Evidence map›Paper›PMID 31640986›Full record

ArticleThe Journal of biological chemistry2019

The R882H substitution in the human

Jonathan E Sandoval, Norbert O Reich

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Enzymology of Mammalian DNA Methyltransferases.Advances in experimental medicine and biology · 2022
    Article
  7. 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

2 authors at 1 institution in 1 country.

Jonathan E SandovalDepartment of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, California 93106-9510.
Norbert O ReichDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106-9510. Electronic address: reich@chem.ucsb.edu.
University of California, Santa Barbara · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A myriad of protein partners modulate the activity of the human DNA methyltransferase 3A (DNMT3A), whose interactions with these other proteins are frequently altered during oncogenesis. We show here that the tumor suppressor p53 decreases DNMT3A activity by forming a heterotetramer complex with DNMT3A. Mutational and modeling experiments suggested that p53 interacts with the same region in DNMT3A as does the structurally characterized DNMT3L. We observed that the p53-mediated repression of DNMT3A activity is blocked by amino acid substitutions within this interface, but surprisingly, also by a distal DNMT3A residue, R882H. DNMT3A R882H occurs frequently in various cancers, including acute myeloid leukemia, and our results suggest that the effects of R882H and other

Indexed as

Mutation, MissenseAllosteric RegulationAmino Acid SubstitutionDNA (Cytosine-5-)-MethyltransferasesDNA MethylationDNA Methyltransferase 3ADNA, NeoplasmHumansLeukemia, Myeloid, AcuteProtein MultimerizationTumor Suppressor Protein p53DNA (Cytosine-5-)-MethyltransferasesDNA Methyltransferase 3ADNA, NeoplasmDNMT3A protein, humanDNMT3L protein, humanTP53 protein, humanTumor Suppressor Protein p53allosteric regulationDNA demethylationDNMT3Aepigeneticsnucleic acid enzymologyp53protein-protein interaction

Identifiers

PMID31640986
PMCPMC6885622
OpenAlexW2981459585

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.