Results 1 to 10 of about 3,977 (97)
A catalatic nucleoprotein of baker's yeast [PDF]
FEBS Letters, 1978 Some years ago we reported the existence in Saccharomyces cerevisiae of an atypical catalase, which we named catalase A; upon purification, this proved to be a heme-containing tetramer with a lower molecular weight (180 000) than usual for catalases of any species [ 1.1. Catalase A did not cross-react irnmunologicahy [l] with the typical catalase (mol.
Tony Ching Ming Seah +2 more
openalex +5 more sources
Histochemical Studies on Nucleoproteins
Proceedings of the Japanese Histochemical Association, 1960 Ceroid pigment in paraffin sections loses its audanophilia due to methylation following a treatment with peracetic acid. Then the cell nucleus is found PAS reaction positive. In this case, it is observed that the nucleus is almost thionin unstainable.
Ryuei Maeda +2 more
openalex +3 more sources
Nucleoproteins of Cell Nuclei [PDF]
Proceedings of the National Academy of Sciences, 1942 A. E. Mirsky, Arthur W. Pollister
openalex +5 more sources
The Nucleoprotein and Phosphoprotein of Measles Virus [PDF]
Frontiers in Microbiology, 2019 Measles virus is a negative strand virus and the genomic and antigenomic RNA binds to the nucleoprotein (N), assembling into a helical nucleocapsid. The polymerase complex comprises two proteins, the Large protein (L), that both polymerizes RNA and caps the mRNA, and the phosphoprotein (P) that co-localizes with L on the nucleocapsid.
Guseva, Serafima +3 more
openaire +7 more sources
Architecture of a Polycomb Nucleoprotein Complex [PDF]
Molecular Cell, 2006 Polycomb group (PcG) epigenetic silencing proteins act through cis-acting DNA sequences, named Polycomb response elements (PREs). Within PREs, Pleiohomeotic (PHO) binding sites and juxtaposed Pc binding elements (PBEs) function as an integrated DNA platform for the synergistic binding of PHO and the multisubunit Polycomb core complex (PCC).
Tielenius Kruythoff-Mohd Sarip, Adone +5 more
openaire +4 more sources
Monomeric Nucleoprotein of Influenza A Virus
PLoS Pathogens, 2013 Isolated influenza A virus nucleoprotein exists in an equilibrium between monomers and trimers. Samples containing only monomers or only trimers can be stabilized by respectively low and high salt. The trimers bind RNA with high affinity but remain trimmers, whereas the monomers polymerise onto RNA forming nucleoprotein-RNA complexes.
Sylvie Chenavas +10 more
openaire +9 more sources
Conserved characteristics of the rhabdovirus nucleoprotein [PDF]
Virus Research, 2007 Rhabdovirus is a negative strand RNA virus that packages a ribonucleoprotein (RNP) complex. The RNP is composed of a genome that is encapsidated completely by the nucleoprotein (N). Structural comparisons of the RNA-nucleoprotein complexes from two members, vesicular stomatitis virus (VSV) and rabies virus (RABV), revealed highly conserved ...
Xin Zhang +4 more
openaire +3 more sources
Nucleoprotein Autoantibodies in Lupus Erythematosus
Journal of Investigative Dermatology, 1985 Autoantibodies against deoxyribonucleic acid (DNA) and ribonucleic acid (RNA) proteins are commonly detected in patients with lupus erythematosus (LE). Antibodies against native DNA are frequently detected in a subset of LE patients with a high prevalence of renal disease.
Luis A. Diaz +2 more
openaire +3 more sources
A nucleoprotein-hairpin in transcription regulation
Journal of Structural Biology, 2009 Regulation of gene transcription in both prokaryotes and eukaryotes involves the formation of DNA-multiprotein complexes. These complexes build a precise three-dimensional topology allowing communication between distal regions of DNA. The switch from early to late transcription in bacteriophage Ø29 involves binding of viral proteins, p4 and p6, to a ...
Gutiérrez del Arroyo, Paloma +5 more
openaire +5 more sources
Genome encapsidation by orthobunyavirus nucleoproteins [PDF]
Proceedings of the National Academy of Sciences, 2013 All negative-sense, single-stranded RNA (−ssRNA) viruses encode a nucleoprotein (NP), the major function of which is to bind viral RNAs and encapsidate them as ribonucleoprotein complexes (RNPs) (1, 2). Consequently, the genomes of −ssRNA viruses do not exist as naked RNA but rather as protein–RNA complexes with high-order structures. In PNAS, Li et al.
Wenjie Zheng, Yizhi Jane Tao
openaire +2 more sources