Evidence map›Paper›PMID 24439206›Full record

ReviewChemistry & biology2014

Chemical and chemoenzymatic synthesis of glycoproteins for deciphering functions.

Lai-Xi Wang, Mohammed N Amin

Abstract readReview
In one paragraph

Review in Chemistry & biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
–field-weighted citation impact
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

63 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Recent Advances in the Chemical Biology ofMolecules (Basel, Switzerland) · 2021
    Review
  11. Advances in the Chemical Synthesis of Carbohydrates and Glycoconjugates.Advances in biochemical engineering/biotechnology · 2021
    Review
  12. Article
  13. Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020
    Review
  14. Glycosylation-dependent opsonophagocytic activity of staphylococcal protein A antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Review
  17. Article
  18. European journal of organic chemistry · 2020
    Article
  19. Article
  20. Article

3 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.

Lai-Xi WangInstitute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA. Electronic address: lwang@som.umaryland.edu.
Mohammed N AminInstitute of Human Virology and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.

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 R01 GM080374NIGMS NIH HHS R01 GM096973
6 · The paper itself

Abstract

Glycoproteins are an important class of biomolecules involved in a number of biological recognition processes. However, natural and recombinant glycoproteins are usually produced as mixtures of glycoforms that differ in the structures of the pendent glycans, which are difficult to separate in pure glycoforms. As a result, synthetic homogeneous glycopeptides and glycoproteins have become indispensable probes for detailed structural and functional studies. A number of elegant chemical and biological strategies have been developed for synthetic construction of tailor-made, full-size glycoproteins to address specific biological problems. In this review, we highlight recent advances in chemical and chemoenzymatic synthesis of homogeneous glycoproteins. Selected examples are given to demonstrate the applications of tailor-made, glycan-defined glycoproteins for deciphering glycosylation functions.

Indexed as

AnimalsCarbohydrate ConformationEnzymesGlycoproteinsGlycosylationHumansEnzymesGlycoproteins

Identifiers

PMID24439206
PMCPMC3923302

What OpenQuestion holds

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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.