Evidence map›Paper›PMID 32123732›Full record

ArticleACS central science2020

Sequential Glycosylation of Proteins with Substrate-Specific

Liang Lin, Weston Kightlinger, Sunaina Kiran Prabhu, Adam J Hockenberry, Chao Li, Lai-Xi Wang, Michael C Jewett, Milan Mrksich

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-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

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Identification of RESP18 Gene Mutations Linked to Hereditary Non-Syndromic Cleft Lip and Palate in a Southern Chinese Family.Medical science monitor : international medical journal of experimental and clinical research · 2024
    Article
  8. Review
  9. Cell-Free Systems for the Production of Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
    Review
  19. Review
  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

8 authors at 2 institutions in 1 country.

Liang LinDepartment of Biomedical Engineering, Center for Synthetic Biology, Department of Chemical and Biological Engineering, Interdisciplinary Biological Sciences Program, and Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Weston KightlingerDepartment of Biomedical Engineering, Center for Synthetic Biology, Department of Chemical and Biological Engineering, Interdisciplinary Biological Sciences Program, and Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Sunaina Kiran PrabhuDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Adam J HockenberryDepartment of Biomedical Engineering, Center for Synthetic Biology, Department of Chemical and Biological Engineering, Interdisciplinary Biological Sciences Program, and Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Chao LiDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Lai-Xi WangDepartment of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, United States.
Michael C JewettDepartment of Biomedical Engineering, Center for Synthetic Biology, Department of Chemical and Biological Engineering, Interdisciplinary Biological Sciences Program, and Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Milan MrksichDepartment of Biomedical Engineering, Center for Synthetic Biology, Department of Chemical and Biological Engineering, Interdisciplinary Biological Sciences Program, and Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Northwestern University · USUniversity of Maryland, College Park · US

Funding

Covergent Chemoenzymatic Synthesis of Glycopeptides and GlycoproteinsR01GM080374 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2007 to 2021
$3.9M
NIGMS NIH HHS R01 GM080374
6 · The paper itself

Abstract

Protein glycosylation is a common post-translational modification that influences the functions and properties of proteins. Despite advances in methods to produce defined glycoproteins by chemoenzymatic elaboration of monosaccharides, the understanding and engineering of glycoproteins remain challenging, in part, due to the difficulty of site-specifically controlling glycosylation at each of several positions within a protein. Here, we address this limitation by discovering and exploiting the unique, conditionally orthogonal peptide acceptor specificities of

Identifiers

PMID32123732
PMCPMC7047269
OpenAlexW3008386665

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.