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Immunomodulatory Properties of Morbillivirus Nucleoproteins
Viral Immunology, 2006Morbillivirus infections have been known for a long time to be associated with an acute immunosuppression in their natural hosts. Here, we show that recombinant Morbillivirus nucleoproteins from canine distemper virus, peste-des-petits-ruminants virus, and Rinderpest virus bind B-lymphocytes from dogs, goats, and cattle, respectively, similarly to ...
Kerdiles, Yann +9 more
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Canadian Journal of Medical Sciences, 1953
A review of work in the bacteriophage field is presented. The discussion is concerned mainly with biochemical aspects of the problem but some reference is also made to genetic studies.
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A review of work in the bacteriophage field is presented. The discussion is concerned mainly with biochemical aspects of the problem but some reference is also made to genetic studies.
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The Nucleoproteinic System [PDF]
, 1991 Our roots reach back to the depths of the past. The grand process — at least within our view of space and time — seems to have endeavored over a period of 10–20 billion years to gain a certain consciousness and understanding of itself. Together with the universe, life patterns originated in their early infancy from an alien phase transition between ...
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Polyelectrolyte properties of nucleoproteins
Journal of Electroanalytical Chemistry and Interfacial Electrochemistry, 1981Abstract Two types of nucleoproteins, viz. reconstituted SV 40 minichromosomes and polymers of chromatin subunits (polynucleosomes), were studied by sedimentation velocity analysis in relation to the ionic strength. The representation of the sedimentation coefficients s app 20,w as a function of the Debye—Huckel electrostatic screening radius 1 ...
Ruth Lindigkeit +4 more
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Energy Transfer in Nucleoproteins
International Journal of Radiation Biology and Related Studies in Physics, Chemistry and Medicine, 1967SummaryArtificial nucleoproteins have been made by complexing DNA with the proteins BSA, trypsin and salmine and also with the polypeptide, poly-L-lysine. These nucleoproteins have been irradiated with gamma-rays and examined using electron spin resonance techniques.
B.B. Singh, A. Charlesby, A.D. Lenherr
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Raman Spectroscopy of Proteins and Nucleoproteins
Current Protocols in Protein Science, 2013AbstractA protein Raman spectrum comprises discrete bands representing vibrational modes of the peptide backbone and its side chains. The spectral positions, intensities, and polarizations of the Raman bands are sensitive to protein secondary, tertiary, and quaternary structures and to side‐chain orientations and local environments. In favorable cases,
Daniel Nemecek +3 more
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Enzymic degradation of thymus nucleoprotein
Biochimica et Biophysica Acta, 1963Abstract Gel-forming deoxyribonucleprotein from calf thymus was treated separately with DNAase II, trypsin and chymotrypsin. The rate of decrease in rigidity and viscosity, the solubilization of DNA and histone products, and the hydrolysis of peptide bonds were followed. 1. 1. A complete loss of rigidity was obtained either by the scission of the
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Physical properties of thymus nucleoprotein
Biochimica et Biophysica Acta, 1954Abstract 1. 1. Nucleoprotein prepared by washing with dilute salt solution and extracting with water can be obtained mainly in the form of a highly aggregated gel-like material. 2. 2. The dispersed nucleoprotein obtained by several previous investigators is probably formed by enzymic degradation of the gel-like material.
P.F. Davison +2 more
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In vitro selection of nucleoprotein enzymes
Nature Biotechnology, 2001Natural nucleic acids frequently rely on proteins for stabilization or catalytic activity. In contrast, nucleic acids selected in vitro can catalyze a wide range of reactions even in the absence of proteins. To augment selected nucleic acids with protein functionalities, we have developed a technique for the selection of protein-dependent ribozyme ...
Andrew D. Ellington +1 more
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Transcript elongation on a nucleoprotein template
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 2002Chromatin forms a general, repeating barrier to elongation of transcripts by eukaryotic RNA polymerases. Recent studies of nucleosome structure and histone modifications reveal a set of likely mechanisms for control of elongation through chromatin.
Jennifer L Speer +2 more
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