Evidence map›Paper›PMID 25325701›Full record

ReviewNature chemical biology2014

The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.

Daniel N Hebert, Lydia Lamriben, Evan T Powers, Jeffery W Kelly

Abstract readReview
In one paragraph

Review in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing 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

95 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. N-glycan-dependent protein maturation and quality control in the ER.Nature reviews. Molecular cell biology · 2025
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review

35 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

4 authors.

Daniel N HebertDepartment of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts.
Lydia LamribenDepartment of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, Massachusetts.
Evan T PowersDepartment of Chemistry, The Scripps Research Institute, La Jolla, California, USA.
Jeffery W Kelly1] Department of Chemistry, The Scripps Research Institute, La Jolla, California, USA. [2] Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California, USA. [3] Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA.

Funding

Discovering small molecules activators of stress responsive signalingR01AG046495 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI JEFFERY W KELLY, Rockland Luke Wiseman · 2013 to 2026
$6.0M
UNDERSTANDING B-SHEET STRUCTURE IN AQUEOUS SOLUTIONR01GM051105 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI KELLY, JEFFERY W · 1994 to 2019
$5.8M
Cellular protein maturation and degradationR01GM086874 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI RAUCH, JENNIFER NICOLE · 2009 to 2025
$4.5M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
Understanding and Ameliorating Loss-of-Function Protein Misfolding DiseasesR01DK075295 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2006 to 2014
$3.9M
Discovering Small Molecule Activators of Stress-Responsive SignalingRF1AG046495 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W, WISEMAN, ROCKLAND LUKE · 2023 to 2025
$2.8M
Post-Reductionist Protein Folding: Determining the In-cell Folding Energy LandscaR01GM094848 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GERSHENSON, ANNE, GIERASCH, LILA M · 2010 to 2013
$1.3M
NIA NIH HHS AG046495NIA NIH HHS R01 AG046495NIA NIH HHS RF1 AG046495NIDDK NIH HHS DK075295NIDDK NIH HHS R01 DK075295NIGMS NIH HHS GM051105NIGMS NIH HHS GM08515NIGMS NIH HHS GM086874NIGMS NIH HHS GM094848NIGMS NIH HHS R01 GM051105NIGMS NIH HHS R01 GM086874NIGMS NIH HHS R01 GM094848NIGMS NIH HHS T32 GM008515
6 · The paper itself

Abstract

Proteins that traffic through the eukaryotic secretory pathway are commonly modified with N-linked carbohydrates. These bulky amphipathic modifications at asparagines intrinsically enhance solubility and folding energetics through carbohydrate-protein interactions. N-linked glycans can also extrinsically enhance glycoprotein folding by using the glycoprotein homeostasis or 'glycoproteostasis' network, which comprises numerous glycan binding and/or modification enzymes or proteins that synthesize, transfer, sculpt and use N-linked glycans to direct folding and trafficking versus degradation and trafficking of nascent N-glycoproteins through the cellular secretory pathway. If protein maturation is perturbed by misfolding, aggregation or both, stress pathways are often activated that result in transcriptional remodeling of the secretory pathway in an attempt to alleviate the insult (or insults). The inability to achieve glycoproteostasis is linked to several pathologies, including amyloidoses, cystic fibrosis and lysosomal storage diseases. Recent progress on genetic and pharmacologic adaptation of the glycoproteostasis network provides hope that drugs of this mechanistic class can be developed for these maladies in the near future.

Indexed as

HomeostasisGlycoproteinsHumansModels, MolecularPolysaccharidesGlycoproteinsPolysaccharides

Identifiers

PMID25325701
PMCPMC4232232

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.