Evidence map›Paper›PMID 31357595›Full record

ReviewInternational journal of molecular sciences2019

Roles of p53 Family Structure and Function in Non-Canonical Response Element Binding and Activation.

Bi-He Cai, Chung-Faye Chao, Hsiang-Chi Huang, Hsueh-Yi Lee, Reiji Kannagi, Jang-Yi Chen

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Amino Acid Composition in Various Types of Nucleic Acid-Binding Proteins.International journal of molecular sciences · 2021
    Review
  12. Review
  13. Article
  14. The Rich World of p53 DNA Binding Targets: The Role of DNA Structure.International journal of molecular sciences · 2019
    Review
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 1 country.

Bi-He CaiDepartment of Biology and Anatomy, National Defense Medical Center, Taipei 11490, Taiwan.ORCID 0000-0003-4226-6096
Chung-Faye ChaoDepartment of Biology and Anatomy, National Defense Medical Center, Taipei 11490, Taiwan.
Hsiang-Chi HuangInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan.
Hsueh-Yi LeeInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan.
Reiji KannagiInstitute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan. rkannagi@ibms.sinica.edu.tw.ORCID 0000-0003-4202-2921
Jang-Yi ChenDepartment of Biology and Anatomy, National Defense Medical Center, Taipei 11490, Taiwan. jychen01@ndmctsgh.edu.tw.ORCID 0000-0003-0179-4984
Institute of Biomedical Sciences, Academia Sinica · TWNational Defense Medical Center · TW

Funding

Academia Sinica and the Ministry of Science and Technology of Taiwan MOST 105-0210-01-13-01Academia Sinica and the Ministry of Science and Technology of Taiwan MOST 106-0210-01-15-02Ministry of National Defense, Republic of China NDMC-MAB-104-033Ministry of National Defense, Republic of China NDMC-MAB-105-051
6 · The paper itself

Abstract

The p53 canonical consensus sequence is a 10-bp repeat of PuPuPuC(A/T)(A/T)GPyPyPy, separated by a spacer with up to 13 bases. C(A/T)(A/T)G is the core sequence and purine (Pu) and pyrimidine (Py) bases comprise the flanking sequence. However, in the p53 noncanonical sequences, there are many variations, such as length of consensus sequence, variance of core sequence or flanking sequence, and variance in number of bases making up the spacer or AT gap composition. In comparison to p53, the p53 family members p63 and p73 have been found to have more tolerance to bind and activate several of these noncanonical sequences. The p53 protein forms monomers, dimers, and tetramers, and its nonspecific binding domain is well-defined; however, those for p63 or p73 are still not fully understood. Study of p63 and p73 structure to determine the monomers, dimers or tetramers to bind and regulate noncanonical sequence is a new challenge which is crucial to obtaining a complete picture of structure and function in order to understand how p63 and p73 regulate genes differently from p53. In this review, we will summarize the rules of p53 family non-canonical sequences, especially focusing on the structure of p53 family members in the regulation of specific target genes. In addition, we will compare different software programs for prediction of p53 family responsive elements containing parameters with canonical or non-canonical sequences.

Indexed as

Response ElementsTranscriptional ActivationAnimalsBase SequenceBinding SitesConsensus SequenceGene Expression RegulationGenetic VariationHumansMultigene FamilyProtein BindingProtein MultimerizationStructure-Activity RelationshipTumor Suppressor Protein p53Tumor Suppressor Protein p53dimernoncanonical sequencep53p63p73tetramer

Identifiers

PMID31357595
PMCPMC6696488
OpenAlexW2965919633

What Socratic 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 Socratic graph.