New Phosphospecific Antibody Reveals Isoform-Specific Phosphorylation of CPEB3 Protein
نویسندگان
چکیده
منابع مشابه
New Phosphospecific Antibody Reveals Isoform-Specific Phosphorylation of CPEB3 Protein
Cytoplasmic Polyadenylation Element Binding proteins (CPEBs) are a family of polyadenylation factors interacting with 3'UTRs of mRNA and thereby regulating gene expression. Various functions of CPEBs in development, synaptic plasticity, and cellular senescence have been reported. Four CPEB family members of partially overlapping functions have been described to date, each containing a distinct ...
متن کاملIsoform-specific phosphorylation-dependent regulation
18 Connexins (Cx) form gap junction channels made up of two connexons 19 (hemichannels) from adjacent cells. Unopposed hemichannels may open towards the extracellular 20 space upon stimulation by e.g. removal of divalent cations from the extracellular solution and allow 21 isoform-specific transmembrane flux of fluorescent dyes and physiologically relevant molecules, 22 such as ATP and ions. Cx...
متن کاملProduction of specific IgY antibody to the recombinant FanC protein produced in Escherichia coli
Objective(s): Enterotoxigenic Escherichia coli (ETEC) strains are one of the primary causes of diarrhea in newborn calves and in humans, pigs, and sheep. IgY technology has been identified as a promising alternative to generating a mass amount of specific antibody for use in immunotherapy and immunodiagnostics. The purpose of this study was to produce specific antibody by egg yolk antibody (IgY...
متن کاملFrac-seq reveals isoform-specific recruitment to polyribosomes.
Pre-mRNA splicing is required for the accurate expression of virtually all human protein coding genes. However, splicing also plays important roles in coordinating subsequent steps of pre-mRNA processing such as polyadenylation and mRNA export. Here, we test the hypothesis that nuclear pre-mRNA processing influences the polyribosome association of alternative mRNA isoforms. By comparing isoform...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: PLOS ONE
سال: 2016
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0150000