Results 321 to 330 of about 121,107 (346)

Biogenesis of small nucleolar ribonucleoproteins

Current Opinion in Cell Biology, 2002
Eukaryotic cells contain a very complex population of small nucleolar RNAs. They function, as small nucleolar ribonucleoproteins, in pre-ribosomal RNA processing reactions, and also guide methylation and pseudouridylation of ribosomal RNA, spliceosomal small nuclear RNAs, and possibly other cellular RNAs.
Vanda Pogacic, Witold Filipowicz
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The nucleolus: a site of ribonucleoprotein maturation

Current Opinion in Cell Biology, 2003
The nucleolus is the site of ribosomal RNA synthesis, processing and ribosome maturation. Various small ribonucleoproteins also undergo maturation in the nucleolus, involving RNA modification and RNA-protein assembly. Such steps and other activities of small ribonucleoproteins also take place in Cajal (coiled) bodies.
Anton V. Borovjagin, Thilo S. Lange, Susan A. Gerbi   +2 more
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CHARACTERIZATION OF BRAIN RIBONUCLEOPROTEIN PARTICLES

Journal of Neurochemistry, 1979
Abstract— Brain RNP particles were characterized to determine whether they play a role in the regulation of brain protein synthesis. RNP particles were isolated from the postribosomal supernatant of cerebral hemispheres of young rabbits, employing conditions which minimize adventitious protein‐RNA interactions.
James B. Mahony, Ian R. Brown
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Ribonucleoprotein interaction with mammalian monosomes

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1968
Abstract A subcellular fraction containing RNA and protein was prepared from rabbit reticulocytes. This fraction had a sedimentation behavior which was different from reticulocyte ribosomal subunits, and was capable of stimulating polypeptide synthesis in a mammalian cell-free system.
Austin S. Weisberger, Steven A. Armentrout   +1 more
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Changes in hepatic ribonucleoproteins in Kwashiorkor

The Indian Journal of Pediatrics, 1973
Using the toluidine blue-ammonium molybdate staining method, different types of RNPs were demonstrated in the hepatocytes of patients with kwashiorkor. DCR-I and DCR-III were found to be reduced. Nucleolar chromatin and nucleolar parachromatin showed an apparent increase.
Vasudha Agarwal, T. P. Bharadwaj
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A Ribonucleoprotein from Amphibian Gastrulæ

Nature, 1958
DISAGGREGATION of amphibian embryos by agents which chelate calcium is succeeded by re-aggregation if the cells are returned to a medium containing calcium1. It is customary to consider that the removal of calcium from the environment of the cells is responsible for the loss of adhesion displayed in disaggregation.
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Heterogeneous nuclear ribonucleoprotein complexes

Molecular Biology Reports, 1990
Heterogeneous nuclear r ibonuc leopro te ins (hnRNPs) associate with RNA polymerase II transcripts immediately following the initiation of transcription to form hnRNP complexes. These structures are the functional assemblies within which hnRNAs and pre-mRNAs exist in the nucleus.
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Enzyme activity of nuclear ribonucleoproteins

Experimental Cell Research, 1977
Abstract Ultrastructural localization of β-glycerophosphatase, glucose-6-phosphatase, ATPase and NAD pyrophosphorylase was investigated in isolated mouse liver nuclei. β-Glycerophosphatase activity was found in interchromatin granules, in nuclear membranes, perinuclear space, and in nuclear pores.
E. Unger, I.B. Buchwalow
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Ribonuclease P: a ribonucleoprotein enzyme

Current Opinion in Chemical Biology, 2000
The ribonucleoprotein ribonuclease P catalyzes the hydrolysis of a specific phosphodiester bond in precursor tRNA to form the mature 5' end of tRNA. Recent studies have shed light on the structures of RNase-P-RNA-P-protein and RNase-P-RNA-precursor-tRNA complexes, as well as on the positions of catalytic metal ions, emphasizing the importance of the ...
Jeffrey C. Kurz, Carol A. Fierke
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Ribonucleoprotein complexes in neurologic diseases

Current Opinion in Neurobiology, 2008
Ribonucleoprotein (RNP) complexes regulate the tissue-specific RNA processing and transport that increases the coding capacity of our genome and the ability to respond quickly and precisely to the diverse set of signals. This review focuses on three proteins that are part of RNP complexes in most cells of our body: TAR DNA-binding protein (TDP-43), the
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