Results 211 to 220 of about 1,109,521 (262)
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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 ...
Marc, Damelin +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 ...
Marc, Damelin +2 more
openaire +2 more sources
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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Phosphorylation of nuclear proteins
Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1983Abstract Many 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
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NuMA, a nuclear protein involved in mitosis and nuclear reformation
Current Opinion in Cell Biology, 1994NuMA, a nuclear protein that associates with the mitotic apparatus, was identified in 1980 as a high molecular weight component of the nuclear matrix with the unusual property of associating with the microtubules of the spindle apparatus during mitosis.
D A, Compton, D W, Cleveland
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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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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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Protein synthesis in nuclear residual protein
Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 19651. 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 ...
G, PATEL, T Y, WANG
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Mechanisms of nuclear protein import
Current Opinion in Cell Biology, 1995The past two years have seen a significant increase in our understanding of nuclear protein import. Five cytosolic import factors have been identified, two of which have been shown to directly interact with components of the nuclear pore complex. These findings enable refinement of previous models for steps in the nuclear import pathway, and provide a ...
F, Melchior, L, Gerace
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gCap39 is a nuclear and cytoplasmic protein
Cell Motility, 1993AbstractgCap39 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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