نتایج جستجو برای: pore

تعداد نتایج: 40268  

Journal: :Structure 2013
Parthasarathy Sampathkumar Seung Joong Kim Paula Upla William J Rice Jeremy Phillips Benjamin L Timney Ursula Pieper Jeffrey B Bonanno Javier Fernandez-Martinez Zhanna Hakhverdyan Natalia E Ketaren Tsutomu Matsui Thomas M Weiss David L Stokes J Michael Sauder Stephen K Burley Andrej Sali Michael P Rout Steven C Almo

The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup19...

Journal: :Journal of structural biology 2002
Birthe Fahrenkrog Bohumil Maco Ammon M Fager Joachim Köser Ursula Sauder Katharine S Ullman Ueli Aebi

Nup153, one of the best characterized nuclear pore complex proteins (nucleoporins), plays a critical role in the import of proteins into the nucleus as well as in the export of RNAs and proteins from the nucleus. Initially an epitope of Nup153 was found to reside at the distal ring of the NPC, whereas more recently another epitope was localized to the nuclear ring moiety of the NPC. In an effor...

Journal: :The Journal of Cell Biology 1989
C W Akey D S Goldfarb

The transport of macromolecules across the nuclear envelope is mediated by the nuclear pore complex (NPC). Using cryo-electron microscopy and image processing we have mapped the interaction of three specific gold probes with the NPC and obtained projection maps of two possible intermediates in nuclear import. The probes used in these experiments were (a) mAb-414, which cross-reacts with Xenopus...

Journal: :Cell 2003
Tobias C. Walther Annabelle Alves Helen Pickersgill Isabelle Loı̈odice Martin Hetzer Vincent Galy Bastian B. Hülsmann Thomas Köcher Matthias Wilm Terry Allen Iain W. Mattaj Valérie Doye

Nuclear pore complexes (NPCs) are large multiprotein assemblies that allow traffic between the cytoplasm and the nucleus. During mitosis in higher eukaryotes, the Nuclear Envelope (NE) breaks down and NPCs disassemble. How NPCs reassemble and incorporate into the NE upon mitotic exit is poorly understood. We demonstrate a function for the conserved Nup107-160 complex in this process. Partial in...

Journal: :EMBO reports 2000
M Suyama T Doerks I C Braun M Sattler E Izaurralde P Bork

Vertebrate TAP is a nuclear mRNA export factor homologous to yeast Mex67p. The middle domain of TAP binds directly to p15, a protein related to the nuclear transport factor 2 (NTF2), whereas its C-terminal domain interacts with various nucleoporins, the components of the nuclear pore complex (NPC). Here, we report that the middle domain of TAP is also similar to NTF2, as well as to regions in R...

Journal: :Cell reports 2014
Pau Pascual-Garcia Jieun Jeong Maya Capelson

The nuclear pore complex is a transport channel embedded in the nuclear envelope and made up of 30 different components termed nucleoporins (Nups). In addition to their classical role in transport, a subset of Nups has a conserved role in the regulation of transcription via direct binding to chromatin. The molecular details of this function remain obscure, and it is unknown how metazoan Nups ar...

Journal: :Molecular biology of the cell 2004
Eric R Griffis Branch Craige Christian Dimaano Katharine S Ullman Maureen A Powers

Despite the apparent overall structural stability of the nuclear pore complex during interphase, at least two nucleoporins have been shown to move dynamically on and off the pore. It is not yet certain what contribution nucleoporin mobility makes to the process of nuclear transport or how such mobility is regulated. Previously, we showed that Nup98 dynamically interacts with the NPC as well as ...

Journal: :Proteins 2012
Parthasarathy Sampathkumar Seung Joong Kim Danalyn Manglicmot Kevin T Bain Jeremiah Gilmore Tarun Gheyi Jeremy Phillips Ursula Pieper Javier Fernandez-Martinez Josef D Franke Tsutomu Matsui Hiro Tsuruta Shane Atwell Devon A Thompson J Spencer Emtage Stephen R Wasserman Michael P Rout Andrej Sali J Michael Sauder Steven C Almo Stephen K Burley

The nuclear pore complex (NPC), embedded in the nuclear envelope, is a large, dynamic molecular assembly that facilitates exchange of macromolecules between the nucleus and the cytoplasm. The yeast NPC is an eightfold symmetric annular structure composed of ~456 polypeptide chains contributed by ~30 distinct proteins termed nucleoporins. Nup116, identified only in fungi, plays a central role in...

Journal: :Nature Reviews Molecular Cell Biology 2001

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید