Evidence map›Paper›PMID 32749901›Full record

ReviewThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2021

Integration of Sugar Metabolism and Proteoglycan Synthesis by UDP-glucose Dehydrogenase.

Brenna M Zimmer, Joseph J Barycki, Melanie A Simpson

Open access · bronzeAbstract readReview
In one paragraph

Review in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Ecological plasticity ofMicrobiology spectrum · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Intersection of Glycosylation and Ferroptosis in Cancer.Antioxidants (Basel, Switzerland) · 2025
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. UDP-glucose dehydrogenase variants cause dystroglycanopathy.Annals of clinical and translational neurology · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Biallelic mutations inGenes & diseases · 2023
    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

3 authors at 1 institution in 1 country.

Brenna M ZimmerDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina.
Joseph J BaryckiDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina.
Melanie A SimpsonDepartment of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina.
North Carolina State University · US

Funding

Mechanisms of Hyaluronan Signaling and Turnover in Prostate CancerR01CA165574 · NCI · UNIVERSITY OF NEBRASKA LINCOLN · PI SIMPSON, MELANIE A. · 2012 to 2016
$1.6M
Defining aberrant steroid elimination in castration resistant prostate cancerR21CA185993 · NCI · UNIVERSITY OF NEBRASKA LINCOLN · PI BARYCKI, JOSEPH J, SIMPSON, MELANIE A. · 2015 to 2016
$333k
NCI NIH HHS R01 CA165574NCI NIH HHS R21 CA185993
6 · The paper itself

Abstract

Regulation of proteoglycan and glycosaminoglycan synthesis is critical throughout development, and to maintain normal adult functions in wound healing and the immune system, among others. It has become increasingly clear that these processes are also under tight metabolic control and that availability of carbohydrate and amino acid metabolite precursors has a role in the control of proteoglycan and glycosaminoglycan turnover. The enzyme uridine diphosphate (UDP)-glucose dehydrogenase (UGDH) produces UDP-glucuronate, an essential precursor for new glycosaminoglycan synthesis that is tightly controlled at multiple levels. Here, we review the cellular mechanisms that regulate UGDH expression, discuss the structural features of the enzyme, and use the structures to provide a context for recent studies that link post-translational modifications and allosteric modulators of UGDH to its function in downstream pathways.

Indexed as

Allosteric RegulationAnimalsBiosynthetic PathwaysHumansModels, MolecularNeoplasmsProtein Processing, Post-TranslationalProteoglycansSugarsUridine Diphosphate Glucose DehydrogenaseProteoglycansSugarsUridine Diphosphate Glucose Dehydrogenasedevelopmental disordersextracellular matrixglucuronidationglycosaminoglycanhyaluronannucleotide sugarspost-translational modificationsproteoglycanUDP-glucuronate

Identifiers

PMID32749901
PMCPMC7780191
OpenAlexW3047568949

What Socratic 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 Socratic graph.