Results 341 to 350 of about 1,731,332 (381)

Identification of a nuclear protein matrix

Biochemical and Biophysical Research Communications, 1974
Abstract The structural framework of the rat liver nucleus has been identified and consists of a nuclear protein matrix. This matrix is 98.4% protein, 0.1% DNA, 1.2% RNA, and 0.5% phospholipid. The nuclear protein matrix is composed primarily of three acidic polypeptide fractions in the molecular weight range of 60–70,000 daltons.
Ronald Berezney, Donald S. Coffey
openaire   +3 more sources

Identity of nuclear membrane and non-histone nuclear proteins

Biochemistry, 1976
The fate of plasma and nuclear membrane polypeptides in preparations of acidic chromosomal protein from chicken erythrocytes has been investigated. It is shown that detergent extraction procedures (Nonidet P-40, Triton X-100, and saponin), commonly employed in the preparation of acidic chromosomal protein, cannot be relied upon to remove plasma and ...
openaire   +3 more sources

Nuclear Protein Transport Pathways

Nephron Experimental Nephrology, 1999
Nuclear proteins like transcription factors and ribosomal proteins are synthesized in the cytoplasm and have to be transported into the nucleus to fulfill their functions. The transport of proteins >20–60 kD through the nuclear pore complex (NPC) into the nucleus is an active, energy-requiring process.
Enno Hartmann, Matthias Köhler, Hermann Haller   +2 more
openaire   +3 more sources

NUCLEAR LOCALIZATION OF S‐100 PROTEIN

Journal of Neurochemistry, 1974
Abstract— S‐100 protein has been found in the nuclei isolated from the brain cortex of rabbit. The nuclear S‐100 constitutes a small portion (0.55 per cent) of the S‐100 present in the cytosol. Most of the large and pale nuclei appear to contain much more S‐100 than the small and dark ones.
A. Caniglia, Nicolo` Miani, Fabrizio Michetti, G. De Renzis, S. Correr   +4 more
openaire   +2 more sources

Nuclear Protein Import

2007
Entry into the eukaryotic cell nucleus occurs through multiple pathways involving specific targeting signals, and intracellular receptor molecules of the importin/karyopherin superfamily which recognise and dock the nuclear import substrates carrying these signals at the nuclear pore.
Jade K. Forwood, David A. Jans
openaire   +2 more sources

Protein synthesis in nuclear residual protein

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1965
1. The incorporation of radioactive amino acids into the nuclear residual protein from calf thymus has been investigated in vitro. 2. The nuclear residue has been found to incorporate actively [14C]tryptophan into its protein. 3. Optimal incorporation of [14C]tryptophan was obtained in the presence of Mg2+, adenosine 5′-triphosphate and an ...
Gordhan Patel, T. Y. Wang
openaire   +3 more sources

Immunolocalization of Nuclear Proteins [PDF]

, 1994
Immunohistochemistry permits the localization at the tissue and subcellular level of antigens for which specific antisera or monoclonal antibodies are available. A wide variety of methods are used for this purpose, and the best method for any particular application must unfortunately be determined empirically.
openaire   +1 more source

Pest sequences in nuclear proteins

International Journal of Biochemistry, 1993
1. Most of proteins which are rapidly degraded inside eukaryotic cells have been found to contain amino acid sequences (PEST sequences) enriched in proline, acidic residues (glutamic acid and/or aspartic acid) and hydrophilic residues (serine and threonine) (Rogers et al. (1986) Science 234, 364-368). 2.
openaire   +3 more sources

siRNA Screening of Nuclear Proteins

2014
Functional gene screening is a basic strategy for identifying candidate genes that are responsible for biological processes of interest to researchers. RNA-mediated interference (RNAi)-based screening is one such approach. Although the knockdown technique using siRNA is widely accepted, careful evaluation is required to avoid false positive candidates ...
Yuko Hasegawa, Shinichi Nakagawa
openaire   +3 more sources

Nuclear protein tyrosine kinases

Trends in Biochemical Sciences, 1994
Protein tyrosine phosphorylation plays an important role in the transduction of extracellular signals. The prototypical protein tyrosine kinases are localized at the plasma membrane and are coupled to receptors that bind extracellular factors. Thus, protein tyrosine phosphorylation was previously thought to occur only in the cytoplasm. However, several
openaire   +3 more sources