Results 161 to 170 of about 35,404 (208)

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.
openaire   +2 more sources

Small Cytoplasmic Ribonucleoproteins

2013
It is now well established that most RNAs are tightly associated with one or more proteins to generate nuclear or cytoplasmic ribonucleoprotein (RNP) complexes. Over 30 years ago, Lerner, Steitz, and coworkers found that the proteic components of these complexes made up some of the antigens recognized by sera of patients affected by systemic lupus ...
ROMANO, MAURIZIO, BURATTI, EMANUELE
openaire   +2 more sources

Influenza virus messenger ribonucleoprotein

Virology, 1975
Abstract Evidence is presented which indicates that influenza virus messenger RNA exists on polysomes, not as free RNA but in the form of a ribonucleoprotein (RNP). The data make it appear extremely unlikely that the presence of RNP on polysomes is an artifact of the extraction procedure.
openaire   +2 more sources

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.
J B, Mahony, I R, Brown
openaire   +2 more sources

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
openaire   +1 more source

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
openaire   +2 more sources

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.
openaire   +1 more source

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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources