Evidence map›Paper›PMID 31899625›Full record

ArticleBiochemistry2020

Length Specificity and Polymerization Mechanism of (1,3)-β-d-Glucan Synthase in Fungal Cell Wall Biosynthesis.

Abhishek Chhetri, Anna Loksztejn, Hai Nguyen, Kaila M Pianalto, Mi Jung Kim, Jiyong Hong, J Andrew Alspaugh, Kenichi Yokoyama

Abstract read
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mitochondrial cardiolipin sequestration of caspofungin underliesbioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

8 authors at 1 institution in 1 country.

Abhishek ChhetriDepartment of Biochemistry , Duke University School of Medicine , Durham , North Carolina 27710 , United States.
Anna LoksztejnDepartment of Biochemistry , Duke University School of Medicine , Durham , North Carolina 27710 , United States.
Hai NguyenDepartment of Biochemistry , Duke University School of Medicine , Durham , North Carolina 27710 , United States.
Kaila M PianaltoDepartment of Medicine , Duke University School of Medicine , Durham , North Carolina 27710 , United States.
Mi Jung KimDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0354 , United States.
Jiyong HongDepartment of Chemistry , Duke University , Durham , North Carolina 27708-0354 , United States.ORCID 0000-0002-5253-0949
J Andrew AlspaughDepartment of Medicine , Duke University School of Medicine , Durham , North Carolina 27710 , United States.
Kenichi YokoyamaDepartment of Biochemistry , Duke University School of Medicine , Durham , North Carolina 27710 , United States.ORCID 0000-0001-5625-469X
Duke University · US

Funding

Tri-Institutional Molecular Mycology and Pathogenesis Training ProgramT32AI052080 · NIAID · DUKE UNIVERSITY · PI ANDREW ALSPAUGH, JOSEPH HEITMAN · 2003 to 2026
$8.7M
Biosynthesis of peptidyl nucleoside antifungal antibioticsR01GM115729 · NIGMS · DUKE UNIVERSITY · PI YOKOYAMA, KENICHI · 2015 to 2023
$3.1M
Howard Hughes Medical InstituteNIAID NIH HHS T32 AI052080NIGMS NIH HHS R01 GM115729
6 · The paper itself

Abstract

(1,3)-β-d-Glucan synthase (GS) catalyzes formation of the linear (1,3)-β-d-glucan in the fungal cell wall and is a target of clinically approved antifungal antibiotics. The catalytic subunit of GS, FKS protein, does not exhibit significant sequence homology to other glycosyltransferases, and thus, significant ambiguity about its catalytic mechanism remains. One of the major technical barriers in studying GS is the absence of activity assay methods that allow characterization of the lengths and amounts of (1,3)-β-d-glucan due to its poor solubility in water and organic solvents. Here, we report a successful development of a novel GS activity assay based on size-exclusion chromatography coupled with pulsed amperometric detection and radiation counting (SEC-PAD-RC), which allows for the simultaneous characterization of the amount and length of the polymer product. The assay revealed that the purified yeast GS produces glucan with a length of 6550 ± 760 mer, consistent with the reported degree of polymerization of (1,3)-β-d-glucan isolated from intact cells. Pre-steady state kinetic analysis revealed a highly efficient but rate-determining chain elongation rate of 51.5 ± 9.8 s

Indexed as

beta-GlucansBiocatalysisCell WallChromatography, GelGlucosyltransferasesKineticsPolymerizationProteoglycansSaccharomyces cerevisiaeSpecies Specificitybeta-Glucansglucan synthaseGlucosyltransferasespolysaccharide-KProteoglycans

Identifiers

PMID31899625
PMCPMC7015794
OpenAlexW2998322238

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.