Evidence map›Paper›PMID 30857263›Full record

ArticleMolecules (Basel, Switzerland)2019

Synthesis, Molecular Docking and β-Glucuronidase Inhibitory Potential of Indole Base Oxadiazole Derivatives.

El Hassane Anouar, Moustapha Eid Moustapha, Muhammad Taha, Mohammed H Geesi, Zeinab R Farag, Fazal Rahim, Noor Barak Almandil, Rai Khalid Farooq, Muhammad Nawaz, Ashik Mosaddik

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2019. 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
1.7field-weighted citation impact, top 18% 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, 19 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  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

10 authors at 4 institutions in 3 countries.

El Hassane AnouarDepartment of Chemistry, College of Science and Humanities, Prince Sattam bin Abdulaziz University, P.O. Box 83, 11942 Al Kharj, Saudi Arabia. anouarelhassane@yahoo.fr.
Moustapha Eid MoustaphaDepartment of Chemistry, College of Science and Humanities, Prince Sattam bin Abdulaziz University, P.O. Box 83, 11942 Al Kharj, Saudi Arabia. m.moustapha@psau.edu.sa.
Muhammad TahaDepartment of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, 31441 Dammam, Saudi Arabia. mtaha@iau.edu.sa.
Mohammed H GeesiDepartment of Chemistry, College of Science and Humanities, Prince Sattam bin Abdulaziz University, P.O. Box 83, 11942 Al Kharj, Saudi Arabia. m.geesi@psau.edu.sa.
Zeinab R FaragChemistry Department, Faculty of Science, Fayoum University, 63514 Fayoum, Egypt. zrf00@fayoum.edu.eg.
Fazal RahimDepartment of Chemistry, Hazara University, Mansehra-21300, Khyber Pakhtunkhwa 21300, Pakistan. fazalstar@gmail.com.
Noor Barak AlmandilDepartment of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, 31441 Dammam, Saudi Arabia. nbalmandil@iau.edu.sa.
Rai Khalid FarooqDepartment of Neuroscience Research, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, 31441 Dammam, Saudi Arabia. rkfarooq@iau.edu.sa.
Muhammad NawazDepartment of Nano-Medicine Research, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, 31441 Dammam, Saudi Arabia. mnnmuhammad@iau.edu.sa.
Ashik MosaddikDepartment of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, 31441 Dammam, Saudi Arabia. amosaddik@iau.edu.sa.
Imam Abdulrahman Bin Faisal University · SAPrince Sattam Bin Abdulaziz University · SAFayoum University · EGHazara University · PK

Funding

Deanship of Scientific Research at Prince Sattam Bin Abdulaziz University 2017/01/7199
6 · The paper itself

Abstract

β-glucuronidase is a lysosomal glycosidase enzyme which catalyzes the extracellular matrix of cancer and normal cells and the glycosaminoglycans of the cell membrane, which is important for cancer cell proliferation, invasion, and metastasis. Liver cancer, colon carcinoma, and neoplasm bladder are triggered by the increase of the level of β-glucuronidase activity. The most valuable structures are indole and oxadiazole which has gain immense attention because of its pharmacological behavior and display many biological properties. Twenty-two (

Indexed as

Enzyme ActivationEnzyme InhibitorsGlucuronidaseIndolesMolecular Docking SimulationMolecular StructureOxadiazolesStructure-Activity RelationshipEnzyme InhibitorsGlucuronidaseIndolesOxadiazolesindolemolecular dockingoxadiazoleSARsynthesisβ-glucuronidase

Identifiers

PMID30857263
PMCPMC6429331
OpenAlexW2921003949

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.