Evidence map›Paper›PMID 29508463›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2018

Exploration of Strategies for Mechanism-Based Inhibitor Design for Family GH99 endo-α-1,2-Mannanases.

Pearl Z Fernandes, Marija Petricevic, Lukasz Sobala, Gideon J Davies, Spencer J Williams

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

5 authors.

Pearl Z FernandesSchool of Chemistry, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Vic, 3010, Australia.
Marija PetricevicSchool of Chemistry, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Vic, 3010, Australia.
Lukasz SobalaYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, YO10 5DD, UK.
Gideon J DaviesYork Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, YO10 5DD, UK.ORCID http://orcid.org/0000-0002-7343-776X
Spencer J WilliamsSchool of Chemistry, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Vic, 3010, Australia.ORCID http://orcid.org/0000-0001-6341-4364

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

endo-α-1,2-Mannosidases and -mannanases, members of glycoside hydrolase family 99 (GH99), cleave α-Glc/Man-1,3-α-Man-OR structures within mammalian N-linked glycans and fungal α-mannan, respectively. They are proposed to act through a two-step mechanism involving a 1,2-anhydrosugar "epoxide" intermediate incorporating two conserved catalytic carboxylates. In the first step, one carboxylate acts as a general base to deprotonate the 2-hydroxy group adjacent to the fissile glycosidic bond, and the other provides general acid assistance to the departure of the aglycon. We report herein the synthesis of two inhibitors designed to interact with either the general base (α-mannosyl-1,3-(2-aminodeoxymannojirimycin), Man2NH

Indexed as

CatalysisCatalytic DomainGlycoside HydrolasesGlycosidesMannansMannosidasesGlycoside HydrolasesGlycosidesMannansMannosidasesenzymesglycosidaseimidazole ringsinhibitorsX-ray crystallography

Identifiers

PMID29508463
PMCPMC6001782

What OpenQuestion holds

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LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

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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.