Results 41 to 50 of about 191,852 (331)

Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import [PDF]

FEBS Letters, 2001
The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin‐β family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between ...
Stewart, M, Baker, RP, Bayliss, R, Clayton, L, Grant, RP, Littlewood, T, Matsuura, Y   +6 more
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Intranuclear filaments containing a nuclear pore complex protein. [PDF]

The Journal of cell biology, 1993
Nuclear pore complexes (NPCs) are anchoring sites of intranuclear filaments of 3-6 nm diameter that are coaxially arranged on the perimeter of a cylinder and project into the nuclear interior for lengths varying in different kinds of cells. Using a specific monoclonal antibody we have found that a polypeptide of approximately 190 kD on SDS-PAGE, which ...
V C, Cordes, S, Reidenbach, A, Köhler, N, Stuurman, R, van Driel, W W, Franke   +5 more
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Vaults. III. Vault ribonucleoprotein particles open into flower-like structures with octagonal symmetry. [PDF]

, 1991
The structure of rat liver vault ribonucleoprotein particles was examined using several different staining techniques in conjunction with EM and digestion with hydrolytic enzymes.
Chugani, DC, Heuser, JE, Kedersha, NL, Rome, LH   +3 more
core   +2 more sources

Silencing nuclear pore protein Tpr elicits a senescent-like phenotype in cancer cells.

PLoS ONE, 2011
BackgroundTpr is a large coiled-coil protein located in the nuclear basket of the nuclear pore complex for which many different functions were proposed from yeast to human.Methodology/principal findingsHere we show that depletion of Tpr by RNA ...
Brigitte David-Watine
doaj   +1 more source

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
core   +1 more source

The subnuclear localization of tRNA ligase in yeast [PDF]

, 1987
Yeast tRNA ligase is an enzyme required for tRNA splicing. A study by indirect immune fluorescence shows that this enzyme is localized in the cell nucleus. At higher resolution, studies using indirect immune electron microscopy show this nuclear location
Abelson, John, Clark, Michael W.
core   +1 more source

Assembly of nuclear pore complexes mediated by major vault protein [PDF]

Journal of Cell Science, 2009
During interphase growth of eukaryotic cells, nuclear pore complexes (NPCs) are continuously incorporated into the intact nuclear envelope (NE) by mechanisms that are largely unknown. De novo formation of NPCs involves local fusion events between the inner and outer nuclear membrane, formation of a transcisternal membranous channel of defined diameter ...
Friederike, Vollmar, Christian, Hacker, René-Peiman, Zahedi, Albert, Sickmann, Andrea, Ewald, Ulrich, Scheer, Marie-Christine, Dabauvalle   +6 more
openaire   +2 more sources

Deciphering Networks of Protein Interactions at the Nuclear Pore Complex [PDF]

Molecular & Cellular Proteomics, 2002
The nuclear pore complex (NPC) gates the only known conduit for molecular exchange between the nucleus and cytoplasm of eukaryotic cells. Macromolecular transport across the NPC is mediated by nucleocytoplasmic shuttling receptors termed karyopherins (Kaps).
Nadia P C, Allen, Samir S, Patel, Lan, Huang, Robert J, Chalkley, Al, Burlingame, Malik, Lutzmann, Eduard C, Hurt, Michael, Rexach   +7 more
openaire   +2 more sources

The HSV1 Tail-Anchored Membrane Protein pUL34 Contains a Basic Motif That Supports Active Transport to the Inner Nuclear Membrane Prior to Formation of the Nuclear Egress Complex

Viruses, 2021
Herpes simplex virus type 1 nucleocapsids are released from the host nucleus by a budding process through the nuclear envelope called nuclear egress. Two viral proteins, the integral membrane proteins pUL34 and pUL31, form the nuclear egress complex at ...
Christina Funk, Débora Marques da Silveira e Santos, Melanie Ott, Verena Raschbichler, Susanne M. Bailer   +4 more
doaj   +1 more source

Differential Mitotic Phosphorylation of Proteins of the Nuclear Pore Complex [PDF]

Journal of Biological Chemistry, 1995
During each cell cycle, the nucleus of higher eukaryotes undergoes a dramatic assembly and disassembly. These events can be faithfully reproduced in vitro using cell-free extracts derived from Xenopus eggs. Such extracts contain three major N-acetylglucosaminylated proteins, p200, p97, and p60.
C, Macaulay, E, Meier, D J, Forbes
openaire   +2 more sources