Structure-Function analysis of a novel DNA-binding domain of the histone acetyltransferase MOZ/KAT6A

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Structure-Function analysis of a novel DNA-binding domain of the histone acetyltransferase MOZ/KAT6A

In this study, we focussed on the poorly characterised NEMM domain comprised within the N-terminal 200 amino acids of the Monocytic Leukemia Zinc Finger Protein (MOZ/KAT6A). MOZ is an important developmental regulator and involved in several diseases such as neurodevelopmental disorders and cancers....

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Bibliographic Details
Main Author:	Schoenfeld, Jonas
Format:	Thesis (University of Nottingham only)
Language:	English
Published:	2019
Subjects:	MOZ KAT6A MYST3 DNA-binding winged helix CRISPR histone acetyltransferase
Online Access:	https://eprints.nottingham.ac.uk/59389/

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