Results 351 to 360 of about 167,361 (378)

Ribonucleoprotein particles from Escherichia coli

Journal of Molecular Biology, 1959
In exponential cultures, 25% of the dry weight of E. coli is accounted for by RNA. Of this about 80 to 90% is present in ribonucleoprotein particles and 10 to 20% in the “soluble” or “non-sedimentable” fraction. Magnesium stabilizes the particles, and on varying its concentration, four kinds of components are observed, with sedimentation constants of
A. TISSIÈRES, J.D. WATSON, D. SCHLESSINGER, B.R. HOLLINGWORTH   +3 more
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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.
S A, Armentrout, A S, Weisberger
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Small cytoplasmic ribonucleoproteins

Trends in Genetics, 1985
Abstract Structurally diverse, small cytoplasmic ribonucleoproteins (scRNPs) exist in eukaryotic cells. VAI RNA encoded by adenovirus and the 7SL RNA-containing signal recognition particle function at different steps in the synthesis of proteins and the targeting of these proteins to subcellular compartments.
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D-RNA Containing Ribonucleoprotein Particles

1971
This paper will deal with ribonucleoprotein particles containing D-RNA or RNA with a DNAlike base composition. This RNA is characterized by a high AU-content, heterogeneity with respect to molecular weight, a relatively rapid turnover, and the ability to stimulate amino acid incorporation in a cell-free system.
G P, Georgiev, O P, Samarina
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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.
I B, Buchwalow, E, Unger
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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 ...
J C, Kurz, C 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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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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Ribonucleoprotein localization in mouse oocytes

Methods, 2011
RNA molecules rarely function alone in cells. For most RNAs, their function requires formation of various ribonucleoprotein (RNP) complexes. For example, mRNP composition can determine mRNA localization, translational repression, level of translation or mRNA stability. RNPs are usually studied by biochemical methods. However, biochemical approaches are
Matyas, Flemr, Petr, Svoboda
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Isolation of messenger-like ribonucleoproteins

Biochemistry, 1975
Subribosomal and polyribosomal messenger ribonucleoproteins (mRNPs) were isolated from Ehrlich ascites tumor cells by a method involving sedimentation of polyribosomal and subribosomal particles, dissociation with EDTA, and rate-zonal sedimentation.
A, Barrieux, H A, Ingraham, D N, David, M G, Rosenfeld   +3 more
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