Evidence map›Paper›PMID 21700702›Full record

ArticleThe Journal of biological chemistry2011

N-acetylglucosamine (GlcNAc) induction of hyphal morphogenesis and transcriptional responses in Candida albicans are not dependent on its metabolism.

Shamoon Naseem, Angelo Gunasekera, Esteban Araya, James B Konopka

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

57 citing papers in PubMed, 92 citations in OpenAlex.

  1. Discovery of functional compounds from dimorphic edibleSynthetic and systems biotechnology · 2026
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  2. Ras1-Independent High Iron-Mediated Hyphal Formation inJournal of fungi (Basel, Switzerland) · 2026
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  3. Supramolecular Carbohydrate Assemblies with Tunable Glycan Surfaces.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Article
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  6. mSphere · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Knockdown ofFrontiers in cellular and infection microbiology · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. A Special Phenotype of AconidialJournal of fungi (Basel, Switzerland) · 2022
    Article
  19. Article
  20. From Jekyll to Hyde: The Yeast-Hyphal Transition ofPathogens (Basel, Switzerland) · 2021
    Review
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 at 1 institution in 1 country.

Shamoon NaseemDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794-5222.
Angelo GunasekeraDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794-5222.
Esteban ArayaDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794-5222.
James B KonopkaDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794-5222. Electronic address: jkonopka@ms.cc.sunysb.edu.
Stony Brook University · US

Funding

VIRAL ONCOLOGYT32CA009176 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI HEARING, PATRICK · 1985 to 2012
$5.2M
N-acetylglucosamine signaling in fungiR01GM087368 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KONOPKA, JAMES B · 2009 to 2012
$1.2M
NCI NIH HHS T32 CA009176NIGMS NIH HHS R01 GM087368
6 · The paper itself

Abstract

N-acetylglucosamine (GlcNAc) stimulates important signaling pathways in a wide range of organisms. In the human fungal pathogen Candida albicans, GlcNAc stimulates hyphal cell morphogenesis, virulence genes, and the genes needed to catabolize GlcNAc. Previous studies on the GlcNAc transporter (NGT1) indicated that GlcNAc has to be internalized to induce signaling. Therefore, the role of GlcNAc catabolism was examined by deleting the genes required to phosphorylate, deacetylate, and deaminate GlcNAc to convert it to fructose-6-PO(4) (HXK1, NAG1, and DAC1). As expected, the mutants failed to utilize GlcNAc. Surprisingly, GlcNAc inhibited the growth of the nag1Δ and dac1Δ mutants in the presence of other sugars, suggesting that excess GlcNAc-6-PO(4) is deleterious. Interestingly, both hxk1Δ and an hxk1Δ nag1Δ dac1Δ triple mutant could be efficiently stimulated by GlcNAc to form hyphae. These mutants could also be stimulated to express GlcNAc-regulated genes. Because GlcNAc must be phosphorylated by Hxk1 to be catabolized, and also for it to enter the anabolic pathways that form chitin, N-linked glycosylation, and glycosylphosphatidylinositol anchors, the mutant phenotypes indicate that GlcNAc metabolism is not needed to induce signaling in C. albicans. Thus, these studies in C. albicans reveal a novel role for GlcNAc in cell signaling that may also regulate critical pathways in other organisms.

Indexed as

Signal TransductionAcetylglucosamineCandida albicansFructosephosphatesFungal ProteinsGene DeletionGene Expression Regulation, FungalGenes, FungalHumansHyphaePhosphorylationAcetylglucosaminefructose-6-phosphateFructosephosphatesFungal Proteins

Identifiers

PMID21700702
PMCPMC3190674
OpenAlexW2134676812

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.