Evidence map›Paper›PMID 31111026›Full record

ArticleFrontiers in chemistry2019

Computational Studies on the Potency and Selectivity of PUGNAc Derivatives Against GH3, GH20, and GH84 β-N-acetyl-D-hexosaminidases.

Lili Dong, Shengqiang Shen, Yefei Xu, Leng Wang, Ruirui Feng, Jianjun Zhang, Huizhe Lu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Frontiers in chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 48% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Review
  2. O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Advances in Optical Sensors ofBioconjugate chemistry · 2022
    Review
  6. 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

7 authors at 1 institution in 1 country.

Lili DongDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
Shengqiang ShenDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
Yefei XuDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
Leng WangDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
Ruirui FengDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
Jianjun ZhangDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
Huizhe LuDepartment of Applied Chemistry, College of Science, China Agricultural University, Beijing, China.
China Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-N-acetyl-D-hexosaminidases have attracted significant attention due to their crucial role in diverse physiological functions including antibacterial synergists, pathogen defense, virus infection, lysosomal storage, and protein glycosylation. In particular, the GH3 β-N-acetyl-D-hexosaminidase of

Indexed as

binding free energyfree energies decompositionmolecular dockingmolecular dynamics simulationsPUGNAc derivativesselectivitiesβ-N-acetyl-D-hexosaminidases

Identifiers

PMID31111026
PMCPMC6499197
OpenAlexW2938031540

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.