@article{
 title = {Structural Insights into Interaction Mechanisms of Alternative Piperazine-urea YEATS Domain Binders in MLLT1},
 type = {article},
 year = {2019},
 keywords = {MLLT1,YEATS domains,cancer,inhibitor development,piperazine-urea},
 volume = {10},
 id = {28f185f1-d0b9-311c-b5d2-5700a7cd12aa},
 created = {2019-12-19T23:59:00.000Z},
 file_attached = {false},
 profile_id = {64f7fb50-d000-335d-a02d-06c5f340a97a},
 last_modified = {2021-02-27T01:23:11.400Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {true},
 abstract = {Copyright © 2019 American Chemical Society. YEATS-domain-containing MLLT1 is an acetyl/acyl-lysine reader domain, which is structurally distinct from well-studied bromodomains and has been strongly associated in development of cancer. Here, we characterized piperazine-urea derivatives as an acetyl/acyl-lysine mimetic moiety for MLLT1. Crystal structures revealed distinct interaction mechanisms of this chemotype compared to the recently described benzimidazole-amide based inhibitors, exploiting different binding pockets within the protein. Thus, the piperazine-urea scaffold offers an alternative strategy for targeting the YEATS domain family.},
 bibtype = {article},
 author = {Ni, X. and Heidenreich, D. and Christott, T. and Bennett, J. and Moustakim, M. and Brennan, P.E. and Fedorov, O. and Knapp, S. and Chaikuad, A.},
 doi = {10.1021/acsmedchemlett.9b00460},
 journal = {ACS Medicinal Chemistry Letters},
 number = {12}
}

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