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Thus, B52 is an essential gene and has a critical role in Drosophila development. Paper-135970.
It binds B52 in vivo and suppresses all phenotypes caused by B52 overexpression. Paper-1999826.
Additional cDNA clones reflect extensive alternative splicing of SRp40 and SRp55 pre-mRNAs. Paper-361326.
Germ line transformation of Drosophila flies with B52 genomic DNA rescues this lethality. Paper-135970.
Drosophila SRp55 also functions as an alternative splicing factor in the human cell-free system. Paper-7507858.
Specific role of the SR protein splicing factor B52 in cell cycle control in Drosophila. Paper-11825869.
Mutations in B52 restore S phase in clones of de2f1 mutant cells and phenocopy the loss of the de2f2 function. Paper-11825869.
Other SR protein family members isolated from these larvae could substitute for B52 splicing activity in vitro. Paper-2054212.
In Chironomus tentans, hrp45 is an SR protein structurally similar to the Drosophila SRp55/ B52 SR protein. Paper-12293123.
In this work, we show that the de2f1 mutant phenotype is rescued by the loss of the pre-mRNA splicing factor SR protein B52. Paper-11825869.
The splicing factor B52/ SRp55 binds within the alternative spliced exon 3a and plays a role in this alternative splicing event. Paper-13668764.
We have used indirect immunofluorescence of polytene chromosomes to examine the chromatin distribution of a 52-kD Drosophila protein designated B52. Paper-6897545.
The predicted primary amino acid sequence of B52 reveals two regions with similarities to a number of other proteins known to interact with nucleic acids. Paper-6897545.
Microarray analyses revealed that many transcripts involved in brain organogenesis have altered splicing profiles upon both loss and gain of B52 function. Paper-12479998.
These results indicate that B52 has unique functions in the removal of some introns during development, and plays a critical role in cellular regulatory networks. Paper-9853442.
We have also identified a 46-kDa protein from Chironomus tentans that binds Drosophila B52 antibodies and has a distribution on chromosomes analogous to B52. Paper-8089415.
The most abundant family members in human (SRp33) and Drosophila ( SRp55) cell lines can replace one another as essential splicing factors in a human cell-free system. Paper-7507858.
Analysis of cloned cDNAs shows that SRp55 and SF2 are highly related and reveals regions of similarity to genetically defined regulators of alternative splicing in Drosophila. Paper-7507858.
B52 is localized to transcriptionally active loci and, at the highly decondensed heat shock loci, can be seen to bracket the RNA polymerase II fluorescence signals symmetrically. Paper-6897545.
To investigate the RNA-binding specificity of B52, we isolated B52-binding RNAs by selection and amplification from a pool of random RNA sequences by using full-length B52 protein as the target. Paper-985688.
The omegaspeckles are distinct from interchromatin granules since nuclear speckles containing serine/ arginine-rich SR-proteins like SC35 and SRp55 did not colocalize with the &ohgr; speckles. Paper-8595750.
Although the SR proteins dASF/ SF2 and B52 caused defects in ommatidia structure, only B52 impaired normal axonal projections of photoreceptors and neurogenesis in visual ganglia. Paper-12479998.
The predicted amino acid sequence of rbp1 is similar to those of the human splicing factor ASF/ SF2, the Drosophila nuclear phosphoprotein SRp55, and the Drosophila puff-associated protein B52. Paper-7222139.
Almost all of the corresponding genes having a known function encode either transcription factors or components of signal transduction pathways, with the B52- binding fragments located to not only exonic but also intronic regions. Paper-9853442.
We have also examined the distribution of B52 on nonpolytene chromosomes in Drosophila cell cultures with an in vivo UV cross-linking method and find that, here too, B52 is associated with boundaries of transcriptionally active chromatin. Paper-6897545.
Immunofluorescence analysis of polytene chromosomes has shown that B52 generally colocalizes with RNA polymerase II; however, in contrast to other splicing factors, B52 brackets RNA polymerase II at highly active heat-shock puffs. Paper-8089415.
To gain insight into splicing regulation, we developed a microarray to assay all annotated alternative splicing events in Drosophila melanogaster and identified the alternative splice events controlled by four splicing regulators: dASF/SF2, B52/ SRp55, hrp48, and PSI. Paper-11017835.
These synonyms are used for gene B52 (CG10851 gene product from transcript CG10851-RB): SRP55, SRp55, SR55, Serine-arginine protein 55, RSp55, RS55, RRM8, Rbp8, Protein enhancer of deformed, MabB52, l(3)s2249, E726, E(Dfd), dSRp55, Dmel\CG10851, CG10851, B52 protein, B52/SRp55, B52/dSRp55, 52 kDa bracketing protein.
These accession numbers are used for gene B52: Q8ING9 (UNIPROT__AC), Q8ING8 (UNIPROT__AC), CAA44483 (NCBI_GENBANK__AC), AAN71172 (NCBI_GENBANK__AC).
B52 is a homologue of sfrs6b (splicing factor, arginine/serine-rich 6b) from Danio rerio.
B52 is a homologue of sfrs6a (splicing factor, arginine/serine-rich 6a) from Danio rerio.
B52 is a homologue of SFRS6 (splicing factor, arginine/serine-rich 6) from Homo sapiens.
B52 is a homologue of SFRS6 (splicing factor, arginine/serine-rich 6) from Bos taurus.
B52 is a homologue of SFRS6 (splicing factor, arginine/serine-rich 6) from Gallus gallus.
B52 is a homologue of Sfrs6 (splicing factor, arginine/serine-rich 6) from Mus musculus.
B52 is a homologue of Sfrs6 (splicing factor, arginine/serine-rich 6) from Rattus norvegicus.
B52 is a homologue of rsp-1 (SR Protein (splicing factor)) from Caenorhabditis elegans.
B52 is a homologue of AgaP_AGAP004592 (AGAP004592-PA) from Anopheles gambiae str. PEST.
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