Evidence map›Paper›PMID 20045480›Full record

ReviewSeminars in cell & developmental biology2010

UDP-GlC:glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control.

Cecilia D'Alessio, Julio J Caramelo, Armando J Parodi

Abstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.7field-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

70 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Production of high-affinity glycosylated anti-mouse conjugated nanobodies inFrontiers in bioengineering and biotechnology · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. GANAB andInternational journal of molecular sciences · 2022
    Review
  11. Article
  12. Article
  13. Revisiting CFTR Interactions: Old Partners and New Players.International journal of molecular sciences · 2021
    Review
  14. Review
  15. TorsinA folding and N-linked glycosylation are sensitive to redox homeostasis.Biochimica et biophysica acta. Molecular cell research · 2021
    Article
  16. To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021
    Review
  17. Article
  18. Selenoprotein F knockout leads to glucose and lipid metabolism disorders in mice.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  19. Review
  20. Review

10 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

3 authors at 1 institution in 1 country.

Cecilia D'AlessioLaboratory of Glycobiology, Fundación Instituto Leloir, Avda. Patricias Argentinas 435, C1405BWE, Buenos Aires, Argentina.
Julio J Caramelo
Armando J Parodi
Consejo Nacional de Investigaciones Científicas y Técnicas · AR

Funding

TRANSIENT GLUCOSYLATION OF GYLCOPROTEINSR01GM044500 · NIGMS · LELOIR INSTITUTE · PI PARODI, ARMANDO JOSE · 1990 to 2011
$840k
Howard Hughes Medical InstituteNIGMS NIH HHS GM044500NIGMS NIH HHS R01 GM044500
6 · The paper itself

Abstract

The N-glycan-dependent quality control of glycoprotein folding prevents endoplasmic to Golgi exit of folding intermediates, irreparably misfolded glycoproteins and incompletely assembled multimeric complexes. It also enhances folding efficiency by preventing aggregation and facilitating formation of proper disulfide bonds. The control mechanism essentially involves four components, resident lectin-chaperones that recognize monoglucosylated polymannose glycans, a lectin-associated oxidoreductase acting on monoglucosylated glycoproteins, a glucosyltransferase that creates monoglucosytlated epitopes in protein-linked glycans and a glucosidase that removes the glucose units added by the glucosyltransferase. This last enzyme is the only mechanism component sensing glycoprotein conformations as it creates monoglucosylated glycans exclusively in not properly folded species or in not completely assembled complexes. The glucosidase is a dimeric heterodimer composed of a catalytic subunit and an additional one that is partially responsible for the ER localization of the enzyme and for the enhancement of the deglucosylation rate as its mannose 6-phosphate receptor homologous domain presents the substrate to the catalytic site. This review deals with our present knowledge on the glucosyltransferase and the glucosidase.

Indexed as

alpha-GlucosidasesAnimalsChromatography, GasGlucoseGlycogen Debranching Enzyme SystemGlycoproteinsGolgi ApparatusHumansLectinsMannansMolecular ChaperonesPolysaccharidesUridine Diphosphate4 alpha-glucanotransferase4-nitrophenyl-alpha-glucosidasealpha-GlucosidasesGlucoseGlycogen Debranching Enzyme SystemGlycoproteinsLectinsMannansMolecular ChaperonespolymannosePolysaccharidesUridine Diphosphate

Identifiers

PMID20045480
PMCPMC2883647
OpenAlexW2061793634

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.