Evidence map›Paper›PMID 36252951›Full record

ReviewJournal of medicinal chemistry2022

Sialidase Inhibitors with Different Mechanisms.

Joseph M Keil, Garrett R Rafn, Isaac M Turan, Majdi A Aljohani, Reza Sahebjam-Atabaki, Xue-Long Sun

Open access · greenAbstract readReview
In one paragraph

Review in Journal of medicinal chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed, 1 pooled it
7.5field-weighted citation impact, top 2% 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

30 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.

  1. Pooled it
  2. Systematic identification of bacterial neuraminidase inhibitors fromJournal of enzyme inhibition and medicinal chemistry · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Frontiers in cellular and infection microbiology · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. 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

6 authors at 1 institution in 1 country.

Joseph M KeilDepartment of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, Ohio 44115, United States.
Garrett R RafnDepartment of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, Ohio 44115, United States.
Isaac M TuranDepartment of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, Ohio 44115, United States.
Majdi A AljohaniDepartment of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, Ohio 44115, United States.
Reza Sahebjam-AtabakiDepartment of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, Ohio 44115, United States.
Xue-Long SunDepartment of Chemistry, Chemical and Biomedical Engineering and Center for Gene Regulation in Health and Disease (GRHD), Cleveland State University, Cleveland, Ohio 44115, United States.ORCID 0000-0001-6483-1709
Cleveland State University · US

Funding

Development of Location-specific Sialidase InhibitorsR15GM144881 · NIGMS · CLEVELAND STATE UNIVERSITY · PI SUN, XUE-LONG · 2021 to 2023
$522k
A Digital Laser Scanner Biomolecular Imaging System: Amersham Typhoon 5S10OD025252 · OD · CLEVELAND STATE UNIVERSITY · PI LI, BIBO · 2018 to 2018
$163k
NIGMS NIH HHS R15 GM144881NIH HHS S10 OD025252
6 · The paper itself

Abstract

Sialidases, or neuraminidases, are enzymes that catalyze the hydrolysis of sialic acid (Sia)-containing molecules, mostly removal of the terminal Sia (desialylation). By desialylation, sialidase can modulate the functionality of the target compound and is thus often involved in biological pathways. Inhibition of sialidases with inhibitors is an important approach for understanding sialidase function and the underlying mechanisms and could serve as a therapeutic approach as well. Transition-state analogues, such as anti-influenza drugs oseltamivir and zanamivir, are major sialidase inhibitors. In addition, difluoro-sialic acids were developed as mechanism-based sialidase inhibitors. Further, fluorinated quinone methide-based suicide substrates were reported. Sialidase product analogue inhibitors were also explored. Finally, natural products have shown competitive inhibiton against viral, bacterial, and human sialidases. This Perspective describes sialidase inhibitors with different mechanisms and their activities and future potential, which include transition-state analogue inhibitors, mechanism-based inhibitors, suicide substrate inhibitors, product analogue inhibitors, and natural product inhibitors.

Indexed as

Biological ProductsNeuraminidaseAntiviral AgentsEnzyme InhibitorsHumansN-Acetylneuraminic AcidOseltamivirSialic AcidsZanamivirAntiviral AgentsBiological ProductsEnzyme InhibitorsN-Acetylneuraminic AcidNeuraminidaseOseltamivirSialic AcidsZanamivir

Identifiers

PMID36252951
PMCPMC9620260
OpenAlexW4306640148

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.