growth properties and a +1 M-to-P change was lethal. These studies indicate that the RGD motif plays a critical role in infectivity, presumably by interacting with integrins, and that downstream amino acids can have an influence on function.

Indexed as

OligopeptidesVirus ReplicationAmino Acid SequenceArginineAspartic AcidGlycineHumansMolecular Sequence DataMutationPicornaviridaeSequence AlignmentViral ProteinsArgininearginyl-glycyl-aspartic acidAspartic AcidGlycineOligopeptidesViral Proteins

Identifiers

PMID11559835
PMCPMC114574
OpenAlexW2130828052

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.