Evidence map›Paper›PMID 33705871›Full record

ReviewSeminars in cancer biology2022

Targeting the acetylation signaling pathway in cancer therapy.

Fabin Dang, Wenyi Wei

Open access · greenAbstract readReview
In one paragraph

Review in Seminars in cancer biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

74 citing papers in PubMed, 102 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Targeting Lactate and Lactylation in Cancer Metabolism and Immunotherapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  5. Article
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  11. Article
  12. Review
  13. HIFU-Driven Targeted Pyroptosis Therapy in Basal-Like Breast Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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.

Fabin DangDepartment of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, 02215, USA.
Wenyi WeiDepartment of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, 02215, USA. Electronic address: wwei2@bidmc.harvard.edu.
Beth Israel Deaconess Medical Center · US

Funding

Discovery, Regulation and Function of the PI 3-Kinase and AKT Pathway in CancerR35CA253097 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI Alex Toker · 2020 to 2026
$6.9M
Deciphering the physiological role and interplay between ubiquitination and phosphorylation pathways to guide targeted cancer therapiesR35CA253027 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI Wenyi Wei · 2020 to 2026
$6.2M
Novel regulation of PI3K/Akt to direct targeted breast cancer therapiesR01CA177910 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WEI, WENYI · 2013 to 2023
$3.9M
Targeting the APC/Cdc20 E3 ubiquitin ligase for chemoradiation sensitizationR01CA200651 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WEI, WENYI · 2016 to 2020
$1.9M
Functional analysis of a tissue context-dependent role for beta-TRCP in lipid metabolism and tumorigenesisR01CA229307 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI WEI, WENYI · 2018 to 2020
$1.1M
Novel regulation of the CDK4/Cdh1/Pin1 signaling axis for targeted breast cancer therapiesK99CA263194 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI DANG, FABIN · 2021 to 2022
$340k
NCI NIH HHS K99 CA263194NCI NIH HHS R01 CA177910NCI NIH HHS R01 CA200651NCI NIH HHS R01 CA229307NCI NIH HHS R35 CA253027NCI NIH HHS R35 CA253097
6 · The paper itself

Abstract

Acetylation represents one of the major post-translational protein modifications, which introduces an acetyl functional group into amino acids such as the lysine residue to yield an acetate ester bond, neutralizing its positive charge. Regulation of protein functions by acetylation occurs in multiple ways, such as affecting protein stability, activity, localization, and interaction with other proteins or DNA. It has been well documented that the recruitment of histone acetyltransferases (HATs) and histone deacetylases (HDACs) to the transcriptional machinery can modulate histone acetylation status, which is directly involved in the dynamic regulation of genes controlling cell proliferation and division. Dysregulation of gene expression is involved in tumorigenesis and aberrant activation of histone deacetylases has been reported in several types of cancer. Moreover, there is growing body of evidence showing that acetylation is widely involved in non-histone proteins to impact their roles in various cellular processes including tumorigenesis. As such, small molecular compounds inhibiting HAT or HDAC enzymatic activities have been developed and investigated for therapeutic purpose. Here we review the recent progress in our understanding of protein acetylation and discuss the therapeutic potential of targeting the acetylation signaling pathway in cancer.

Indexed as

Histone Deacetylase InhibitorsNeoplasmsAcetylationCarcinogenesisHistone DeacetylasesHumansProtein Processing, Post-TranslationalProteinsSignal TransductionHistone Deacetylase InhibitorsHistone DeacetylasesProteinsAcetylationAcetyl transferaseCell signalingDeacetylaseDeacetylase inhibitorTumorigenesis

Identifiers

PMID33705871
PMCPMC8423867
OpenAlexW3133766777

What Socratic holds

Textmetadata
LicenceTDM
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.