Evidence map›Paper›PMID 30389408›Full record

ArticleBioorganic & medicinal chemistry2018

Triazole-linked transition state analogs as selective inhibitors against V. cholerae sialidase.

Teri J Slack, Wanqing Li, Dashuang Shi, John B McArthur, Gengxiang Zhao, Yanhong Li, An Xiao, Zahra Khedri, Hai Yu, Yang Liu and 1 more

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

8 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022
    Review
  5. Article
  6. Review
  7. Review
  8. 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

11 authors at 2 institutions in 1 country.

Teri J SlackDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Wanqing LiDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Dashuang ShiCenter for Genetic Medicine Research, Children's National Medical Center, 111 Michigan Ave, NW, Washington DC 20012, USA.
John B McArthurDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Gengxiang ZhaoCenter for Genetic Medicine Research, Children's National Medical Center, 111 Michigan Ave, NW, Washington DC 20012, USA.
Yanhong LiDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
An XiaoDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Zahra KhedriDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Hai YuDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA.
Yang LiuCenter for Genetic Medicine Research, Children's National Medical Center, 111 Michigan Ave, NW, Washington DC 20012, USA.
Xi ChenDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, CA 95616, USA. Electronic address: xiichen@ucdavis.edu.
University of California, Davis · USChildren's National · US

Funding

Supplement: Exploring the biology of O-acetyl sialic acids using stable synthetic mimicsR01AI130684 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI, VARKI, AJIT P · 2017 to 2020
$2.3M
Targeting endogenous sialidases for treatment of endotoxic shockR43AI108115 · NIAID · ONCOIMMUNE, INC. · PI QIU, PING · 2014 to 2015
$395k
NIAID NIH HHS R01 AI130684NIAID NIH HHS R43 AI108115
6 · The paper itself

Abstract

Sialidases or neuraminidases are enzymes that catalyze the cleavage of terminal sialic acids from oligosaccharides and glycoconjugates. They play important roles in bacterial and viral infection and have been attractive targets for drug development. Structure-based drug design has led to potent inhibitors against neuraminidases of influenza A viruses that have been used successfully as approved therapeutics. However, selective and effective inhibitors against bacterial and human sialidases are still being actively pursued. Guided by crystal structural analysis, several derivatives of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en or DANA) were designed and synthesized as triazole-linked transition state analogs. Inhibition studies revealed that glycopeptide analog E-(TriazoleNeu5Ac2en)-AKE and compound (TriazoleNeu5Ac2en)-A were selective inhibitors against Vibrio cholerae sialidase, while glycopeptide analog (TriazoleNeu5Ac2en)-AdE selectively inhibited Vibrio cholerae and A. ureafaciens sialidases.

Indexed as

Catalytic DomainEnzyme AssaysEnzyme InhibitorsGlycopeptidesHumansMolecular Docking SimulationNeuraminidaseTriazolesVibrio choleraeEnzyme InhibitorsGlycopeptidesNeuraminidaseTriazolesCarbohydrateGlycopeptideNeuraminidaseSialidaseSialidase inhibitor

Identifiers

PMID30389408
PMCPMC6326775
OpenAlexW2898427751

What OpenQuestion holds

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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.