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Small nuclear ribonucleoprotein polypeptide A

U1A, U1A protein
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. [provided by RefSeq, Oct 2010] (from NCBI)
Top mentioned proteins: CAN, ACID, UIC, POLYMERASE, OUT
Papers on U1A
Use of the U1A Protein to Facilitate Crystallization and Structure Determination of Large RNAs.
Ferré-D'Amaré, Bethesda, United States. In Methods Mol Biol, Dec 2015
Once suitable crystals are obtained, the U1A protein, of known structure, can be employed to facilitate preparation of heavy atom or anomalously scattering atom derivatives, or as a source of partial model phases for the molecular replacement method.
IL-10, IL-12B and IL-17 gene polymorphisms in patients with mixed connective tissue disease.
Olesinska et al., Warsaw, Poland. In Mod Rheumatol, May 2015
In addition the -1082G/A IL-10 gene polymorphism was associated with esophageal involvement and with anti-U1-A and -C antibodies.
U1 snRNP is mislocalized in ALS patient fibroblasts bearing NLS mutations in FUS and is required for motor neuron outgrowth in zebrafish.
Reed et al., Boston, United States. In Nucleic Acids Res, May 2015
Here, we report that components of the U1 snRNP core particle (Sm proteins and U1 snRNA), but not the mature U1 snRNP-specific proteins (U1-70K, U1A and U1C), co-mislocalize with FUS to the cytoplasm in ALS patient fibroblasts harboring mutations in the FUS nuclear localization signal (NLS).
Native conformational dynamics of the spliceosomal U1A protein.
Gruebele et al., Urbana, United States. In J Phys Chem B, Apr 2015
The complex of spliceosomal U1A protein and its cognate SL2 RNA is a prototype system for protein-RNA binding studies.
Mechanisms of autoantibody production in systemic lupus erythematosus.
Reeves et al., Gainesville, United States. In Front Immunol, 2014
We show that the levels of autoantibodies against the U1A protein (part of a ribonucleoprotein) are markedly higher than autoantibodies against other antigens, including dsDNA and the non-nucleic acid-associated autoantigens insulin and thyroglobulin.
Maintenance of autoantibody production in pristane-induced murine lupus.
Reeves et al., Gainesville, United States. In Arthritis Res Ther, 2014
Naïve B cells, switched memory B cells, switched plasmablasts, and plasma cells were flow-sorted and total IgG and anti-U1A (RNP) autoantibodies were determined with ELISA.
Flexizymes: their evolutionary history and the origin of catalytic function.
Suga et al., Tokyo, Japan. In Acc Chem Res, 2012
The X-ray crystal structure, solved as a co-complex with phenylalanine ethyl ester and U1A-binding protein, revealed the structural basis of this enzyme.
U1A protein-stem loop 2 RNA recognition: prediction of structural differences from protein mutations.
Baranger et al., Middletown, United States. In Biopolymers, 2011
structural analysis of U1A protein-stem loop 2 RNA recognition
The small nuclear ribonucleoprotein U1A interacts with NS5 from yellow fever virus.
Nogueira et al., Ribeirão Preto, Brazil. In Arch Virol, 2011
study shows that the yellow fever virus (YFV) NS5 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 protein with U1A
Multistep kinetics of the U1A-SL2 RNA complex dissociation.
Baranger et al., Urbana, United States. In J Mol Biol, 2011
An analysis of the kinetic data suggests three phases of U1A-SL2 RNA complex dissociation with time scales of approximately 100 mus, 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.
Use of the spliceosomal protein U1A to facilitate crystallization and structure determination of complex RNAs.
Ferré-D'Amaré, Seattle, United States. In Methods, 2010
An approach that has resulted in 10 new RNA structures in the past decade is the use of the U1A crystallization module.
Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins.
Hughes et al., Toronto, Canada. In Nat Biotechnol, 2009
We tested RNAcompete by analyzing nine diverse RBPs (HuR, Vts1, FUSIP1, PTB, U1A, SF2/ASF, SLM2, RBM4 and YB1).
A bipartite U1 site represses U1A expression by synergizing with PIE to inhibit nuclear polyadenylation.
Gunderson et al., United States. In Rna, 2007
Functional U1A site in a cellular gene and of a single gene containing two dissimilar elements that inhibit nuclear polyadenylation.
Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3'-UTR.
Lutz et al., Newark, United States. In Rna, 2007
Identification of PSF, p54(nrb), PTB, and U1A as proteins specifically bound to the COX-2 polyadenylation signal upstream sequence elements .
The U1 snRNA hairpin II as a RNA affinity tag for selecting snoRNP complexes.
Fournier et al., Amherst Center, United States. In Methods Enzymol, 2006
In our approach, the U1A protein contains a unique affinity tag and is coexpressed in vivo with the tagged snoRNA to yield snoRNP-U1A complexes with two unique protein tags-one in the bound U1A protein and the other in the snoRNP core protein.
Kinetic studies of RNA-protein interactions using surface plasmon resonance.
Laird-Offringa et al., Los Angeles, United States. In Methods, 2002
In addition, we present examples to illustrate how kinetic studies have provided us with unique insights into the interaction of the spliceosomal U1A protein and the neuronal HuD protein with their respective RNA targets.
Poly(A) tail synthesis and regulation: recent structural insights.
Hall, United States. In Curr Opin Struct Biol, 2002
Recently determined structures of poly(A) polymerase, U1A and domains of the poly(A)-binding protein provide a framework for understanding the synthesis and regulation of the poly(A) tail.
Active disruption of an RNA-protein interaction by a DExH/D RNA helicase.
Pyle et al., New York City, United States. In Science, 2001
We demonstrate that the DExH protein NPH-II from vaccinia virus can displace the protein U1A from RNA in an active adenosine triphosphate-dependent fashion.
Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA.
Nagai et al., Cambridge, United Kingdom. In Nature, 1998
Unlike its close homologue the U1A protein, U2B" binds to its cognate RNA only in the presence of U2A', which contains leucine-rich repeats in its sequence.
Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation.
Varani et al., Cambridge, United Kingdom. In Nature, 1996
The human U1A protein binds an RNA hairpin during splicing, and regulates its own expression by binding an internal loop in the 3'-untranslated region of its pre-mRNA, preventing polyadenylation.
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