Results 301 to 310 of about 8,215,941 (358)
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Nuclear protein tyrosine kinases
Trends in Biochemical Sciences, 1994Protein 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 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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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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Nuclear export of proteins: The role of nuclear retention
Cell, 1993Proteins that shuttle between nucleus and cytoplasm are implicated in transport and signal transduction processes. Using assays based on interspecies heterokaryons and microinjection of Xenopus oocytes, we examined what structural features determine nuclear export of shuttling proteins.
Schmidt-Zachmann, M. S. +3 more
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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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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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Nuclear basic proteins in spermiogenesis
Biochimie, 1998In animal species, spermiogenesis, the late stage of spermatogenesis, is characterized by a dramatic remodelling of chromatin which involves morphological changes and various modifications in the nature of the nuclear basic proteins. According to the evolution of species, three situations can be observed: a) persistence of somatic histones or ...
D, Wouters-Tyrou +3 more
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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.
David A. Jans, Jade K. Forwood
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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.
David A. Jans, Jade K. Forwood
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Phosphorylated CREB binds specifically to the nuclear protein CBP
Nature, 1993J. Chrivia +5 more
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