Higher nucleoporin-Importinβ affinity at the nuclear basket increases nucleocytoplasmic import. [PDF]
, 2013 Several in vitro studies have shown the presence of an affinity gradient in nuclear pore complex proteins for the import receptor Importinβ, at least partially contributing to nucleocytoplasmic transport, while others have historically argued against the
Azimi, Mohammad, Mofrad, Mohammad
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Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore [PDF]
, 2004 Resident integral proteins of the inner nuclear membrane (INM) are synthesized as membrane-integrated proteins on the peripheral endoplasmic reticulum (ER) and are transported to the INM throughout interphase using an unknown trafficking mechanism.
Gerace, Larry +3 more
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Three-dimensional structure and flexibility of a membrane-coating module of the nuclear pore complex. [PDF]
, 2009 The nuclear pore complex mediates nucleocytoplasmic transport in all eukaryotes and is among the largest cellular assemblies of proteins, collectively known as nucleoporins. Nucleoporins are organized into distinct subcomplexes.
Blobel, Günter, Kampmann, Martin
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Components of Coated Vesicles and Nuclear Pore Complexes Share a Common Molecular Architecture [PDF]
, 2004 Numerous features distinguish prokaryotes from eukaryotes, chief among which are the distinctive internal membrane systems of eukaryotic cells. These membrane systems form elaborate compartments and vesicular trafficking pathways, and sequester the ...
Amos +67 more
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The NAE Pathway : autobahn to the nucleus for cell surface receptors [PDF]
, 2019 Various growth factors and full-length cell surface receptors such as EGFR are translocated from the cell surface to the nucleoplasm, baffling cell biologists to the mechanisms and functions of this process. Elevated levels of nuclear EGFR correlate with
Bard, Frederic A. +3 more
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Simple biophysics underpins collective conformations of the intrinsically disordered proteins of the Nuclear Pore Complex [PDF]
, 2016 Nuclear Pore Complexes (NPCs) are key cellular transporter that control nucleocytoplasmic transport in eukaryotic cells, but its transport mechanism is still not understood.
Coalson, Rob D. +7 more
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Ciliary and Nuclear Transport: Different Places, Similar Routes? [PDF]
, 2012 Cilia and flagella are membrane-sheathed, microtubule-based protrusions that decorate the surface of many eukaryotic cells. At their base, they form a selective barrier that concentrates certain proteins within the cilia but excludes others.
Obado, Samson O., Rout, Michael P.
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The hrp23 Protein in the Balbiani Ring Pre-mRNP Particles Is Released Just before or at the Binding of the Particles to the Nuclear Pore Complex [PDF]
, 1998 Balbiani ring (BR) pre-mRNP particles reside in the nuclei of salivary glands of the dipteran Chironomus tentans and carry the message for giant-sized salivary proteins.
Alzhanova-Ericsson +79 more
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The Structure Inventory of the Nuclear Pore Complex [PDF]
, 2018 The nuclear pore complex (NPC) is the principal gateway for molecular exchange between nucleus and cytoplasm across the nuclear envelope. Due to its sheer size of estimated 50-112 MDa and its complex buildup from about 500-1000 individual proteins, it is
Schwartz, Thomas
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Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex. [PDF]
, 2015 The nuclear pore complex (NPC) is the portal for bidirectional transportation of cargos between the nucleus and the cytoplasm. While most of the structural elements of the NPC, i.e.
Lee, BL +3 more
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