@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},
 created = {2020-12-17T05:29:52.354Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2020-12-17T05:29:52.354Z},
 read = {false},
 starred = {false},
 authored = {false},
 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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