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dc.contributor.authorHe, Lizhi
dc.contributor.authorGao, Mingshi
dc.contributor.authorPratt, Henry E
dc.contributor.authorWeng, Zhiping
dc.contributor.authorStruhl, Kevin
dc.date2022-08-11T08:08:00.000
dc.date.accessioned2022-08-23T15:38:35Z
dc.date.available2022-08-23T15:38:35Z
dc.date.issued2022-04-28
dc.date.submitted2022-07-05
dc.identifier.citation<p>He L, Gao M, Pratt H, Weng Z, Struhl K. MafB, WDR77, and ß-catenin interact with each other and have similar genome association profiles. PLoS One. 2022 Apr 28;17(4):e0264799. doi: 10.1371/journal.pone.0264799. PMID: 35482762; PMCID: PMC9049301. <a href="https://doi.org/10.1371/journal.pone.0264799">Link to article on publisher's site</a></p>
dc.identifier.issn1932-6203 (Linking)
dc.identifier.doi10.1371/journal.pone.0264799
dc.identifier.pmid35482762
dc.identifier.urihttp://hdl.handle.net/20.500.14038/25965
dc.description.abstractMafB (a bZIP transcription factor), ss-catenin (the ultimate target of the Wnt signal transduction pathway that acts as a transcriptional co-activator of LEF/TCF proteins), and WDR77 (a transcriptional co-activator of multiple hormone receptors) are important for breast cellular transformation. Unexpectedly, these proteins interact directly with each other, and they have similar genomic binding profiles. Furthermore, while some of these common target sites coincide with those bound by LEF/TCF, the majority are located just downstream of transcription initiation sites at a position near paused RNA polymerase (Pol II) and the +1 nucleosome. Occupancy levels of these factors at these promoter-proximal sites are strongly correlated with the level of paused Pol II and transcriptional activity.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=35482762&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright © 2022 He et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectBioinformatics
dc.subjectComputational Biology
dc.subjectGenetics and Genomics
dc.titleMafB, WDR77, and ß-catenin interact with each other and have similar genome association profiles
dc.typeJournal Article
dc.source.journaltitlePloS one
dc.source.volume17
dc.source.issue4
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1187&amp;context=bioinformatics_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bioinformatics_pubs/176
dc.identifier.contextkey30064406
refterms.dateFOA2022-08-23T15:38:35Z
html.description.abstract<p>MafB (a bZIP transcription factor), ss-catenin (the ultimate target of the Wnt signal transduction pathway that acts as a transcriptional co-activator of LEF/TCF proteins), and WDR77 (a transcriptional co-activator of multiple hormone receptors) are important for breast cellular transformation. Unexpectedly, these proteins interact directly with each other, and they have similar genomic binding profiles. Furthermore, while some of these common target sites coincide with those bound by LEF/TCF, the majority are located just downstream of transcription initiation sites at a position near paused RNA polymerase (Pol II) and the +1 nucleosome. Occupancy levels of these factors at these promoter-proximal sites are strongly correlated with the level of paused Pol II and transcriptional activity.</p>
dc.identifier.submissionpathbioinformatics_pubs/176
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.contributor.departmentProgram in Bioinformatics and Integrative Biology
dc.source.pagese0264799


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Copyright © 2022 He et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Except where otherwise noted, this item's license is described as Copyright © 2022 He et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.