@article{
 title = {Insight into the architecture of the NuRD complex: Structure of the RbAp48-MTA1 subcomplex},
 type = {article},
 year = {2014},
 pages = {21844-21855},
 volume = {289},
 id = {a0afaf4d-99c7-3fea-9a0a-a55fcb967c4a},
 created = {2023-01-10T01:44:39.545Z},
 file_attached = {false},
 profile_id = {a5a2ab6f-a8b5-3db6-97bc-618752ee4386},
 group_id = {bc1ab1d4-9e57-37e6-9fb5-435fca0ee9d2},
 last_modified = {2023-01-10T01:44:39.545Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {Background: The NuRD complex controls gene expression through altering chromatin structure. Results: The MTA1-RbAp48 structure shows how the RbAp46/p48 histone chaperones are recruited to NuRD. Conclusion: The MTA subunits act as scaffolds for NuRD complex assembly. Significance: The MTA/RbAp48 interaction prevents binding of histone H4, which is crucial for understanding the role of the RbAp46/p48 chaperones in the complex. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.},
 bibtype = {article},
 author = {Alqarni, S.S.M. and Murthy, A. and Zhang, W. and Przewloka, M.R. and Silva, A.P.G. and Watson, A.A. and Lejon, S. and Pei, X.Y. and Smits, A.H. and Kloet, S.L. and Mackay, J.P. and Laue, E.D.},
 doi = {10.1074/jbc.M114.558940},
 journal = {Journal of Biological Chemistry},
 number = {32}
}

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