<HashMap><database>GEO</database><file_versions><headers><Content-Type>application/xml</Content-Type></headers><body><files><Other>ftp://ftp.ncbi.nlm.nih.gov/geo/series/GSE298nnn/GSE298427/</Other></files><type>primary</type></body><statusCode>OK</statusCode><statusCodeValue>200</statusCodeValue></file_versions><scores/><additional><omics_type>Transcriptomics</omics_type><species>Mus musculus</species><gds_type>Expression profiling by high throughput sequencing</gds_type><full_dataset_link>https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE298427</full_dataset_link><repository>GEO</repository><entry_type>GSE</entry_type></additional><is_claimable>false</is_claimable><name>Progesterone receptor isoform PGR-A in female fertility</name><description>Progesterone is a critical reproductive hormone that acts via progesterone receptor transcriptional regulators. The short PGR-A isoform lacks a 164 amino acid N-terminal region present in PGR-B that markedly enhances its transcriptional activity. Isoform-specific mutants inactivating either PGR-A (PRAKO) or PGR-B (PRBKO) indicated that PGR-A is specifically essential for female fertility. This study revises that interpretation by showing that an inadvertent frame-shift mutation in the PRAKO caused ablation of both isoforms, instead of the intended PGR-A isoform-specific null mutation. A true PGR-A specific mutant generated through CRISPR-Cas9 editing with a complete lack of PGR-A, but retained expression of PGR-B showed a phenotype indistinguishable from wild type as previously shown for PRBKO females. Thus, the distinct function of PGR isoforms is more nuanced than previously appreciated.</description><dates><publication>2026/07/07</publication></dates><accession>GSE298427</accession><cross_references><GSM>GSM9014129</GSM><GSM>GSM9014128</GSM><GSM>GSM9014127</GSM><GSM>GSM9014126</GSM><GSM>GSM9014125</GSM><GSM>GSM9014124</GSM><GSM>GSM9014123</GSM><GSM>GSM9014130</GSM><GPL>24247</GPL><GSE>298427</GSE><taxon>Mus musculus</taxon></cross_references></HashMap>