Evidence map›Paper›PMID 32828427›Full record

ReviewBioorganic & medicinal chemistry2020

Uridine natural products: Challenging targets and inspiration for novel small molecule inhibitors.

Christine A Arbour, Barbara Imperiali

Open access · greenAbstract readReview
In one paragraph

Review in Bioorganic & medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Proteome-wide bioinformatic annotation and functional validation of the monotopic phosphoglycosyl transferase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
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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

2 authors at 1 institution in 1 country.

Christine A ArbourDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Barbara ImperialiDepartment of Biology and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: imper@mit.edu.
Massachusetts Institute of Technology · US

Funding

Structure and function of the monotopic phosphoglycosyl transferase superfamily: Initiators of biosynthesis of complex bacterial glycoconjugatesR01GM131627 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N. · 2019 to 2025
$3.1M
Design and synthesis of nucleoside-based small molecules to inhibit phosphoglycosyl transferasesF32GM136023 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ARBOUR, CHRISTINE · 2020 to 2023
$234k
NIGMS NIH HHS F32 GM136023NIGMS NIH HHS R01 GM131627
6 · The paper itself

Abstract

Nucleoside derivatives, in particular those featuring uridine, are familiar components of the nucleoside family of bioactive natural products. The structural complexity and biological activities of these compounds have inspired research from organic chemistry and chemical biology communities seeking to develop novel approaches to assemble the challenging molecular targets, to gain inspiration for enzyme inhibitor development and to fuel antibiotic discovery efforts. This review will present recent case studies describing the total synthesis and biosynthesis of uridine natural products, and de novo synthetic efforts exploiting features of the natural products to produce simplified scaffolds. This research has culminated in the development of complementary strategies that can lead to effective uridine-based inhibitors and antibiotics. The strengths and challenges of the juxtaposing methods will be illustrated by examining select uridine natural products. Moreover, structure-activity relationships (SAR) for each natural product-inspired scaffold will be discussed, highlighting the impact on inhibitor development, with the aim of future uridine-based small molecule expansion.

Indexed as

Anti-Bacterial AgentsBiological ProductsDrug DiscoveryEnzyme InhibitorsHumansMolecular StructurePhosphatesPolyprenolsStructure-Activity RelationshipUridineAnti-Bacterial AgentsBiological ProductsEnzyme InhibitorsPhosphatesPolyprenolsUridineInhibitor discoveryNatural product antibioticsNucleoside analogStructure-activity relationshipUridine

Identifiers

PMID32828427
PMCPMC7446765
OpenAlexW3046124372

What OpenQuestion holds

Textmetadata
LicenceTDM
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.