Evidence map›Paper›PMID 26713107›Full record

ArticleACS medicinal chemistry letters2015

4(5)-Aryl-2-C-glucopyranosyl-imidazoles as New Nanomolar Glucose Analogue Inhibitors of Glycogen Phosphorylase.

Éva Bokor, Sándor Kun, Tibor Docsa, Pál Gergely, László Somsák

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2015. 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
2.8field-weighted citation impact, top 10% 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, 36 citations in OpenAlex.

  1. Article
  2. Synthesis, In Silico and Kinetics Evaluation ofInternational journal of molecular sciences · 2024
    Article
  3. Article
  4. Dual-Target Compounds against Type 2Pharmaceuticals (Basel, Switzerland) · 2021
    Article
  5. Article
  6. Article
  7. Article
  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

5 authors at 1 institution in 1 country.

Éva BokorDepartment of Organic Chemistry, University of Debrecen , POB 20, H-4010 Debrecen, Hungary.
Sándor KunDepartment of Organic Chemistry, University of Debrecen , POB 20, H-4010 Debrecen, Hungary.
Tibor DocsaDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen , Egyetem tér 1, H-4032 Debrecen, Hungary.
Pál GergelyDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen , Egyetem tér 1, H-4032 Debrecen, Hungary.
László SomsákDepartment of Organic Chemistry, University of Debrecen , POB 20, H-4010 Debrecen, Hungary.
University of Debrecen · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Inhibition of glycogen phosphorylases may lead to pharmacological treatments of diseases in which glycogen metabolism plays an important role: first of all in diabetes, but also in cardiovascular and tumorous disorders. C-(β-d-Glucopyranosyl) isoxazole, pyrazole, thiazole, and imidazole type compounds were synthesized, and the latter showed the strongest inhibition against rabbit muscle glycogen phosphorylase b. Most efficient was 2-(β-d-glucopyranosyl)-4(5)-(2-naphthyl)-imidazole (11b, K i = 31 nM) representing the best nanomolar glucose derived inhibitor of the enzyme.

Indexed as

C-Glucopyranosyl derivativeglycogen phosphorylaseimidazoleinhibitorisoxazolepyrazolethiazole

Identifiers

PMID26713107
PMCPMC4677374
OpenAlexW2404624651

What OpenQuestion holds

Textmetadata
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.