Results 261 to 270 of about 26,288 (294)

Autoantibodies to Ribonucleoproteins

Clinics in Rheumatic Diseases, 1985
Presently we recognize at least 12 different autoantibodies that involve ribonucleoproteins as antigens in patients with SLE and other rheumatic diseases. Such autoantibodies have a number of clinically useful diagnostic associations. Moreover, they have proved to be powerful tools for understanding the structure and function of a variety of cellular ...
J A, Hardin, T, Mimori
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Antibodies in Ribonucleoproteins

Nature, 1960
IN many hypotheses concerning the mechanism of the immune response the nucleic acids have been assigned a role in the production of antibodies, although no clear evidence for their participation is yet available. As regards protein synthesis in general, there is reason for believing that the ribonucleoproteins lie in the pathway of this synthetic ...
M, FELDMAN, D, ELSON, A, GLOBERSON
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Informational ribonucleoprotein particles of newt oocytes: Polyribosome-associated ribonucleoproteins

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1974
Various species of rapidly labelled, informational ribonucleoproteins can be isolated from homogenates of newt oocytes. Polyribosome-associated ribonucleoprotein can be separated from heterogeneous nuclear ribonucleoprotein and free cytoplasmic ribonucleoprotein by sucrose gradient centrifugation.
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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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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
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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.
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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.
J B, Mahony, I R, Brown
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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.
Witold, Filipowicz, Vanda, Pogacić
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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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