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The nuclear pore complex [PDF]
, 1998 The nuclear pore complex is the largest supramolecular complex that assembles in the eukaryotic cell. This structure is highly dynamic and must disassemble prior to mitosis and reassemble after the event. The directed movement of macromolecules into and out of the nucleus occurs through the nuclear pore complex, a potentially regulatory point for ...
Natasha V. Raikhel, Antje Heese-Peck
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Nuclear pores and nuclear assembly
Current Opinion in Cell Biology, 2001Communication between the nucleus and cytoplasm occurs through large macromolecular structures, the nuclear pores. Quantitative scanning transmission electron microscopy has estimated the mass of a nuclear pore to be 60 million Daltons in yeast and 120 million Daltons in vertebrates.
Douglass J. Forbes, Sanjay K. Vasu
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Journal of Cell Science, 2000
All transport between the nucleus and the cytoplasm passes through the nuclear pore complex (NPC) (Functions). Small (20–40 kDa) molecules passively diffuse through the NPC, whereas there are a series of signal- and temperature-dependent mechanisms for large molecules.
Martin W. Goldberg +4 more
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All transport between the nucleus and the cytoplasm passes through the nuclear pore complex (NPC) (Functions). Small (20–40 kDa) molecules passively diffuse through the NPC, whereas there are a series of signal- and temperature-dependent mechanisms for large molecules.
Martin W. Goldberg +4 more
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Problems at the nuclear pore [PDF]
Nature, 2015 Expansion of a repetitive DNA sequence is associated with neurodegeneration. Three studies identify genes involved in nuclear import and export that can mediate the toxicity this expansion causes. See Article p.56 & Letter p.129 The most common ...
Randal S. Tibbetts, Bennett W. Fox
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Nuclear transport and nuclear pores in yeast
Antonie van Leeuwenhoek, 1992The central features of nuclear import have been conserved during evolution. In yeast the nuclear accumulation of proteins follows the same selective and active transport mechanisms known from higher eukaryotes. Yeast nuclear proteins contain nuclear localization sequences (NLS) which are presumably recognized by receptors in the cytoplasm and the ...
U. Nehrbass, E. C. Hurt
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Annual Review of Biochemistry, 1995
The nuclear pore complex (NPC) creates an aqueous channel across the nuclear envelope through which macromolecular transport between nucleus and cytoplasm occurs. Nucleocytoplasmic traffic is bidirectional and involves diverse substrates, including protein and RNA.
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The nuclear pore complex (NPC) creates an aqueous channel across the nuclear envelope through which macromolecular transport between nucleus and cytoplasm occurs. Nucleocytoplasmic traffic is bidirectional and involves diverse substrates, including protein and RNA.
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Nuclear pores in the apoptotic cell
The Histochemical Journal, 1994During apoptosis, nuclear pores undergo strong modifications, which are described here in five different apoptotic models. Conventional electron microscopy, supported by freeze-fracture analysis, showed a constant migration of nuclear pores towards the diffuse chromatin areas.
FALCIERI, ELISABETTA +5 more
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The nuclear pore: at the crossroads
The FASEB Journal, 1992The nuclear pore complex is at the crossroads of macromolecular traffic across the nuclear envelope. Our knowledge of the mechanism whereby nuclear transport is mediated by the nuclear pore complex is also at a crossroads; a molecular understanding of this process has major implications for applied medical sciences.
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Pores for thought: nuclear pore complex proteins
Trends in Cell Biology, 1994Nuclear pore complexes (NPCs) are enormous macromolecular structures that mediate the active exchange of proteins and RNPs between the nucleus and cytoplasm. Recent work has resulted in a windfall of identified NPC polypeptides, many with unique sequences.
Michael P. Rout, Susan R. Wente
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Science, 2011
The flexibility of an intrinsically disordered domain of a membrane protein allows it to pass through the nuclear pore.
Richard W. Kriwacki, Mi-Kyung Yoon
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The flexibility of an intrinsically disordered domain of a membrane protein allows it to pass through the nuclear pore.
Richard W. Kriwacki, Mi-Kyung Yoon
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