Evidence map›Paper›PMID 22782562›Full record

ArticleBiopolymers2012

N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability.

Joshua L Price, Elizabeth K Culyba, Wentao Chen, Amber N Murray, Sarah R Hanson, Chi-Huey Wong, Evan T Powers, Jeffery W Kelly

Abstract read
In one paragraph

Article in Biopolymers, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 68 citations in OpenAlex.

  1. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Carbohydrate-binding moduleChemical science · 2020
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Oligosaccharide Synthesis and Translational Innovation.Journal of the American Chemical Society · 2019
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 2 institutions in 1 country.

Joshua L PriceDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA.
Elizabeth K Culyba
Wentao Chen
Amber N Murray
Sarah R Hanson
Chi-Huey Wong
Evan T Powers
Jeffery W Kelly
Scripps Research Institute · USBrigham Young University · US

Funding

UNDERSTANDING B-SHEET STRUCTURE IN AQUEOUS SOLUTIONR01GM051105 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI KELLY, JEFFERY W · 1994 to 2019
$5.8M
Carbohydrate-based Antiinfective AgentsR01AI072155 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WONG, CHI-HUEY · 2007 to 2014
$3.7M
The role of N-glycosylation on beta-sheet protein folding energeticsF32GM086039 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI PRICE, JOSHUA L · 2008 to 2010
$134k
NIAID NIH HHS AI072155NIAID NIH HHS R01 AI072155NIGMS NIH HHS F32 GM086039NIGMS NIH HHS GM051105NIGMS NIH HHS R01 GM051105
6 · The paper itself

Abstract

N-glycosylation can increase the rate of protein folding, enhance thermodynamic stability, and slow protein unfolding; however, the molecular basis for these effects is incompletely understood. Without clear engineering guidelines, attempts to use N-glycosylation as an approach for stabilizing proteins have resulted in unpredictable energetic consequences. Here, we review the recent development of three "enhanced aromatic sequons," which appear to facilitate stabilizing native-state interactions between Phe, Asn-GlcNAc and Thr when placed in an appropriate reverse turn context. It has proven to be straightforward to engineer a stabilizing enhanced aromatic sequon into glycosylation-naïve proteins that have not evolved to optimize specific protein-carbohydrate interactions. Incorporating these enhanced aromatic sequons into appropriate reverse turn types within proteins should enhance the well-known pharmacokinetic benefits of N-glycosylation-based stabilization by lowering the population of protease-susceptible unfolded and aggregation-prone misfolded states, thereby making such proteins more useful in research and pharmaceutical applications.

Indexed as

Amino Acid SequenceBinding SitesCD2 AntigensGlycoproteinsGlycosylationHumansModels, MolecularProtein ConformationCD2 AntigensGlycoproteins

Identifiers

PMID22782562
PMCPMC3539202
OpenAlexW2142359405

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.