Evidence map›Paper›PMID 38367495›Full record

ArticleEuropean journal of medicinal chemistry2024

Does size matter? - Comparing pyranoses with septanoses as ligands of the bacterial lectin FimH.

Jonathan Cramer, Bryant Pero, Xiaohua Jiang, Cristin Bosko, Marleen Silbermann, Said Rabbani, Sebastian Wilke, Dilara D Nemli, Beat Ernst, Mark W Peczuh

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

Article in European journal of medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

10 authors at 3 institutions in 3 countries.

Jonathan CramerMolecular Pharmacy Group, Department of Pharmaceutical Sciences, Pharmacenter, University of Basel, Klingelbergstrasse 50, 4056, Basel, Switzerland; Institute for Pharmaceutical and Medicinal Chemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany.
Bryant PeroDepartment of Chemistry, University of Connecticut, 55 North Eagleville Road, U3060, Storrs, CT, 06269, USA.
Xiaohua JiangMolecular Pharmacy Group, Department of Pharmaceutical Sciences, Pharmacenter, University of Basel, Klingelbergstrasse 50, 4056, Basel, Switzerland.
Cristin BoskoDepartment of Chemistry, University of Connecticut, 55 North Eagleville Road, U3060, Storrs, CT, 06269, USA.
Marleen SilbermannMolecular Pharmacy Group, Department of Pharmaceutical Sciences, Pharmacenter, University of Basel, Klingelbergstrasse 50, 4056, Basel, Switzerland.
Said RabbaniMolecular Pharmacy Group, Department of Pharmaceutical Sciences, Pharmacenter, University of Basel, Klingelbergstrasse 50, 4056, Basel, Switzerland.
Sebastian WilkeInstitute for Pharmaceutical and Medicinal Chemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany.
Dilara D NemliInstitute for Pharmaceutical and Medicinal Chemistry, Heinrich-Heine-Universität Düsseldorf, Universitätsstraße 1, 40225, Düsseldorf, Germany.
Beat ErnstMolecular Pharmacy Group, Department of Pharmaceutical Sciences, Pharmacenter, University of Basel, Klingelbergstrasse 50, 4056, Basel, Switzerland.
Mark W PeczuhDepartment of Chemistry, University of Connecticut, 55 North Eagleville Road, U3060, Storrs, CT, 06269, USA. Electronic address: mark.peczuh@uconn.edu.
University of Basel · CHUniversity of Connecticut · USHeinrich Heine University Düsseldorf · DE

Funding

Ring Expanded Glycomimetic FimH Antagonists as Lead Compounds for anti-UTI TherapiesR21AI142363 · NIAID · UNIVERSITY OF CONNECTICUT STORRS · PI PECZUH, MARK W · 2019 to 2020
$397k
NIAID NIH HHS R21 AI142363
6 · The paper itself

Abstract

The pharmacological modulation of disease-relevant carbohydrate-protein interactions represents an underexplored area of medicinal chemistry. One particular challenge in the design of glycomimetic compounds is the inherent instability of the glycosidic bond toward enzymatic cleavage. This problem has traditionally been approached by employing S-, N-, or C-glycosides with reduced susceptibility toward glycosidases. The application of ring-extended glycomimetics is an innovative approach to circumvent this issue. On the example of the bacterial adhesin FimH, it was explored how design principles from pyranose glycomimetics transfer to analogous septanose structures. A series of ring-extended FimH antagonists exhibiting the well-proven pharmacophore necessary for targeting the tyrosine-gate of FimH was synthesized. The resulting septanoses were evaluated for their affinity to the conformationally rigid isolated lectin domain of FimH (FimH

Indexed as

LectinsMonosaccharidesLigandsMolecular ConformationTyrosineLectinsLigandsMonosaccharidesTyrosineAntiadhesive therapyBacterial lectinGlycomimeticsSeptanoseUrinary tract infections

Identifiers

PMID38367495
PMCPMC10964925
OpenAlexW4391656899

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.