Evidence map›Paper›PMID 33728787›Full record

ArticleAngewandte Chemie (International ed. in English)2021

Functionalized High Mannose-Specific Lectins for the Discovery of Type I Mannosidase Inhibitors.

Suresh E Kurhade, Jack D Weiner, Fei Philip Gao, Mark P Farrell

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Lectin Drug Conjugates Targeting High Mannose N-Glycans.Chembiochem : a European journal of chemical biology · 2022
    Article
  4. 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

4 authors at 1 institution in 1 country.

Suresh E KurhadeDepartment of Medicinal Chemistry, The University of Kansas, 2034 Becker Drive, Lawrence, KS, 66047, USA.
Jack D WeinerDepartment of Medicinal Chemistry, The University of Kansas, 2034 Becker Drive, Lawrence, KS, 66047, USA.
Fei Philip GaoProtein Production Group, The University of Kansas, 2034 Becker Drive, Lawrence, KS, 66047, USA.
Mark P FarrellDepartment of Medicinal Chemistry, The University of Kansas, 2034 Becker Drive, Lawrence, KS, 66047, USA.ORCID 0000-0002-6866-428X
University of Kansas · US

Funding

Synthetic Chemical Biology CoreP20GM113117 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI OROZCO, ROBIN C. · 2016 to 2025
$23.9M
Understanding the mechanobiology of stem cells in a microengineered 3D cardiac tissue environment with cardiomyopathyP20GM103638 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI LUNTE, SUSAN M · 2012 to 2021
$22.1M
Phase trafficking in combinatorial chemistry: ROM polymerizationP50GM069663 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI AUBE, JEFFREY · 2003 to 2012
$18.9M
Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
NIGMS NIH HHS P20 GM103638NIGMS NIH HHS P20 GM113117NIGMS NIH HHS P30 GM110761NIGMS NIH HHS P50 GM069663
6 · The paper itself

Abstract

An engineered cyanovirin-N homologue that exhibits specificity for high mannose N-glycans has been constructed to aid type I α 1,2-mannosidase inhibitor discovery and development. Engineering the lectins C-terminus permitted facile functionalization with fluorophores via a sortase and click strategy. The resulting lectin constructs exhibit specificity for cells presenting high mannose N-glycans. Importantly, these lectin constructs can also be applied to specifically assess changes in cell surface glycosylation induced by type I mannosidase inhibitors. Testing the utility of these lectin constructs led to the discovery of type I mannosidase inhibitors with nanomolar potency. Cumulatively, these findings reveal the specificity and utility of the functionalized cyanovirin-N homologue constructs, and highlight their potential in analytical contexts that require high mannose-specific lectins.

Indexed as

AlkaloidsAmino Acid MotifsAminoacyltransferasesBacterial ProteinsCell LineCysteine EndopeptidasesDrug DesignFluorescent DyesGlycosylationHumansLectinsMannoseMannosidasesMicroscopy, FluorescenceAlkaloidsAminoacyltransferasesBacterial Proteinscyanovirin NCysteine EndopeptidasesFluorescent DyeskifunensineLectinsMannoseMannosidasesmannosyl-oligosaccharide 1,2-alpha-mannosidasesortase Abioconjugationlectinmannosidase inhibitorsnatural productsprotein modifications

Identifiers

PMID33728787
PMCPMC8131250
OpenAlexW3139350169

What OpenQuestion holds

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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.