Evidence map›Paper›PMID 24702330›Full record

ArticleBioconjugate chemistry2014

Chemoenzymatic Fc glycosylation via engineered aldehyde tags.

Elizabeth L Smith, John P Giddens, Anthony T Iavarone, Kamil Godula, Lai-Xi Wang, Carolyn R Bertozzi

Open access · bronzeAbstract read
In one paragraph

Article in Bioconjugate chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

25 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
  2. Review
  3. Introduction of Carbonyl Groups into Antibodies.Molecules (Basel, Switzerland) · 2023
    Review
  4. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Synthetic and semi-synthetic approaches to unprotectedBeilstein journal of organic chemistry · 2018
    Review
  12. Article
  13. Improving theranostics in pancreatic cancer.Journal of surgical oncology · 2017
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article
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

6 authors at 1 institution in 1 country.

Elizabeth L SmithDepartments of Chemistry and ‡Molecular and Cell Biology and §Howard Hughes Medical Institute, ∥QB3/Chemistry Mass Spectrometry Facility, University of California , Berkeley, California 94720, United States.
John P Giddens
Anthony T Iavarone
Kamil Godula
Lai-Xi Wang
Carolyn R Bertozzi
University of Maryland, Baltimore · US

Funding

Investigations of Golgi EnzymesR01GM059907 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 1999 to 2016
$5.9M
Synthesis and Function of Antibody Fc Domain GlycoformsR01GM096973 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI WANG, LAI-XI · 2011 to 2020
$2.4M
NIGMS NIH HHS GM059907NIGMS NIH HHS GM096973NIGMS NIH HHS R01 GM059907NIGMS NIH HHS R01 GM096973
6 · The paper itself

Abstract

Glycoproteins with chemically defined glycosylation sites and structures are important biopharmaceutical targets and critical tools for glycobiology. One approach toward constructing such molecules involves chemical glycosylation of aldehyde-tagged proteins. Here, we report the installation of a genetically encoded aldehyde tag at the internal glycosylation site of the crystallizable fragment (Fc) of IgG1. We replaced the natural Fc N-glycosylation sequon with a five amino-acid sequence that was efficiently converted by recombinant formylglycine generating enzyme in vitro, thereby introducing aldehyde groups for subsequent chemical elaboration. Oxime-linked glycoconjugates were synthesized by conjugating aminooxy N-acetylglucosamine to the modified Fc followed by enzymatic transfer of complex N-glycans from corresponding glycan oxazolines by an EndoS-derived glycosynthase. In this manner we generated specific Fc glycoforms without relying on natural protein glycosylation machineries.

Indexed as

Protein EngineeringAldehydesAnimalsCHO CellsCricetulusGlycosylationImmunoglobulin Fc FragmentsImmunoglobulin GMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseRecombinant ProteinsStreptococcus pyogenesAldehydesImmunoglobulin Fc FragmentsImmunoglobulin GMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseRecombinant Proteins

Identifiers

PMID24702330
PMCPMC4004622
OpenAlexW1989418439

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.