# Correction: Stapled histone H3 tails are super-substrates for lysine methyltransferase SETD7

**Authors:** Nurgül Bilgin, Laust Moesgaard, Jacob Kongsted, Jasmin Mecinović

PMC · DOI: 10.1039/d6sc90024k · Chemical Science · 2026-02-03

## TL;DR

This paper corrects a previous study on how stapled histone H3 tails interact with the enzyme SETD7.

## Contribution

The correction addresses errors or clarifications in the original findings about SETD7's interaction with histone H3 tails.

## Key findings

- The original study's conclusions about stapled histone H3 tails as super-substrates for SETD7 were corrected.
- The correction provides updated data or interpretations regarding the enzyme-substrate interaction.

## Abstract

Correction for ‘Stapled histone H3 tails are super-substrates for lysine methyltransferase SETD7’ by Nurgül Bilgin et al., Chem. Sci., 2026, https://doi.org/10.1039/d5sc08094k.

## Linked entities

- **Proteins:** SETD7 (SET domain containing 7, histone lysine methyltransferase)

## Full-text entities

- **Genes:** SETD7 (SET domain containing 7, histone lysine methyltransferase) [NCBI Gene 80854] {aka KMT7, SET7, SET7/9, SET9}

## Full text

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## References

1 references — full list in the complete paper: https://tomesphere.com/paper/PMC12865590/full.md

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Source: https://tomesphere.com/paper/PMC12865590