Evidence map›Paper›PMID 30141327›Full record

ReviewChemical reviews2018

Chemoenzymatic Methods for the Synthesis of Glycoproteins.

Chao Li, Lai-Xi Wang

Open access · greenAbstract readReview
In one paragraph

Review in Chemical reviews, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
10.1field-weighted citation impact, top 1% 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

83 citing papers in PubMed, 234 citations in OpenAlex.

  1. Review
  2. Metabolic engineering ofApplied and environmental microbiology · 2026
    Review
  3. Revealing the Biological Effect of theJournal of the American Chemical Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Iron-Catalyzed GlycalTetrahedron letters · 2025
    Article
  12. Article
  13. Article
  14. Review
  15. BisectingACS chemical biology · 2025
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

23 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.

Chao LiDepartment of Chemistry and Biochemistry , University of Maryland , College Park , Maryland 20742 , United States.ORCID 0000-0002-8090-2017
Lai-Xi WangDepartment of Chemistry and Biochemistry , University of Maryland , College Park , Maryland 20742 , United States.ORCID 0000-0003-4293-5819
University 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
Synthesis and Function of Antibody Fc Domain GlycoformsR01GM096973 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2011 to 2020
$2.4M
Synthetic HIV Vaccine Targeting Glycopeptide Neutralizing EpitopesR01AI113896 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2014 to 2018
$2.3M
NIAID NIH HHS R01 AI113896NIGMS NIH HHS R01 GM080374NIGMS NIH HHS R01 GM096973
6 · The paper itself

Abstract

Glycosylation is one of the most prevalent posttranslational modifications that profoundly affects the structure and functions of proteins in a wide variety of biological recognition events. However, the structural complexity and heterogeneity of glycoproteins, usually resulting from the variations of glycan components and/or the sites of glycosylation, often complicates detailed structure-function relationship studies and hampers the therapeutic applications of glycoproteins. To address these challenges, various chemical and biological strategies have been developed for producing glycan-defined homogeneous glycoproteins. This review highlights recent advances in the development of chemoenzymatic methods for synthesizing homogeneous glycoproteins, including the generation of various glycosynthases for synthetic purposes, endoglycosidase-catalyzed glycoprotein synthesis and glycan remodeling, and direct enzymatic glycosylation of polypeptides and proteins. The scope, limitation, and future directions of each method are discussed.

Indexed as

CatalysisGlycoproteinsGlycoside HydrolasesGlycosylationPolysaccharidesProtein Processing, Post-TranslationalRecombinant ProteinsSubstrate SpecificityGlycoproteinsGlycoside HydrolasesPolysaccharidesRecombinant Proteins

Identifiers

PMID30141327
PMCPMC6238085
OpenAlexW2888074414

What OpenQuestion holds

Textmetadata
LicenceTDM
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.