Evidence map›Paper›PMID 32526139›Full record

ReviewACS synthetic biology2020

Synthetic Glycobiology: Parts, Systems, and Applications.

Weston Kightlinger, Katherine F Warfel, Matthew P DeLisa, Michael C Jewett

Open access · hybridAbstract readReview
In one paragraph

Review in ACS synthetic biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 83 citations in OpenAlex.

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  19. Identification of a second glycoform of the clinically prevalent O1 antigen fromProceedings of the National Academy of Sciences of the United States of America · 2023
    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

4 authors at 2 institutions in 1 country.

Weston KightlingerDepartment of Chemical and Biological Engineering, Northwestern University, 2145 Sheridan Road, Tech E136, Evanston, Illinois 60208, United States.ORCID 0000-0002-5264-4866
Katherine F WarfelDepartment of Chemical and Biological Engineering, Northwestern University, 2145 Sheridan Road, Tech E136, Evanston, Illinois 60208, United States.ORCID 0000-0002-7780-6294
Matthew P DeLisaDepartment of Microbiology, Cornell University, 123 Wing Drive, Ithaca, New York 14853, United States.ORCID 0000-0003-3226-1566
Michael C JewettDepartment of Chemical and Biological Engineering, Northwestern University, 2145 Sheridan Road, Tech E136, Evanston, Illinois 60208, United States.ORCID 0000-0003-2948-6211
Northwestern University · USCornell 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
NIAID NIH HHS U19 AI142780
6 · The paper itself

Abstract

Protein glycosylation, the attachment of sugars to amino acid side chains, can endow proteins with a wide variety of properties of great interest to the engineering biology community. However, natural glycosylation systems are limited in the diversity of glycoproteins they can synthesize, the scale at which they can be harnessed for biotechnology, and the homogeneity of glycoprotein structures they can produce. Here we provide an overview of the emerging field of synthetic glycobiology, the application of synthetic biology tools and design principles to better understand and engineer glycosylation. Specifically, we focus on how the biosynthetic and analytical tools of synthetic biology have been used to redesign glycosylation systems to obtain defined glycosylation structures on proteins for diverse applications in medicine, materials, and diagnostics. We review the key biological parts available to synthetic biologists interested in engineering glycoproteins to solve compelling problems in glycoscience, describe recent efforts to construct synthetic glycoprotein synthesis systems, and outline exemplary applications as well as new opportunities in this emerging space.

Indexed as

AnimalsBacteriaBiotechnologyFungiGlycosylationGlycosyltransferasesPlantsProteinsSynthetic BiologyGlycosyltransferasesProteinsglycoengineeringglycosyltransferaseprotein glycosylationsynthetic glycobiology

Identifiers

PMID32526139
PMCPMC7372563
OpenAlexW3034280936

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.