Associated Papers
FOXL2 directs DNA double-strand break repair pathways by differentially interacting with Ku.
Jin H et al.
Nature Communications, 2020
A Novel FOXL2 Mutation Implying Blepharophimosis-Ptosis-Epicanthus Inversus Syndrome Type I.
Li F et al.
Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology, 2018
Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.
Holehouse AS et al.
Plos One, 2015
26659599 (PubMed )
Supplement: pone.0144692.s002.xlsx › suppTable_2.txt
Differential apoptotic and proliferative activities of wild-type FOXL2 and blepharophimosis-ptosis-epicanthus inversus syndrome (BPES)-associated mutant FOXL2 proteins.
Kim JH et al.
The Journal of Reproduction and Development, 2014
FOXL2 posttranslational modifications mediated by GSK3β determine the growth of granulosa cell tumours.
Kim JH et al.
Nature Communications, 2014
Mutational probing of the forkhead domain of the transcription factor FOXL2 provides insights into the pathogenicity of naturally occurring mutations.
Todeschini AL et al.
Human Molecular Genetics, 2011
Transcription factor FOXL2 protects granulosa cells from stress and delays cell cycle: role of its regulation by the SIRT1 deacetylase.
Benayoun BA et al.
Human Molecular Genetics, 2011
Functional study on a novel missense mutation of the transcription factor FOXL2 causes blepharophimosis-ptosis-epicanthus inversus syndrome (BPES).
Fan JY et al.
Mutagenesis, 2011
Functional exploration of the adult ovarian granulosa cell tumor-associated somatic FOXL2 mutation p.Cys134Trp (c.402C>G).
Benayoun BA et al.
Plos One, 2010
Towards a functional classification of pathogenic FOXL2 mutations using transactivation reporter systems.
Dipietromaria A et al.
Human Molecular Genetics, 2009
Differential functional effects of novel mutations of the transcription factor FOXL2 in BPES patients.
Nallathambi J et al.
Human Mutation, 2008
Missense mutations in the forkhead domain of FOXL2 lead to subcellular mislocalization, protein aggregation and impaired transactivation.
Beysen D et al.
Human Molecular Genetics, 2008
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