Evidence map›Paper›PMID 30679555›Full record

ArticleScientific reports2019

Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2.

Shilpa Yadahalli, José L Neira, Christopher M Johnson, Yaw Sing Tan, Pamela J E Rowling, Anasuya Chattopadhyay, Chandra S Verma, Laura S Itzhaki

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
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  7. New insights into cancer: MDM2 binds to the citrullinating enzyme PADI4.Protein science : a publication of the Protein Society · 2023
    Article
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  9. Review
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Targeting intrinsically disordered proteins involved in cancer.Cellular and molecular life sciences : CMLS · 2020
    Review
  16. Article
  17. Article
  18. 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

8 authors.

Shilpa YadahalliBioinformatics Institute, Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, Singapore, 138671, Singapore.
José L NeiraInstituto de Biocomputación y Física de Sistemas Complejos, Joint Units IQFR-CSIC-BIFI, and GBsC-CSIC-BIFI, Universidad de Zaragoza, 50009, Zaragoza, Spain.
Christopher M JohnsonMedical Research Council Laboratory of Molecular Biology, Francis Crick Avenue, CB2 2QH, Cambridge, United Kingdom.
Yaw Sing TanBioinformatics Institute, Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, Singapore, 138671, Singapore.
Pamela J E RowlingDepartment of Pharmacology, Tennis Court Road, University of Cambridge, CB2 1PD, Cambridge, United Kingdom.
Anasuya ChattopadhyayDepartment of Pharmacology, Tennis Court Road, University of Cambridge, CB2 1PD, Cambridge, United Kingdom.
Chandra S VermaBioinformatics Institute, Agency for Science, Technology and Research (A*STAR), 30 Biopolis Street, Singapore, 138671, Singapore. chandra@bii.a-star.edu.sg.
Laura S ItzhakiDepartment of Pharmacology, Tennis Court Road, University of Cambridge, CB2 1PD, Cambridge, United Kingdom. lsi10@cam.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

p53 is frequently mutated in human cancers. Its levels are tightly regulated by the E3 ubiquitin ligase MDM2. The complex between MDM2 and p53 is largely formed by the interaction between the N-terminal domain of MDM2 and the N-terminal transactivation (TA) domain of p53 (residues 15-29). We investigated the kinetic and thermodynamic basis of the MDM2/p53 interaction by using wild-type and mutant variants of the TA domain. We focus on the effects of phosphorylation at positions Thr18 and Ser20 including their substitution with phosphomimetics. Conformational propensities of the isolated peptides were investigated using in silico methods and experimentally by circular dichroism and

Indexed as

Binding SitesCircular DichroismHumansKineticsMagnetic Resonance SpectroscopyMolecular Dynamics SimulationMutationPeptide FragmentsPhosphorylationProtein ConformationProtein Interaction Domains and MotifsProto-Oncogene Proteins c-mdm2SerineSpectrometry, FluorescenceThermodynamicsThreonineMDM2 protein, humanPeptide FragmentsProto-Oncogene Proteins c-mdm2SerineThreonineTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID30679555
PMCPMC6345774

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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.