Evidence map›Paper›PMID 9050863›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion.

A Mehta, X Lu, T M Block, B S Blumberg, R A Dwek

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Mechanisms of Antiviral Activity of Iminosugars Against Dengue Virus.Advances in experimental medicine and biology · 2018
    Review
  16. Iminosugar antivirals: the therapeutic sweet spot.Biochemical Society transactions · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. Molecular mechanisms underlying HBsAg negativity in occult HBV infection.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2015
    Review
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

5 authors.

A MehtaThe Glycobiology Institute, Department of Biochemistry, Oxford University, United Kingdom.
X Lu
T M Block
B S Blumberg
R A Dwek

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI CHARNITA M. ZEIGLER-JOHNSON · 1985 to 2026
$138.8M
NCI NIH HHS CA-06927NCI NIH HHS P30 CA006927
6 · The paper itself

Abstract

The role of N-linked glycosylation and glycan trimming in the function of glycoproteins remains a central question in biology. Hepatitis B virus specifies three glycoproteins (L, M, and S) that are derived from alternate translation of the same ORF. All three glycoproteins contain a common N-glycosylation site in the S domain while M possesses an additional N-glycosylation site at its amino terminus. In the presence of N-butyl-deoxnojirimycin (an inhibitor of alpha-glucosidase) virions and the M protein are surprisingly retained. Preliminary evidence suggests that the retained M protein is hyperglucosylated and localized to lysosomal vesicles. In contrast, the S and L proteins are secreted, and their glycosylation state is unaffected by the presence of the inhibitor. Site-directed mutagenesis provides evidence that virion secretion requires the glycosylation sequon in the pre-S2 domain of M. This highlights the potential role of the M protein oligosaccharide as a therapeutic target.

Indexed as

1-DeoxynojirimycinAntigens, SurfaceBlotting, SouthernCarcinoma, HepatocellularCentrifugation, Density GradientDNA, ViralGlycoside Hydrolase InhibitorsGlycosylationHepatitis B virusHumansOligosaccharidesPolysaccharidesTransfectionTumor Cells, CulturedViral Envelope ProteinsViral Matrix Proteins1-DeoxynojirimycinAntigens, SurfaceDNA, ViralGlycoside Hydrolase InhibitorsL protein, hepatitis B virusOligosaccharidesPolysaccharidesViral Envelope ProteinsViral Matrix Proteins

Identifiers

PMID9050863
PMCPMC20001

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.