Evidence map›Paper›PMID 22141574›Full record

ReviewACS chemical biology2012

Emerging technologies for making glycan-defined glycoproteins.

Lai-Xi Wang, Joseph V Lomino

Open access · greenAbstract readReview
In one paragraph

Review in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

57 citing papers in PubMed, 139 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Introduction of Carbonyl Groups into Antibodies.Molecules (Basel, Switzerland) · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Cell Free Remodeling of Glycosylation of Antibodies.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Article
  10. Advances in the Chemical Synthesis of Carbohydrates and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021
    Review
  11. Glycosylation-dependent opsonophagocytic activity of staphylococcal protein A antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  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

2 authors at 1 institution in 1 country.

Lai-Xi WangInstitute of Human Virology, University of Maryland School of Medicine, Baltimore, 21201, United States. lwang@som.umaryland.edu
Joseph V Lomino
University of Maryland, Baltimore · 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
NIGMS NIH HHS GM080374NIGMS NIH HHS GM096973NIGMS NIH HHS R01 GM080374NIGMS NIH HHS R01 GM096973
6 · The paper itself

Abstract

Protein glycosylation is a common and complex posttranslational modification of proteins, which expands functional diversity while boosting structural heterogeneity. Glycoproteins, the end products of such a modification, are typically produced as mixtures of glycoforms possessing the same polypeptide backbone but differing in the site of glycosylation and/or in the structures of pendant glycans, from which single glycoforms are difficult to isolate. The urgent need for glycan-defined glycoproteins in both detailed structure-function relationship studies and therapeutic applications has stimulated an extensive interest in developing various methods for manipulating protein glycosylation. This review highlights emerging technologies that hold great promise in making a variety of glycan-defined glycoproteins, with a particular emphasis in the following three areas: specific glycoengineering of host biosynthetic pathways, in vitro chemoenzymatic glycosylation remodeling, and chemoselective and site-specific glycosylation of proteins.

Indexed as

Protein Processing, Post-TranslationalAnimalsCarbohydrate ConformationCarbohydrate SequenceCHO CellsCricetinaeEscherichia coliGene ExpressionGlycoconjugatesGlycoproteinsGlycosylationHEK293 CellsHumansIsomerismModels, MolecularMolecular Sequence DataGlycoconjugatesGlycoproteinsPolysaccharides

Identifiers

PMID22141574
PMCPMC3262938
OpenAlexW1974196334

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.