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The protein encoded by SNRPA associates with stem loop II of the U1 small nuclear ribonucleoprotein, which binds the 5' splice site of precursor mRNAs and is required for splicing. Additionally we are shipping Small Nuclear Ribonucleoprotein Polypeptide A Antibodies (96) and Small Nuclear Ribonucleoprotein Polypeptide A Kits (4) and many more products for this protein.
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p65 (show GORASP1 Proteins) activation triggered by TCR signaling could promote SNRPA transcription and 3' UTR shortening of STAT5B (show STAT5B Proteins). Thus we propose that the alternative polyadenylation switching of STAT5B (show STAT5B Proteins) induced by TCR activation is mediated by SNRPA.
a new mechanism for regulating SMN (show STMN1 Proteins) levels and provides new insight into the roles of U1A in 3' processing of mRNAs.
An analysis of the kinetic data suggests three phases of U1A-SL2 (show MMP10 Proteins) RNA complex dissociation with time scales of approximately 100 mus (show TRPV6 Proteins), approximately 50 ms, and approximately 2 s. We propose that the first step of dissociation is a fast rearrangement of the complex to form a loosely bound complex.
structural analysis of U1A protein-stem loop 2 RNA recognition
study shows that the yellow fever virus (YFV) NS5 (show RAF1 Proteins) protein is able to interact with U1A, a protein involved in splicing and polyadenylation; a region between amino acids 368 and 448 was identified as the site of interaction of the NS5 (show RAF1 Proteins) protein with U1A
13)C NMR relaxation studies of base and ribose dynamics for the RNA internal loop target of human U1A protein located within the 3'-untranslated region (3'-UTR) of the mRNA coding for U1A itself
Identification of PSF (show IGFBP7 Proteins), p54(nrb (show NONO Proteins)), PTB (show PTBP1 Proteins), and U1A as proteins specifically bound to the COX-2 polyadenylation signal upstream sequence elements .
Functional U1A site in a cellular gene and of a single gene containing two dissimilar elements that inhibit nuclear polyadenylation.
We found that only the modified U1 snRNA (IVS-AAA (show AAAS Proteins)) that completely matched both the intronic and exonic U1 binding sequences of the mutated DDC (show DDC Proteins) gene could correct splicing errors of either the mutated human DDC (show DDC Proteins) minigene or the mouse artificial splicing construct in vitro
Endogenous non-snRNP associated U1A inhibits poly(A) polymerase activity proportional to U1A recovered, suggesting that available U1A level alone is responsible for changes in its inhibitory effect at the secretory IgM poly (A) site.
tissue expression analysis indicated that that swine SDHB (show SDHB Proteins), SNRPA and CRYBB1 (show CRYBB1 Proteins) gene were differentially expressed in tissues including fat, lung, muscle, small intestine, kidney, large intestine, spleen and liver
The protein encoded by this gene associates with stem loop II of the U1 small nuclear ribonucleoprotein, which binds the 5' splice site of precursor mRNAs and is required for splicing. The encoded protein autoregulates itself by polyadenylation inhibition of its own pre-mRNA via dimerization and has been implicated in the coupling of splicing and polyadenylation.
U1 small nuclear RNP-specific A
, U1 small nuclear ribonucleoprotein A
, U1 snRNP A
, U1 snRNP-specific protein A
, U1 snRNP protein A
, protein A of the U1 small nuclear RNA
, sans fille