نتایج جستجو برای: pore system

تعداد نتایج: 2266274  

Journal: :Genes to cells : devoted to molecular & cellular mechanisms 2010
Haruki Iino Kazuhiro Maeshima Reiko Nakatomi Shingo Kose Tsutomu Hashikawa Taro Tachibana Naoko Imamoto

Nuclear pore complexes (NPCs) are 'supramolecular complexes' on the nuclear envelope assembled from multiple copies of approximately 30 different proteins called nucleoporins (Nups) that provide aqueous channels for nucleocytoplasmic transport during interphase. Although the structural aspects of NPCs have been characterized in detail, NPC formation and its regulation, especially during interph...

Journal: :Journal of cell science 2015
Greg Kabachinski Thomas U Schwartz

Nuclear pore complexes (NPCs) are indispensable for cell function and are at the center of several human diseases. NPCs provide access to the nucleus and regulate the transport of proteins and RNA across the nuclear envelope. They are aqueous channels generated from a complex network of evolutionarily conserved proteins known as nucleporins. In this Cell Science at a Glance article and the acco...

2013
Laura Occhipinti Yiming Chang Martin Altvater Anna M. Menet Stefan Kemmler Vikram G. Panse

Multiple export receptors passage bound pre-ribosomes through nuclear pore complexes (NPCs) by transiently interacting with the Phe-Gly (FG) meshwork of their transport channels. Here, we reveal how the non-FG interacting yeast mRNA export factor Gly-Leu-FG lethal 2 (Gle2) functions in the export of the large pre-ribosomal subunit (pre-60S). Structure-guided studies uncovered conserved platform...

2013
Mohammad Azimi Mohammad R. K. Mofrad

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 presence of such a gradient. Nonetheless, the existence of an affinity gradient has remained an uncharacterized contributing factor. To shed l...

Journal: :Cell 2010
Chunhui Hou Victor G. Corces

Although components of the nuclear pore complex have been implicated in gene regulation independent of their role at the nuclear envelope, the evidence so far has been indirect. Capelson et al. (2010) and Kalverda et al. (2010) now reveal that certain nucleoporins are actively involved in transcription inside the nucleoplasm of Drosophila cells.

Journal: :Current opinion in cell biology 2012
David Grünwald Robert H Singer

The nuclear pore complex (NPC) has long been viewed as a point-like entry and exit channel between the nucleus and the cytoplasm. New data support a different view whereby the complex displays distinct spatial dynamics of variable duration ranging from milliseconds to events spanning the entire cell cycle. Discrete interaction sites outside the central channel become apparent, and transport reg...

Journal: :Molecular biology of the cell 2004
Sandra Krull Johan Thyberg Birgitta Björkroth Hans-Richard Rackwitz Volker C Cordes

The vertebrate nuclear pore complex (NPC) is a macromolecular assembly of protein subcomplexes forming a structure of eightfold radial symmetry. The NPC core consists of globular subunits sandwiched between two coaxial ring-like structures of which the ring facing the nuclear interior is capped by a fibrous structure called the nuclear basket. By postembedding immunoelectron microscopy, we have...

Journal: :Cell 1995
Aurelian Radu Mary Shannon Moore Günter Blobel

We report the cDNA deduced primary structure of a wheat germ agglutinin-reactive nuclear pore complex (NPC) protein of rat. The protein, termed Nup98 (for nucleoporin of 98 kDa), contains numerous GLFG and FG repeats and some FXFG repeats and is thus a vertebrate member of a family of GLFG nucleoporins that were previously discovered in yeast. Immunoelectron microscopy showed Nup98 to be asymme...

Journal: :Journal of cell science 1995
M Grote U Kubitscheck R Reichelt R Peters

Ultrathin sections of Lowicryl K4M embedded cultured 3T3 cells, human keratinocytes and mouse/rat liver tissue were incubated with polyspecific primary antibodies against p62 and other nucleoporins followed by 10 nm gold labeled secondary antibodies. By quantitatively evaluating both cross sections and tangential sections of the NPC, we found that irrespective of the cell type antibodies predom...

Journal: :The Journal of Cell Biology 2001
David J. Dilworth Adisetyantari Suprapto Julio C. Padovan Brian T. Chait Richard W. Wozniak Michael P. Rout John D. Aitchison

Nucleocytoplasmic transport is mediated by the interplay between soluble transport factors and nucleoporins resident within the nuclear pore complex (NPC). Understanding this process demands knowledge of components of both the soluble and stationary phases and the interface between them. Here, we provide evidence that Nup2p, previously considered to be a typical yeast nucleoporin that binds imp...

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