Evidence map›Paper›PMID 36380579›Full record

ArticleBiochemistry2022

Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR.

Alexander S Krois, Sangho Park, Maria A Martinez-Yamout, H Jane Dyson, Peter E Wright

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2022. 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
1.4field-weighted citation impact, top 17% 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, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. TowardsbioRxiv : the preprint server for biology · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Glutamine-rich regions of the disordered CREB transactivation domain mediate dynamic intra- and intermolecular interactions.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Article
  11. Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023
    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

5 authors at 1 institution in 1 country.

Alexander S KroisDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, Scripps Research, 10550 North Torrey Pines Road, La Jolla, California92037, United Sates.
Sangho ParkDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, Scripps Research, 10550 North Torrey Pines Road, La Jolla, California92037, United Sates.
Maria A Martinez-YamoutDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, Scripps Research, 10550 North Torrey Pines Road, La Jolla, California92037, United Sates.ORCID 0000-0003-4376-437X
H Jane DysonDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, Scripps Research, 10550 North Torrey Pines Road, La Jolla, California92037, United Sates.ORCID 0000-0001-6855-3398
Peter E WrightDepartment of Integrative Structural and Computational Biology and Skaggs Institute of Chemical Biology, Scripps Research, 10550 North Torrey Pines Road, La Jolla, California92037, United Sates.ORCID 0000-0002-1368-0223
Scripps Research Institute · US

Funding

Structural basis for CBP/p300 transcriptional regulationR01CA096865 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2002 to 2016
$6.2M
Protein Dynamics in Dihydrofolate Reductase CatalysisR01GM075995 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WRIGHT, PETER EDWIN · 2006 to 2021
$6.1M
Structural Studies of Large Dynamic ComplexesR35GM131693 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DYSON, HELEN JANE · 2019 to 2023
$2.6M
NCI NIH HHS R01 CA096865NIGMS NIH HHS R01 GM075995NIGMS NIH HHS R35 GM131693
6 · The paper itself

Abstract

The C-terminal region of the tumor suppressor protein p53 contains three domains, nuclear localization signal (NLS), tetramerization domain (TET), and C-terminal regulatory domain (CTD), which are essential for p53 function. Characterization of the structure and interactions of these domains within full-length p53 has been limited by the overall size and flexibility of the p53 tetramer. Using

Indexed as

DNATumor Suppressor Protein p53Isotope LabelingProtein BindingProtein Structure, TertiaryDNATumor Suppressor Protein p53

Identifiers

PMID36380579
PMCPMC9788666
OpenAlexW4309161821

What OpenQuestion holds

Textmetadata
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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.