Evidence map›Paper›PMID 2522097›Full record

ArticleThe Journal of cell biology1989

Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts.

J E Skibbens, M G Roth, K S Matlin

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

74 citing papers in PubMed, 205 citations in OpenAlex.

  1. Article
  2. Review
  3. Rab3 mediates a pathway for endocytic sorting and plasma membrane recycling of ordered microdomains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. The Continuing Mystery of Lipid Rafts.Journal of molecular biology · 2016
    Review
  11. Review
  12. Article
  13. Intact sphingomyelin biosynthetic pathway is essential for intracellular transport of influenza virus glycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Membrane organization and lipid rafts.Cold Spring Harbor perspectives in biology · 2011
    Review
  19. Article
  20. Review

14 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

3 authors at 1 institution in 1 country.

J E SkibbensVerna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030.
M G Roth
K S Matlin
Baylor College of Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biochemical changes in the influenza virus hemagglutinin during intracellular transport to the apical plasma membrane of epithelial cells were investigated in Madin-Darby canine kidney (MDCK) cells and in LLC-PK1 cells stably transfected with a hemagglutinin gene. After pulse-labeling a substantial fraction of hemagglutinin was observed to become insoluble in isotonic solutions of Triton X-100. Insolubility of hemagglutinin was detected late in the transport pathway after addition of complex sugars in the Golgi complex but before insertion of the protein in the plasma membrane. Insolubility was not dependent on oligosaccharide modification since deoxymannojirimycin (dMM), which inhibits mannose trimming, failed to prevent its onset. Insolubility was not due to assembly of virus particles at the plasma membrane because insoluble hemagglutinin was also observed in transfected cells. Hemagglutinin insolubility was also seen in MDCK cells cultured in suspension and in chick embryo fibroblasts, indicating that insolubility and plasma membrane polarity are not simply correlated. In addition to insolubility, an apparent transport-dependent reduction of the disulfide bond linking HA1 and HA2 in hemagglutinin was detected. Because of the timing of both insolubility and the loss of the disulfide bond, these modifications may be important in the delivery of the hemagglutinin to the cell surface.

Indexed as

Influenza A virus1-DeoxynojirimycinAnimalsBiological TransportCell LineCell MembraneChemical PhenomenaChemistryEpitheliumFibroblastsFluorescent Antibody TechniqueGlucosamineGolgi ApparatusHemagglutinins, ViralSolubility1-DeoxynojirimycinGlucosamineHemagglutinins, Viral

Identifiers

PMID2522097
PMCPMC2115377
OpenAlexW2160937520

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.