Evidence map›Paper›PMID 26078940›Full record

ArticleBioMed research international2015

Molecular Analysis of AFP and HSA Interactions with PTEN Protein.

Mingyue Zhu, Bo Lin, Peng Zhou, Mengsen Li

Open access · hybridAbstract read
In one paragraph

Article in BioMed research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Alpha-fetoprotein: Past, present, and future.Hepatology communications · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  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

4 authors at 2 institutions in 1 country.

Mingyue ZhuCollege of Agriculture, Hainan University, Haikou, Hainan 570228, China ; Hainan Provincial Key Laboratory of Carcinogenesis and Intervention, Hainan Medical College, Haikou, Hainan 571199, China.
Bo LinHainan Provincial Key Laboratory of Carcinogenesis and Intervention, Hainan Medical College, Haikou, Hainan 571199, China ; Key Laboratory of Molecular Biology, Hainan Medical College, Haikou, Hainan 571199, China.
Peng ZhouCollege of Agriculture, Hainan University, Haikou, Hainan 570228, China.
Mengsen LiCollege of Agriculture, Hainan University, Haikou, Hainan 570228, China ; Hainan Provincial Key Laboratory of Carcinogenesis and Intervention, Hainan Medical College, Haikou, Hainan 571199, China ; Key Laboratory of Molecular Biology, Hainan Medical College, Haikou, Hainan 571199, China ; Institution of Tumor, Hainan Medical College, Haikou, Hainan 570102, China.
Hainan Medical College Hospital · CNHainan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human cytoplasmic alpha-fetoprotein (AFP) has been classified as a member of the albuminoid gene family. The protein sequence of AFP has significant homology to that of human serum albumin (HSA), but its biological characteristics are vastly different from HSA. The AFP functions as a regulator in the phosphatidylinositol 3-kinase (PI3K)/protein kinase B (AKT) pathway, but HSA plays a key role as a transport protein. To probe their molecular mechanisms, we have applied colocalization, coimmunoprecipitation (co-IP), and molecular docking approaches to analyze the differences between AFP and HSA. The data from colocalization and co-IP displayed a strong interaction between AFP and PTEN (phosphatase and tensin homolog), demonstrating that AFP did bind to PTEN, but HSA did not. The molecular docking study further showed that the AFP domains I and III could contact with PTEN. In silicon substitutions of AFP binding site residues at position 490M/K and 105L/R corresponding to residues K490 and R105 in HSA resulted in steric clashes with PTEN residues R150 and K46, respectively. These steric clashes may explain the reason why HSA cannot bind to PTEN. Ultimately, the experimental results and the molecular modeling data from the interactions of AFP and HSA with PTEN will help us to identify targets for designing drugs and vaccines against human hepatocellular carcinoma.

Indexed as

alpha-FetoproteinsBinding SitesCarcinoma, HepatocellularCell Line, TumorHumansLiver NeoplasmsMolecular Docking SimulationPhosphatidylinositol 3-KinasesProtein BindingProtein ConformationPTEN PhosphohydrolaseSerum AlbuminSignal TransductionAFP protein, humanalpha-FetoproteinsPhosphatidylinositol 3-KinasesPTEN PhosphohydrolasePTEN protein, humanSerum Albumin

Identifiers

PMID26078940
PMCPMC4452835
OpenAlexW1559377204

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Registered trials

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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.