Evidence map›Paper›PMID 33916219›Full record

ReviewMetabolites2021

Protein Acetylation at the Interface of Genetics, Epigenetics and Environment in Cancer.

Mio Harachi, Kenta Masui, Webster K Cavenee, Paul S Mischel, Noriyuki Shibata

Open access · goldAbstract readReview
In one paragraph

Review in Metabolites, 2021. 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
1.9field-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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026
    Article
  2. Review
  3. Review
  4. The role of acetylation and deacetylation in cancer metabolism.Clinical and translational medicine · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Proteomic Profiling and Biomarker Discovery in Colorectal Liver Metastases.International journal of molecular sciences · 2022
    Review
  12. Review
  13. Review
  14. Review
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  16. Review
  17. Review
  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

5 authors at 3 institutions in 2 countries.

Mio HarachiDepartment of Pathology, Division of Pathological Neuroscience, Tokyo Women's Medical University, Tokyo 162-8666, Japan.
Kenta MasuiDepartment of Pathology, Division of Pathological Neuroscience, Tokyo Women's Medical University, Tokyo 162-8666, Japan.ORCID 0000-0002-5824-6690
Webster K CaveneeLudwig Institute for Cancer Research, University of California San Diego, La Jolla, CA 92093, USA.
Paul S MischelDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Noriyuki ShibataDepartment of Pathology, Division of Pathological Neuroscience, Tokyo Women's Medical University, Tokyo 162-8666, Japan.
Tokyo Women's Medical University · JPStanford University · USUniversity of California San Diego · US

Funding

The role of mTORC2 in reprogramming cancer cell metabolismR01NS073831 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MISCHEL, PAUL S · 2011 to 2020
$3.4M
Japan Society for the Promotion of Science 19K07649NIH HHS NS73831NINDS NIH HHS R01 NS073831
6 · The paper itself

Abstract

Metabolic reprogramming is an emerging hallmark of cancer and is driven by abnormalities of oncogenes and tumor suppressors. Accelerated metabolism causes cancer cell aggression through the dysregulation of rate-limiting metabolic enzymes as well as by facilitating the production of intermediary metabolites. However, the mechanisms by which a shift in the metabolic landscape reshapes the intracellular signaling to promote the survival of cancer cells remain to be clarified. Recent high-resolution mass spectrometry-based proteomic analyses have spotlighted that, unexpectedly, lysine residues of numerous cytosolic as well as nuclear proteins are acetylated and that this modification modulates protein activity, sublocalization and stability, with profound impact on cellular function. More importantly, cancer cells exploit acetylation as a post-translational protein for microenvironmental adaptation, nominating it as a means for dynamic modulation of the phenotypes of cancer cells at the interface between genetics and environments. The objectives of this review were to describe the functional implications of protein lysine acetylation in cancer biology by examining recent evidence that implicates oncogenic signaling as a strong driver of protein acetylation, which might be exploitable for novel therapeutic strategies against cancer.

Indexed as

epigeneticsmechanistic target of rapamycin (mTOR) complexesmetabolic reprogrammingmicroenvironmentprotein acetylation

Identifiers

PMID33916219
PMCPMC8066013
OpenAlexW3147705470

What OpenQuestion 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 OpenQuestion graph.