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Authors report a modifying effect of a polymorphism of CELF4 on the dose-dependent association between anthracyclines and cardiomyopathy, which possibly occurs through a pathway that involves the expression of abnormally spliced TNNT2 (show TNNT2 Proteins) variants.
Determination of CELF4 protein domains required for RNA splicing.
Celf4 might be regulating alternative early in retinal development.
we suggest that CELF4 deficiency leads to abnormal neuronal function by combining a specific effect on neuronal excitation with a general impairment of synaptic transmission.
Data point strongly to the conclusion that Celf4 deletion primarily from excitatory neurons promotes convulsive seizure phenotypes.
CELF (show CEBPD Proteins) protein activity is required for normal alternative splicing in the heart in vivo and normal CELF (show CEBPD Proteins)-mediated alternative splicing regulation is in turn required for normal cardiac function.
Brunol4 deficiency in mice results in a complex seizure phenotype, likely due to the coordinate dysregulation of several molecules, providing a unique new animal model of epilepsy
Members of the CELF/BRUNOL protein family contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation. Multiple transcript variants encoding different isoforms have been found for this gene.
, CUG-BP- and ETR-3-like factor 4
, CUGBP Elav-like family member 4
, RNA-binding protein BRUNOL-4
, bruno-like protein 4
, RNA binding protein Bruno-like 4
, Bruno -like 4, RNA binding protein
, CUG-BP and ETR-3 like factor 4
, LYST-interacting protein LIP9
, RNA-binding protein BRUNOL4
, bruno-like 4, RNA binding protein
, CUG-BP and ETR-3-like factor 4