Evidence map›Paper›PMID 33090335›Full record

ReviewJournal of industrial microbiology & biotechnology2020

Cell-free systems for accelerating glycoprotein expression and biomanufacturing.

Jasmine Hershewe, Weston Kightlinger, Michael C Jewett

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of industrial microbiology & biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Cell-Free Systems for the Production of Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Bioengineered Enzymes and Precision Fermentation in the Food Industry.International journal of molecular sciences · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Jasmine HersheweDepartment of Chemical and Biological Engineering, Northwestern University, Technological Institute E136, 2145 Sheridan Road, Evanston, IL, 60208-3120, USA.ORCID http://orcid.org/0000-0003-4795-9721
Weston KightlingerDepartment of Chemical and Biological Engineering, Northwestern University, Technological Institute E136, 2145 Sheridan Road, Evanston, IL, 60208-3120, USA.ORCID http://orcid.org/0000-0002-5264-4866
Michael C JewettDepartment of Chemical and Biological Engineering, Northwestern University, Technological Institute E136, 2145 Sheridan Road, Evanston, IL, 60208-3120, USA. m-jewett@northwestern.edu.ORCID http://orcid.org/0000-0003-2948-6211
Northwestern University · US

Funding

Innovative technologies to transform antibiotic discovery. Project 4 Infection site-specific amplification of antimicrobial conjugatesU19AI142780 · NIAID · BROAD INSTITUTE, INC. · PI HUNG, DEBORAH T · 2019 to 2023
$33.9M
Air Force Research Laboratory (US) FA8650-15-2-5518Army Research Office NDSEG-36373Bill and Melinda Gates Foundation OPP1217652Defense Advanced Research Projects Agency HR0011-15-C-0084Defense Threat Reduction Agency HDTRA1-15-10052/P00001NIAID NIH HHS U19 AI142780NIH HHS 1U19AI142780-01
6 · The paper itself

Abstract

Protein glycosylation, the enzymatic modification of amino acid sidechains with sugar moieties, plays critical roles in cellular function, human health, and biotechnology. However, studying and producing defined glycoproteins remains challenging. Cell-free glycoprotein synthesis systems, in which protein synthesis and glycosylation are performed in crude cell extracts, offer new approaches to address these challenges. Here, we review versatile, state-of-the-art systems for biomanufacturing glycoproteins in prokaryotic and eukaryotic cell-free systems with natural and synthetic N-linked glycosylation pathways. We discuss existing challenges and future opportunities in the use of cell-free systems for the design, manufacture, and study of glycoprotein biomedicines.

Indexed as

Cell-Free SystemGlycoproteinsGlycosylationBiotechnologyHumansProkaryotic CellsProtein BiosynthesisGlycoproteinsCell-free protein synthesisGlycoengineeringGlycosylationHigh-throughput experimentationSynthetic biology

Identifiers

PMID33090335
PMCPMC7578589
OpenAlexW3094275607

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.