Results 241 to 250 of about 24,694 (278)
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Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1981
hnRNP are made of two classes of unit, monoparticles and heterogeneous complexes. The monoparticles are much more easily dissociated by salt than the heterogeneous complexes. We made use of this differential salt sensitivity to determine the localization of snRNA in hnRNP.
H, Gallinaro, M, Jacob
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hnRNP are made of two classes of unit, monoparticles and heterogeneous complexes. The monoparticles are much more easily dissociated by salt than the heterogeneous complexes. We made use of this differential salt sensitivity to determine the localization of snRNA in hnRNP.
H, Gallinaro, M, Jacob
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Saccharomyces cerevisiae telomerase is an Sm small nuclear ribonucleoprotein particle
Nature, 1999Activation of the chromosome end-replicating enzyme telomerase can greatly extend the lifespan of normal human cells and is associated with most human cancers. In all eukaryotes examined, telomerase has an RNA subunit, a conserved reverse transcriptase subunit and additional proteins, but little is known about the assembly of these components.
A G, Seto +4 more
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Are U4 small nuclear ribonucleoproteins involved in polyadenylation?
Nature, 1984The mechanism whereby eukaryotic pre-messenger RNAs are polyadenylated is unknown. Most models for polyadenylation invoke cleavage of precursor transcripts at the site of poly(A) addition followed by polymerization of A residues by poly(A) polymerase. Analysis of the sequences surrounding poly(A) addition sites has identified the consensus recognition ...
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The role of small nuclear ribonucleoprotein particles in pre-mRNA splicing
Nature, 1987A small set of distinctive short RNA molecules are found in the nuclei of all higher eukaryotic cells and yeast, in protein complexes known as 'small nuclear ribonucleoprotein particles', or snRNPs. Recent work has confirmed early suggestions that these particles form part of the machinery by which primary RNA transcripts are processed to their mature,
T, Maniatis, R, Reed
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1990
Publisher Summary The snRNAs exist in the cell as ribonucleoprotein (RNP) complexes. While the snRNAs U1, U2, and U5 are organized in separate RNP particles, the majority of the snRNAs U4 and U6 reside in a single RNP complex. Several proteins in the molecular weight range of 25K to 200K were recently identified as possible U5-specific proteins ...
M, Bach, P, Bringmann, R, Lührmann
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Publisher Summary The snRNAs exist in the cell as ribonucleoprotein (RNP) complexes. While the snRNAs U1, U2, and U5 are organized in separate RNP particles, the majority of the snRNAs U4 and U6 reside in a single RNP complex. Several proteins in the molecular weight range of 25K to 200K were recently identified as possible U5-specific proteins ...
M, Bach, P, Bringmann, R, Lührmann
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The small nuclear ribonucleoproteins, SmB and B', are products of a single gene
Gene, 1991Nucleotide sequencing of HeLa genomic DNA amplified by the polymerase chain reaction revealed 696-bp and 841-bp introns within the gene encoding the proteins SmB and SmB', respectively. Since splice consensus sequences were observed flanking the 145-bp insertion detected in the cDNA encoding SmB, we conclude that SmB and SmB' are derived from ...
J L, Chu, K B, Elkon
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Interactions between small nuclear ribonucleoprotein particles in formation of spliceosomes
Cell, 1987Electrophoretic separation of ribonucleoprotein particles in a nondenaturing gel was used to analyze the splicing of mRNA precursors. Early in the reaction, a complex formed consisting of the U2 small nuclear ribonucleoprotein particle (snRNP) bound to sequences upstream of the 3' splice site. This complex is modeled as a precursor of a larger complex,
M M, Konarska, P A, Sharp
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Journal of molecular biology, 1985
A small nuclear ribonucleoprotein, U1 snRNP, has been implicated in mRNA processing. In this investigation sites of protein binding on U1 RNA were mapped by nuclease protection and RNA sequencing. Partially purified human U1 snRNP was sequentially digested with Escherichia coli RNAase III and S1 nuclease.
W L, Lin, T, Pederson
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A small nuclear ribonucleoprotein, U1 snRNP, has been implicated in mRNA processing. In this investigation sites of protein binding on U1 RNA were mapped by nuclease protection and RNA sequencing. Partially purified human U1 snRNP was sequentially digested with Escherichia coli RNAase III and S1 nuclease.
W L, Lin, T, Pederson
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Peptide autoantigenicity of the small nuclear ribonucleoprotein C.
Clinical and experimental rheumatology, 1995This study determines the antigenic regions of the nRNP C lupus autoantigen.Twenty-one anti-nRNP C sera, six patients with other autoimmune serology, and five normal control sera were assessed for binding with the overlapping octapeptides of the nRNP C protein.
J A, James, J B, Harley
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Structural analysis of U small nuclear ribonucleoproteins by in vitro assembly
1990Publisher Summary U small nuclear ribonucleoproteins (snRNPs) are essential cofactors in the splicing process of lower as well as higher eukaryotes. The major U snRNPs (U1, U2, U4-U6) of higher eukaryotes and the yeast counterparts are required to remove introns from messenger RNA precursors.
J, Hamm, I W, Mattaj
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