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Related Concept Videos

Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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 variants are also...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...

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Related Experiment Video

Updated: Jun 2, 2026

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Histone onco-modifications.

J Füllgrabe1, E Kavanagh, B Joseph

  • 1Department of Oncology-Pathology, Cancer Centrum Karolinska, Karolinska Institutet, Stockholm, Sweden.

Oncogene
|April 26, 2011
PubMed
Summary
This summary is machine-generated.

Aberrant histone modifications, epigenetic changes impacting gene regulation, are linked to cancer development. The study proposes "histone onco-modifications" to describe these cancer-associated histone changes.

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Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
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Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

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Related Experiment Videos

Last Updated: Jun 2, 2026

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

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

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

Area of Science:

  • Epigenetics and Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • Post-translational modifications (PTMs) of histones regulate crucial cellular processes.
  • Disruption of these PTMs is implicated in carcinogenesis.
  • Aberrant histone modifications are observed in various human cancers.

Purpose of the Study:

  • To review aberrant covalent histone modifications in cancer.
  • To discuss the contribution of epigenetic changes in histone modification to cancer development.
  • To propose new terminology for cancer-associated histone modifications.

Main Methods:

  • Literature review of studies on histone modifications and cancer.
  • Analysis of the role of histone-modifying enzymes in cancer epigenetics.
  • Synthesis of findings to propose a new term.

Main Results:

  • Histone PTMs are critical for gene expression, DNA repair, and chromosome dynamics.
  • Alterations in histone-modifying enzymes lead to aberrant histone modifications.
  • These epigenetic changes contribute to the development and progression of human cancers.

Conclusions:

  • A new term, 'histone onco-modifications,' is proposed.
  • This terminology highlights the active role of histone modifications in cancer.
  • Understanding histone onco-modifications is crucial for cancer research and therapy.