Evidence map›Paper›PMID 17979671›Full record

ReviewCurrent drug targets2007

Protein N-glycosylation in the baculovirus-insect cell system.

Xianzong Shi, Donald L Jarvis

Abstract readReview
In one paragraph

Review in Current drug targets, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

101 citing papers in PubMed, 195 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Cross-species protection suggestsInfection and immunity · 2025
    Article
  9. Review
  10. Engineering the mossFrontiers in plant science · 2025
    Article
  11. Article
  12. Article
  13. Insect cell production of chimeric virus-like particles based on human immunodeficiency virus GAG proteins and yellow fever virus envelope protein.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  14. Review
  15. Article
  16. Baculovirus-Assisted Production ofPathogens (Basel, Switzerland) · 2024
    Article
  17. Article
  18. Dimerization of the CNNM extracellular domain.Protein science : a publication of the Protein Society · 2024
    Article
  19. Article
  20. Article

41 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

2 authors at 1 institution in 1 country.

Xianzong ShiDepartment of Molecular Biology, University of Wyoming, 1000 E. University Avenue, Laramie, WY 82071, USA.
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

One of the major advantages of the baculovirus-insect cell system is that it is a eukaryotic system that can provide posttranslational modifications, such as protein N-glycosylation. However, this is a vastly oversimplified view, which reflects a poor understanding of insect glycobiology. In general, insect protein glycosylation pathways are far simpler than the corresponding pathways of higher eukaryotes. Paradoxically, it is increasingly clear that various insects encode and can express more elaborate protein glycosylation functions in restricted fashion. Thus, the information gathered in a wide variety of studies on insect protein N-glycosylation during the past 25 years has provided what now appears to be a reasonably detailed, comprehensive, and accurate understanding of the protein N-glycosylation capabilities of the baculovirus-insect cell system. In this chapter, we discuss the models of insect protein N-glycosylation that have emerged from these studies and how this impacts the use of baculovirus-insect cell systems for recombinant glycoprotein production. We also discuss the use of these models as baselines for metabolic engineering efforts leading to the development of new baculovirus-insect cell systems with humanized protein N-glycosylation pathways, which can be used to produce more authentic recombinant N-glycoproteins for drug development and other biomedical applications.

Indexed as

AnimalsBaculoviridaeGlycoproteinsGlycosylationInsectaInsect ProteinsModels, BiologicalProtein EngineeringRecombinant ProteinsGlycoproteinsInsect ProteinsRecombinant Proteins

Identifiers

PMID17979671
PMCPMC3647355
OpenAlexW1992271352

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.