Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.1K
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
The writer...
8.1K
Histone Modification02:32

Histone Modification

12.9K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
12.9K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.3K
Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
4.3K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

6.7K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
6.7K
Epigenetic Regulation01:37

Epigenetic Regulation

3.0K
Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
3.0K
mTOR Signaling and Cancer Progression03:03

mTOR Signaling and Cancer Progression

3.7K
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
3.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Hydration-Modulated Glass Transition and Dynamics in Amorphous Porous Organic Cages.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Correction to: Paeonol Inhibits the Replication of Bovine Herpesvirus Type 1 In Vitro Through Regulating the PI3K/AKT Pathway.

Current microbiology·2026
Same author

Sororin locks the DNA-exit gate of cohesin to preserve sister-chromatid cohesion.

Nature communications·2026
Same author

CELF1 is a non-canonical eIF4E binding protein that promotes translation of epithelial-mesenchymal transition effector mRNAs.

Nucleic acids research·2026
Same author

MERTK inhibition cooperates with immunomodulatory cyclophosphamide to induce CXCL9<sup>+</sup> monocyte-macrophage programming and durable anti-tumor immunity in triple negative breast cancer.

bioRxiv : the preprint server for biology·2026
Same author

Asymmetric Surface Charge Engineering Regulates Solvation Structure and Ionic Conductivity in Confined Polymer Electrolytes.

Small (Weinheim an der Bergstrasse, Germany)·2026

Related Experiment Video

Updated: May 16, 2025

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

6.5K

Histone acetylation modulators in breast cancer.

Xueying Yuan1, Jeffrey M Rosen2

  • 1Department of Molecular and Cellular Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX, USA.

Breast Cancer Research : BCR
|April 1, 2025
PubMed
Summary

Histone acetylation modulators show promise for breast cancer treatment by targeting cancer cells and immunosuppressive myeloid cells. This review explores their therapeutic potential in breast cancer management.

Keywords:
EpigeneticsHistone acetylationMyeloid cells

More Related Videos

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

21.2K
Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

3.8K

Related Experiment Videos

Last Updated: May 16, 2025

Assays for Validating Histone Acetyltransferase Inhibitors
09:11

Assays for Validating Histone Acetyltransferase Inhibitors

Published on: August 6, 2020

6.5K
Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

21.2K
Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

3.8K

Area of Science:

  • Oncology
  • Epigenetics
  • Immunology

Background:

  • Breast cancer is a leading global cancer in women.
  • Epigenetic alterations, specifically histone acetylation dysregulation, are implicated in breast cancer development.
  • Histone acetylation modulators are emerging as potential therapeutic agents.

Purpose of the Study:

  • To comprehensively review the roles of histone acetylation modulators in breast cancer.
  • To examine the effects of histone acetylation inhibitors on breast cancer.
  • To highlight the impact of epigenetic reprogramming on immunosuppressive myeloid cells in breast cancer progression.

Main Methods:

  • Literature review of epigenetic reprogramming in breast cancer.
  • Analysis of histone acetylation modulators and their inhibitors.
  • Investigation of the interplay between histone acetylation and immunosuppressive myeloid cells.

Main Results:

  • Histone acetylation modulators influence both breast cancer cells and immunosuppressive myeloid cells.
  • Dysregulated histone acetylation contributes to breast cancer progression.
  • Modulators can alter the function and phenotype of immunosuppressive myeloid cells.

Conclusions:

  • Histone acetylation modulators represent promising therapeutic targets for breast cancer.
  • Targeting epigenetic mechanisms offers a novel strategy for breast cancer treatment.
  • Understanding the role of myeloid cells in conjunction with epigenetic modulators is crucial for effective therapy.