Evidence map›Paper›PMID 30540922›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019

Conformational stability and dynamics of the cancer-associated isoform Δ133p53β are modulated by p53 peptides and p53-specific DNA.

Jiangtao Lei, Ruxi Qi, Yegen Tang, Wenning Wang, Guanghong Wei, Ruth Nussinov, Buyong Ma

Open access · bronzeAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.3field-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

28 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. The p53 Isoforms as Potential Biomarkers in Different Cancer Entities.International journal of molecular sciences · 2026
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  5. Exon 4 and intron 4Biomedical reports · 2025
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  10. Human Disabled-2 regulates thromboxane ANature communications · 2024
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  11. Article
  12. Review
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  15. Review
  16. 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

7 authors at 4 institutions in 3 countries.

Jiangtao LeiState Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences-Ministry of Education, Department of Physics, Fudan University, Shanghai, China.
Ruxi QiState Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences-Ministry of Education, Department of Physics, Fudan University, Shanghai, China.
Yegen TangDepartment of Chemistry, Institute of Biomedical Sciences, Fudan University, Shanghai, China.
Wenning WangDepartment of Chemistry, Institute of Biomedical Sciences, Fudan University, Shanghai, China.
Guanghong WeiState Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences-Ministry of Education, Department of Physics, Fudan University, Shanghai, China.
Ruth NussinovBasic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, Maryland, USA; and.
Buyong MaBasic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, Maryland, USA; and.
Fudan University · CNState Key Laboratory of Surface PhysicsNational Cancer Institute · USTel Aviv University · IL

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

p53 is a tumor suppressor protein that maintains genome stability, but its Δ133p53β and Δ160p53β isoforms promote breast cancer cell invasion. The sequence truncations in the p53 core domain raise key questions related to their physicochemical properties, including structural stabilities, interaction mechanisms, and DNA-binding abilities. Herein, we investigated the conformational dynamics of Δ133p53β and Δ160p53β with and without binding to p53-specific DNA by using molecular dynamics simulations. We observed that the core domains of the 2 truncated isoforms are much less stable than wild-type (wt) p53β, and the increased solvent exposure of their aggregation-triggering segment indicates their higher aggregation propensities than wt p53. We also found that Δ133p53β stability is modulable by peptide or DNA interactions. Adding a p53 peptide (derived from truncated p53 sequence 107-129) may help stabilize Δ133p53. Most importantly, our simulations of p53 isomer-DNA complexes indicate that Δ133p53β dimer, but not Δ160p53β dimer, could form a stable complex with p53-specific DNA, which is consistent with recent experiments. This study provides physicochemical insight into Δ133p53β, Δ133p53β-DNA complexes, Δ133p53β's pathologic mechanism, and peptide-based inhibitor design against p53-related cancers.-Lei, J., Qi, R., Tang, Y., Wang, W., Wei, G., Nussinov, R., Ma, B. Conformational stability and dynamics of the cancer-associated isoform Δ133p53β are modulated by p53 peptides and p53-specific DNA.

Indexed as

Cell Line, TumorDNAHumansMolecular Dynamics SimulationPeptidesProtein IsoformsDNAPeptidesProtein Isoformsp53 aggregationp53 response elementΔ160p53β cancer

Identifiers

PMID30540922
PMCPMC6404584
OpenAlexW2904737867

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.