Evidence map›Paper›PMID 24646834›Full record

ArticleMolecules and cells2014

A conserved mechanism for binding of p53 DNA-binding domain and anti-apoptotic Bcl-2 family proteins.

Dong-Hwa Lee, Ji-Hyang Ha, Yul Kim, Mi Jang, Sung Jean Park, Ho Sup Yoon, Eun-Hee Kim, Kwang-Hee Bae, Byoung Chul Park, Sung Goo Park and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Molecules and cells, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

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  10. Anti-Proliferative Effect of Wogonin on Ovary Cancer Cells Involves Activation of Apoptosis and Cell Cycle Arrest.Medical science monitor : international medical journal of experimental and clinical research · 2019
    Article
  11. Article
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  13. Diallyl Trisulfide Inhibits Growth of NCI-H460International journal of biological sciences · 2017
    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

12 authors at 5 institutions in 2 countries.

Dong-Hwa LeeMedical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Ji-Hyang Ha
Yul Kim
Mi Jang
Sung Jean Park
Ho Sup Yoon
Eun-Hee Kim
Kwang-Hee Bae
Byoung Chul Park
Sung Goo Park
Gwan-Su Yi
Seung-Wook Chi
Korea Research Institute of Bioscience and Biotechnology · KRGachon University · KRKorea Institute of Brain Science · KRKorea Basic Science Institute · KRNanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The molecular interaction between tumor suppressor p53 and the anti-apoptotic Bcl-2 family proteins plays an essential role in the transcription-independent apoptotic pathway of p53. In this study, we investigated the binding of p53 DNA-binding domain (p53DBD) with the anti-apoptotic Bcl-2 family proteins, Bcl-w, Mcl-1, and Bcl-2, using GST pull-down assay and NMR spectroscopy. The GST pull-down assays and NMR experiments demonstrated the direct binding of the p53DBD with Bcl-w, Mcl-1, and Bcl-2. Further, NMR chemical shift perturbation data showed that Bcl-w and Mcl-1 bind to the positively charged DNA-binding surface of p53DBD. Noticeably, the refined structural models of the complexes between p53DBD and Bcl-w, Mcl-1, and Bcl-2 showed that the binding mode of p53DBD is highly conserved among the anti-apoptotic Bcl-2 family proteins. Furthermore, the chemical shift perturbations on Bcl-w, Mcl-1, and Bcl-2 induced by p53DBD binding occurred not only at the p53DBD-binding acidic region but also at the BH3 peptide-binding pocket, which suggests an allosteric conformational change similar to that observed in Bcl-XL. Taken altogether, our results revealed a structural basis for a conserved binding mechanism between p53DBD and the anti-apoptotic Bcl-2 family proteins, which shed light on to the molecular understanding of the transcription-independent apoptosis pathway of p53.

Indexed as

Allosteric RegulationApoptosis Regulatory ProteinsCell LineHumansModels, MolecularMyeloid Cell Leukemia Sequence 1 ProteinNuclear Magnetic Resonance, BiomolecularPeptide MappingProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryProtein Structure, SecondaryProto-Oncogene Proteins c-bcl-2Tumor Suppressor Protein p53Apoptosis Regulatory ProteinsBCL2L2 protein, humanMCL1 protein, humanMyeloid Cell Leukemia Sequence 1 ProteinProto-Oncogene Proteins c-bcl-2TP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID24646834
PMCPMC3969048
OpenAlexW1988913922

What OpenQuestion holds

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LicenceCC BY-NC-SA
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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.