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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,...
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...
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...
2D NMR: Overview of Heteronuclear Correlation Techniques01:18

2D NMR: Overview of Heteronuclear Correlation Techniques

Heteronuclear correlation spectroscopy is an analytical technique that investigates the coupling between different types of nuclei, often a proton and an X-nucleus, such as carbon-13 or nitrogen-15. This method is commonly used in nuclear magnetic resonance (NMR) spectroscopy to gain insights into complex chemical compounds' structural and compositional aspects. A typical heteronuclear correlation spectrum displays X-nucleus chemical shifts on one axis and a proton spectrum on the other axis.
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.

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Updated: May 7, 2026

CorrelationCalculator and Filigree: Tools for Data-Driven Network Analysis of Metabolomics Data
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CorrelationCalculator and Filigree: Tools for Data-Driven Network Analysis of Metabolomics Data

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Finding associations among histone modifications using sparse partial correlation networks.

Julia Lasserre1, Ho-Ryun Chung, Martin Vingron

  • 1Computational Molecular Biology, MPI for Molecular Genetics, Berlin, Germany.

Plos Computational Biology
|September 17, 2013
PubMed
Summary
This summary is machine-generated.

This study reveals direct relationships between histone modifications using partial correlation networks. These networks offer insights into gene transcription regulation and identify potential confounding factors.

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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Analysis of Histone Antibody Specificity with Peptide Microarrays

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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Area of Science:

  • Molecular Biology
  • Genomics
  • Bioinformatics

Background:

  • Histone modifications are crucial for gene transcription regulation.
  • Existing studies often overlook the complex relationships between histone modifications, using simplified models.

Purpose of the Study:

  • To infer undirected networks of histone modifications based on partial correlations.
  • To identify direct associations and potential confounding factors between histone modifications.
  • To assess the stability and integrate networks across different cell types.

Main Methods:

  • Utilized partial correlation analysis to model relationships between histone modifications.
  • Applied the methodology to histone modification data from CD4+ cells.
  • Validated network stability using data from IMR90 and H1 cell types.

Main Results:

  • Developed partial correlation networks revealing direct associations between histone modifications.
  • Identified potential confounding factors by analyzing differences between correlation and partial correlation.
  • Demonstrated remarkable similarity of networks across different cell types.
  • Integrated networks into a consensus network for increased robustness.

Conclusions:

  • Partial correlation networks provide a robust framework for understanding histone modification interplay.
  • The identified networks are well-supported by existing biological knowledge.
  • Consensus networks enhance the reliability of findings on gene transcription regulation.