Evidence map›Paper›PMID 12626399›Full record

ArticleGlycobiology2003

A transgenic insect cell line engineered to produce CMP-sialic acid and sialylated glycoproteins.

Jared J Aumiller, Jason R Hollister, Donald L Jarvis

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology.Advances in biochemical engineering/biotechnology · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Vaccine delivery using nanoparticles.Frontiers in cellular and infection microbiology · 2013
    Review
  18. Article
  19. IgG-Fc glycoengineering in non-mammalian expression hosts.Archives of biochemistry and biophysics · 2012
    Review
  20. Article
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.

Jared J AumillerDepartment of Molecular Biology, University of Wyoming, P.O. Box 3944, Laramie, WY 82071-3944, USA.
Jason R Hollister
Donald L Jarvis
University of Wyoming · US

Funding

N-GLYCOSYLATION MECHANISM IN INSECT CELLSR01GM049734 · NIGMS · UNIVERSITY OF WYOMING · PI JARVIS, DONALD L. · 1994 to 2010
$2.7M
NIGMS NIH HHS GM49734NIGMS NIH HHS R01 GM049734
6 · The paper itself

Abstract

We have previously engineered transgenic insect cell lines to express mammalian glycosyltransferases and showed that these cells can sialylate N-glycoproteins, despite the fact that they have little intracellular sialic acid and no detectable CMP-sialic acid. In the accompanying study, we presented evidence that these cell lines can salvage sialic acids for de novo glycoprotein sialylation from extracellular sialoglycoproteins, such as fetuin, found in fetal bovine serum. This finding led us to create a new transgenic insect cell line designed to synthesize its own sialic acid and CMP-sialic acid. SfSWT-1 cells, which encode five mammalian glycosyltransferases, were transformed with two additional mammalian genes that encode sialic acid synthase and CMP-sialic acid synthetase. The resulting cell line expressed all seven mammalian genes, produced CMP-sialic acid, and sialylated a recombinant glycoprotein when cultured in a serum-free growth medium supplemented with N-acetylmannosamine. Thus the addition of mammalian genes encoding two enzymes involved in CMP-sialic acid biosynthesis yielded a new transgenic insect cell line, SfSWT-3, that can sialylate recombinant glycoproteins in the absence of fetal bovine serum. This new cell line will be widely useful as an improved host for baculovirus-mediated recombinant glycoprotein production.

Indexed as

Genetic EngineeringSpodopteraAnimalsAnimals, Genetically ModifiedBaculoviridaeCell DivisionCell LineCytidine Monophosphate N-Acetylneuraminic AcidGenetic VectorsGlycoproteinsN-Acylneuraminate CytidylyltransferaseOxo-Acid-LyasesCytidine Monophosphate N-Acetylneuraminic AcidGlycoproteinsN-acetylneuraminate synthaseN-Acylneuraminate CytidylyltransferaseOxo-Acid-Lyases

Identifiers

PMID12626399
PMCPMC3612900
OpenAlexW2117728762

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.