Evidence map›Paper›PMID 19204290›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability.

Sarah R Hanson, Elizabeth K Culyba, Tsui-Ling Hsu, Chi-Huey Wong, Jeffery W Kelly, Evan T Powers

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing 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

105 citing papers in PubMed.

  1. Review
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  13. Computational design of N-linked glycans for high throughput epitope profiling.Protein science : a publication of the Protein Society · 2023
    Article
  14. Review
  15. Review
  16. Article
  17. Hidden Relationships betweenInternational journal of molecular sciences · 2022
    Review
  18. Review
  19. Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Collagen's enigmatic, highly conservedProceedings of the National Academy of Sciences of the United States of America · 2021
    Article

45 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

6 authors.

Sarah R HansonDepartment of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Elizabeth K Culyba
Tsui-Ling Hsu
Chi-Huey Wong
Jeffery W Kelly
Evan T Powers

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
ENZYMES IN ORGANIC SYNTHESISR37GM044154 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WONG, CHI-HUEY · 2001 to 2008
$3.3M
ENZYMES IN ORGANIC SYNTHESISR01GM044154 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WONG, CHI-HUEY · 1989 to 1999
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NIGMS NIH HHS GM044154NIGMS NIH HHS GM51105NIGMS NIH HHS R01 GM044154NIGMS NIH HHS R01 GM051105NIGMS NIH HHS R37 GM044154
6 · The paper itself

Abstract

The folding energetics of the mono-N-glycosylated adhesion domain of the human immune cell receptor cluster of differentiation 2 (hCD2ad) were studied systematically to understand the influence of the N-glycan on the folding energy landscape. Fully elaborated N-glycan structures accelerate folding by 4-fold and stabilize the beta-sandwich structure by 3.1 kcal/mol, relative to the nonglycosylated protein. The N-glycan's first saccharide unit accounts for the entire acceleration of folding and for 2/3 of the native state stabilization. The remaining third of the stabilization is derived from the next 2 saccharide units. Thus, the conserved N-linked triose core, ManGlcNAc(2), improves both the kinetics and the thermodynamics of protein folding. The native state stabilization and decreased activation barrier for folding conferred by N-glycosylation provide a powerful and potentially general mechanism for enhancing folding in the secretory pathway.

Indexed as

Protein FoldingAnimalsCD2 AntigensCircular DichroismGlycoproteinsHumansKineticsModels, MolecularMutationProtein StabilityProtein Structure, TertiaryRatsTrisaccharidesCD2 AntigensGlycoproteinsTrisaccharides

Identifiers

PMID19204290
PMCPMC2651298

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.