{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Chen Y"],"funding":["Howard Hughes Medical Institute","NCI NIH HHS","National Institutes of Health","NIH HHS"],"pagination":["e75064"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9681212"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11"],"pubmed_abstract":["Transcription factors (TFs) are classically attributed a modular construction, containing well-structured sequence-specific DNA-binding domains (DBDs) paired with disordered activation domains (ADs) responsible for protein-protein interactions targeting co-factors or the core transcription initiation machinery. However, this simple division of labor model struggles to explain why TFs with identical DNA-binding sequence specificity determined in vitro exhibit distinct binding profiles in vivo. The family of hypoxia-inducible factors (HIFs) offer a stark example: aberrantly expressed in several cancer types, HIF-1α and HIF-2α subunit isoforms recognize the same DNA motif in vitro - the hypoxia response element (HRE) - but only share a subset of their target genes in vivo, while eliciting con"],"journal":["eLife"],"pubmed_title":["Mechanisms governing target search and binding dynamics of hypoxia-inducible factors."],"pmcid":["PMC9681212"],"funding_grant_id":["S10 OD018174","U54 CA231641","U54-CA231641-01"],"pubmed_authors":["Tjian R","Darzacq X","Chen Y","Cattoglio C","Dailey GM","Zhu Q"],"additional_accession":[]},"is_claimable":false,"name":"Mechanisms governing target search and binding dynamics of hypoxia-inducible factors.","description":"Transcription factors (TFs) are classically attributed a modular construction, containing well-structured sequence-specific DNA-binding domains (DBDs) paired with disordered activation domains (ADs) responsible for protein-protein interactions targeting co-factors or the core transcription initiation machinery. However, this simple division of labor model struggles to explain why TFs with identical DNA-binding sequence specificity determined in vitro exhibit distinct binding profiles in vivo. The family of hypoxia-inducible factors (HIFs) offer a stark example: aberrantly expressed in several cancer types, HIF-1α and HIF-2α subunit isoforms recognize the same DNA motif in vitro - the hypoxia response element (HRE) - but only share a subset of their target genes in vivo, while eliciting con","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-05-10T06:35:14.048Z","creation":"2025-02-19T04:20:09.367Z"},"accession":"S-EPMC9681212","cross_references":{"pubmed":["36322456"],"doi":["10.7554/eLife.75064"]}}