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2002
Publisher Summary This chapter discusses the process of nuclear protein transport. Work on the mechanism of nuclear transport has led to a fairly detailed understanding of how proteins are targeted for import or export. This work has changed the way in which researchers need to think about potential transport mechanisms for their own protein of ...
Anita H. Corbett+2 more
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Publisher Summary This chapter discusses the process of nuclear protein transport. Work on the mechanism of nuclear transport has led to a fairly detailed understanding of how proteins are targeted for import or export. This work has changed the way in which researchers need to think about potential transport mechanisms for their own protein of ...
Anita H. Corbett+2 more
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Phosphorylation of nuclear proteins
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1983Many nuclear proteins are phosphorylated: they range from enzymes to several structural proteins such as histones, non-histone chromosomal proteins and the nuclear lamins. The pattern of phosphorylation varies through the cell cycle. Although histone H1 is phosphorylated during interphase its phosphorylation increases sharply during mitosis. Histone H3,
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IN VIVO ADP-RIBOSYLATION OF NUCLEAR PROTEINS [PDF]
128P
E. LEONE+4 more
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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+3 more
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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+3 more
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Nuclear proteins in spermatogenesis
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1986Mammalian somatic type histone variants are replaced or supplemented in early primary spermatocytes and possibly spermatogonia by testis specific and testis enriched histone variants. The testis complement of histones is replaced entirely by transition basic proteins in mid-spermatids.
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Nuclear envelope proteins and their role in nuclear positioning and replication
Biochemical Society Transactions, 2010Controlled movement of the nucleus is important in a wide variety of plant cellular events. Positioning involving intact nuclei occurs in cell division, development, tip growing systems such as the root hair and in response to stimuli, including light, touch and infection.
Katja Graumann+2 more
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Inner nuclear membrane proteins and the nuclear lamina
Journal of Cell Science, 2001The nuclear lamina is a scaffolding structure at the nuclear periphery and is required for maintenance of nuclear shape, spacing of nuclear pore complexes, organization of heterochromatin, DNA replication, and regulation of transcription factors.
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Extraction of Nuclear Proteins
2006The integrity of a subcellular proteome such as the nucleus, is largely dependent on purification of the isolated compartment away from other cellular contaminants. The separation of high-purity nuclei from plants is a difficult task. However, successful purification has been achieved through a series of fractionation processes.
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Characterization of a Sperm Nuclear Protein
American Journal of Reproductive Immunology, 1996PROBLEM: 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.
Malcho G. Petrov+3 more
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Studies of the nuclear residual proteins
Archives of Biochemistry and Biophysics, 1968Abstract The nuclear residual proteins of rat liver have been prepared by solubilization with sodium deoxycholate and Sephadex gel filtration. These proteins were examined by analytical ultracentrifugation, DEAE-cellulose chromatography, starch gel electrophoresis, amino acid composition, and alkali-labile phosphorus analysis.
V. Patel+7 more
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