Alternative Splicing: Molecular Mechanisms, Biological Functions, Diseases, and Potential Therapeutic Targets. [PDF]
MedComm (2020)Alternative splicing (AS) expands proteomic diversity and functional complexity in eukaryotes, regulated by spliceosomal components, RNA elements, and epigenetic modifications. Dysregulated AS contributes to diseases, including cancer, neurodegenerative disorders, and cardiovascular conditions, among others. Therapeutic interventions, such as antisense
Zhu ZM +5 more
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Autoantibodies to ribonucleoprotein particles containing U2 small nuclear RNA. [PDF]
The EMBO Journal, 1985 Autoantibodies exclusively precipitating U1 and U2 small nuclear ribonucleoprotein (snRNP) particles [anti-(U1,U2)RNP] were detected in sera from four patients with autoimmune disorders. When tested by immunoblotting, these sera recognized up to four different protein antigens in purified mixtures of U1-U6 RNP particles.
W, Habets +4 more
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Mutations in an Essential U2 Small Nuclear RNA Structure Cause Cold-Sensitive U2 Small Nuclear Ribonucleoprotein Function by Favoring Competing Alternative U2 RNA Structures [PDF]
Molecular and Cellular Biology, 1994 Mutations in stem-loop IIa of yeast U2 RNA cause cold-sensitive growth and cold-sensitive U2 small nuclear ribonucleoprotein function in vitro. Cold-sensitive U2 small nuclear RNA adopts an alternative conformation that occludes the loop and disrupts the stem but does so at both restrictive and permissive temperatures.
M I, Zavanelli +3 more
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Human U1 and U2 small nuclear ribonucleoproteins contain common and unique polypeptides. [PDF]
Molecular and Cellular Biology, 1982 Immunoprecipitation of human small nuclear ribonucleoproteins (snRNPs) containing the small nuclear RNAs U1, U2, U4, U5, and U6 with two antibodies produced in certain patients suffering from systemic lupus erythematosus was used to identify the polypeptides present on human U1 and U2 snRNPs. U1 and U2 snRNPs contain both common and unique polypeptides;
C S, Kinlaw +2 more
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Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. [PDF]
Proceedings of the National Academy of Sciences, 1989 Binding of U2 small nuclear ribonucleoprotein (snRNP) to the pre-mRNA branch site is an early step in spliceosome assembly and appears to commit a pre-mRNA to the splicing pathway. We have shown previously that this ATP-dependent binding requires a non-rnRNP factor, U2 snRNP auxiliary factor (U2AF), in addition to U2 snRNP.
P D, Zamore, M R, Green
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The C-group Heterogeneous Nuclear Ribonucleoprotein Proteins Bind to the 5′ Stem-Loop of the U2 Small Nuclear Ribonucleoprotein Particle [PDF]
Journal of Biological Chemistry, 1996 The C-group heterogeneous nuclear ribonucleoprotein (hnRNP) proteins bind to nascent pre-messenger RNA. In vitro studies have indicated that the C hnRNP proteins bind particularly strongly to the intron polypyrimidine tract of pre-mRNA and may be important for pre-mRNA splicing.
J, Temsamani, T, Pederson
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Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit. [PDF]
Proceedings of the National Academy of Sciences, 1992 U2 small nuclear ribonucleoprotein auxiliary factor (U2AF), an essential mammalian splicing factor, is composed of two subunits: a 65-kDa protein (U2AF65), which binds the pre-mRNA polypyrimidine tract and is required for in vitro splicing, and an associated 35-kDa protein (U2AF35). Here we report the isolation of a cDNA encoding U2AF35.
Zhang, M. +4 more
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Direct Interactions between Pre-mRNA and Six U2 Small Nuclear Ribonucleoproteins during Spliceosome Assembly [PDF]
Molecular and Cellular Biology, 1994 Highly purified mammalian spliceosomal complex B contains more than 30 specific protein components. We have carried out UV cross-linking studies to determine which of these components directly contacts pre-mRNA in purified prespliceosomal and spliceosomal complexes.
D, Staknis, R, Reed
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Probing Interactions between the U2 Small Nuclear Ribonucleoprotein and the DEAD-box Protein, Prp5 [PDF]
Journal of Biological Chemistry, 2002 Pre-mRNA binding to the yeast U2 small nuclear ribonucleoprotein (snRNP) during prespliceosome formation requires ATP hydrolysis, the highly conserved UACUAAC box of the branch point region of the pre-mRNA, and several factors. Here we analyzed the binding of a radiolabeled 2'-O-methyl oligonucleotide complementary to U2 small nuclear RNA to study ...
Barham K Abu, Abu Dayyeh +3 more
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Ser/Arg-rich Protein-mediated Communication between U1 and U2 Small Nuclear Ribonucleoprotein Particles [PDF]
Journal of Biological Chemistry, 2004 Previous work demonstrated that U1 small nuclear ribonucleoprotein particle (snRNP), bound to a downstream 5' splice site, can positively influence utilization of an upstream 3' splice site via exon definition in both trans- and cis-splicing systems. Although exon definition results in the enhancement of splicing of an upstream intron, the nature of ...
Lisa A, Boukis +3 more
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