Evidence map›Paper›PMID 24348024›Full record

ArticleBioinformatics and biology insights2013

Three Dimensional Structure Prediction of Fatty Acid Binding Site on Human Transmembrane Receptor CD36.

Zineb Tarhda, Oussama Semlali, Anas Kettani, Ahmed Moussa, Nada A Abumrad, Azeddine Ibrahimi

Open access · goldAbstract read
In one paragraph

Article in Bioinformatics and biology insights, 2013. 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
1.0field-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, 19 citations in OpenAlex.

  1. Article
  2. 5-HTJournal of atherosclerosis and thrombosis · 2022
    Article
  3. Review
  4. Mechanisms of foam cell formation in atherosclerosis.Journal of molecular medicine (Berlin, Germany) · 2017
    Review
  5. Article
  6. Article
  7. Macrophage-mediated cholesterol handling in atherosclerosis.Journal of cellular and molecular medicine · 2016
    Review
  8. Article
  9. Lead discovery and in silico 3D structure modeling of tumorigenic FAM72A (p17).Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    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

6 authors at 2 institutions in 2 countries.

Zineb TarhdaMedical Biotechnology lab, Pharmacology and Toxicology Lab, Faculty of Medicine and Pharmacy, University Mohammed V Souissi, Rabat, Morocco.
Oussama SemlaliMedical Biotechnology lab, Pharmacology and Toxicology Lab, Faculty of Medicine and Pharmacy, University Mohammed V Souissi, Rabat, Morocco.
Anas KettaniFaculty of Science, University Ben Msik, Casablanca, Morocco.
Ahmed MoussaENSA, Tanger, Morocco.
Nada A AbumradDepartment of Medicine, Center for Human Nutrition, Washington University School of Medicine, St. Louis, Missouri, USA.
Azeddine IbrahimiMedical Biotechnology lab, Pharmacology and Toxicology Lab, Faculty of Medicine and Pharmacy, University Mohammed V Souissi, Rabat, Morocco.
École Nationale de Commerce et de Gestion de Tanger · MAWashington University in St. Louis · US

Funding

CD36 AND INTESTINAL FAT ABSORPTIONR01DK060022 · NIDDK · WASHINGTON UNIVERSITY · PI ABUMRAD, NADA A. · 2001 to 2021
$7.7M
FATTY ACID TRANSPORTER: REGULATION, IDENTIFICATIONR01DK033301 · NIDDK · WASHINGTON UNIVERSITY · PI ABUMRAD, NADA A. · 1986 to 2017
$5.2M
NIDDK NIH HHS R01 DK033301NIDDK NIH HHS R01 DK060022
6 · The paper itself

Abstract

CD36 is an integral membrane protein which is thought to have a hairpin-like structure with alpha-helices at the C and N terminals projecting through the membrane as well as a larger extracellular loop. This receptor interacts with a number of ligands including oxidized low density lipoprotein and long chain fatty acids (LCFAs). It is also implicated in lipid metabolism and heart diseases. It is therefore important to determine the 3D structure of the CD36 site involved in lipid binding. In this study, we predict the 3D structure of the fatty acid (FA) binding site [127-279 aa] of the CD36 receptor based on homology modeling with X-ray structure of Human Muscle Fatty Acid Binding Protein (PDB code: 1HMT). Qualitative and quantitative analysis of the resulting model suggests that this model was reliable and stable, taking in consideration over 97.8% of the residues in the most favored regions as well as the significant overall quality factor. Protein analysis, which relied on the secondary structure prediction of the target sequence and the comparison of 1HMT and CD36 [127-279 aa] secondary structures, led to the determination of the amino acid sequence consensus. These results also led to the identification of the functional sites on CD36 and revealed the presence of residues which may play a major role during ligand-protein interactions.

Indexed as

3D modelCD36fatty acids binding sitehomology modeling

Identifiers

PMID24348024
PMCPMC3859822
OpenAlexW2046263652

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.