1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4. Silva, A., P., G., Kwan, A., H., & Mackay, J., P. Biomolecular NMR Assignments, 8(1):137-139, 4, 2014.
Website doi abstract bibtex Chromatin-remodeling proteins have a pivotal role in normal cell function and development, catalyzing conformational changes in DNA that ultimately result in changes in gene expression patterns. Chromodomain helicase DNA-binding protein 4 (CHD4), the defining subunit of the nucleosome remodeling and deacetylase (NuRD) complex, is a nucleosome-remodeling protein of the SNF2/ISWI2 family, members of which contain two chromo domains and an ATP-dependent helicase module. CHD3, CHD4 and CHD5 also contain two contiguous PHD domains and have an extended N-terminal region that has not previously been characterized. We have identified a stable domain in the N-terminal region of CHD4 and report here the backbone and side chain resonance assignments for this domain at pH 7.5 and 25 °C (BMRB No. 18906). © 2013 Springer Science+Business Media Dordrecht.
@article{
title = {1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4},
type = {article},
year = {2014},
keywords = {CHD4,Chromatin remodeling,N-terminal domain,NuRD complex,PAR-binding motif},
pages = {137-139},
volume = {8},
websites = {http://link.springer.com/10.1007/s12104-013-9469-3},
month = {4},
day = {17},
id = {6b604bfa-8cf1-39d7-9959-cdd1ad06e0c1},
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last_modified = {2020-12-17T05:29:52.354Z},
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confirmed = {true},
hidden = {false},
citation_key = {Silva2014},
source_type = {ARTICLE},
notes = {cited By 1},
private_publication = {false},
abstract = {Chromatin-remodeling proteins have a pivotal role in normal cell function and development, catalyzing conformational changes in DNA that ultimately result in changes in gene expression patterns. Chromodomain helicase DNA-binding protein 4 (CHD4), the defining subunit of the nucleosome remodeling and deacetylase (NuRD) complex, is a nucleosome-remodeling protein of the SNF2/ISWI2 family, members of which contain two chromo domains and an ATP-dependent helicase module. CHD3, CHD4 and CHD5 also contain two contiguous PHD domains and have an extended N-terminal region that has not previously been characterized. We have identified a stable domain in the N-terminal region of CHD4 and report here the backbone and side chain resonance assignments for this domain at pH 7.5 and 25 °C (BMRB No. 18906). © 2013 Springer Science+Business Media Dordrecht.},
bibtype = {article},
author = {Silva, Ana P. G. and Kwan, Ann H. and Mackay, Joel P.},
doi = {10.1007/s12104-013-9469-3},
journal = {Biomolecular NMR Assignments},
number = {1}
}
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