Results 221 to 230 of about 1,114,768 (261)

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.
M, Köhler, H, Haller, E, Hartmann
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Protein dynamics in the nuclear compartment

Current Opinion in Genetics & Development, 2002
The classic view of a transcriptional initiation complex is that of an assembly of factors with many protein-protein contacts, leading to a multi-component complex whose existence is a result of the stabilizing influence of the many intermolecular interactions.
Gordon L, Hager, Cem, Elbi, Matthias, Becker   +2 more
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Nuclear protein kinase C

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2006
Protein kinase C (PKC) isozymes constitute a family of ubiquitous phosphotransferases which act as key transducers in many agonist-induced signaling cascades. To date, at least 11 different PKC isotypes have been identified and are believed to play distinct regulatory roles. PKC isoforms are physiologically activated by a number of lipid cofactors. PKC
MARTELLI, ALBERTO MARIA, EVANGELISTI, CAMILLA, Nyakern M., MANZOLI, FRANCESCO ANTONIO   +3 more
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gCap39 is a nuclear and cytoplasmic protein

Cell Motility, 1993
AbstractgCap39 is a newly identified member of the Ca2+‐ and polyphosphoinositidemodulated gelsolin family of actin binding proteins which is different from gelsolin in several important respects: it caps filament ends, it does not sever filaments, it binds reversibly to actin, it is phosphorylated in vivo, and it is also present in the nucleus. gCap39
K, Onoda, F X, Yu, H L, Yin
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An inhibitor protein of nuclear protein kinases

Nature, 1979
THE cyclical phosphorylation and dephosphorylation of proteins, catalysed by protein kinases and phosphoprotein phosphatases, respectively, are important ways in which cells regulate many of their metabolic activities. Cells seem to have at least two distinct phosphorylation systems, one in the cytoplasm, the other in the nucleus.
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Characterization of a Sperm Nuclear Protein

American Journal of Reproductive Immunology, 1996
PROBLEM: The molecular identity of sperm DNA‐binding structural proteins contributing to the integrity of a sperm residual high salt/nuclease resistant nuclear structure is studied by cDNA cloning and monoclonal antibodies to the recombinant polypeptide.
I N, Batova, M G, Petrov, S D, Kyurkchiev, I R, Kehayov   +3 more
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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
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Nuclear Proteins of Neoplastic Cells

1964
Publisher Summary Proteins and enzymes of the nucleus are important for the synthetic reactions involved in neoplastic cells and to the aberrations of growth that characterize these cells. It has been difficult to isolate and purify the proteins of the nucleus but in recent years, the enzymatic activities of some of these proteins have been ...
H, BUSCH, W J, STEELE
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Nuclear Pore Complex Proteins

1996
The nuclear envelope forms the boundary between the nucleus and the cytoplasm and as such regulates the exchange of macromolecules between the two compartments. The channels through the nuclear envelop that actually mediate this macromolecular traffic are the nuclear pore complexes.
R, Bastos, N, Panté, B, Burke
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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.
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