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Proteins Connecting the Nuclear Pore Complex with the Nuclear Interior [PDF]

Journal of Cell Biology, 1999
While much has been learned in recent years about the movement of soluble transport factors across the nuclear pore complex (NPC), comparatively little is known about intranuclear trafficking. We isolated the previously identified Saccharomyces protein Mlp1p (myosin-like protein) by an assay designed to find nuclear envelope (NE) associated proteins ...
Caterina Strambio-De-Castillia, G Blobel, Michael P Rout   +2 more
exaly   +3 more sources

The functional versatility of the nuclear pore complex proteins [PDF]

Seminars in Cell & Developmental Biology, 2017
Over the past few decades, it is increasingly evident that nucleoporins are multi-functional proteins that are not only pivotal for the formation of the nuclear pore complex. They also have key roles in mitosis, gene expression, development and disease. In this review, the versatility and functions of nucleoporins outside the NPC will be discussed.
Mohammed, Hezwani, Birthe, Fahrenkrog
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Function and assembly of nuclear pore complex proteins

Biochemistry and Cell Biology, 1999
Nuclear pore complexes (NPCs) are extremely elaborate structures that mediate the bidirectional movement of macromolecules between the nucleus and cytoplasm. The current view of NPC organization features a massive symmetrical framework that is embedded in the double membranes of the nuclear envelope. It embraces a central channel of as yet ill-defined
K, Bodoor, S, Shaikh, P, Enarson, S, Chowdhury, D, Salina, W H, Raharjo, B, Burke   +6 more
openaire   +3 more sources

The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins [PDF]

EMBO Journal, 2001
The nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC component that has been implicated in protein and RNP transport and in the interaction of NPCs with the nuclear lamina. Here, Nup153 is localized by immunogold
Maarten Fornerod, Terry D Allen, I W Mattaj   +2 more
exaly   +4 more sources

Pores for thought: nuclear pore complex proteins

Trends in Cell Biology, 1994
Nuclear 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.
M P, Rout, S R, Wente
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A new family of yeast nuclear pore complex proteins. [PDF]

Journal of Cell Biology, 1992
We have identified a novel family of yeast nuclear pore complex proteins. Three individual members of this family, NUP49, NUP100, and NUP116, have been isolated and then characterized by a combination of molecular genetics and immunolocalization. Employing immunoelectron and immunofluorescence microscopy on yeast cells, we found that the binding of a ...
Susan R Wente, Michael P Rout, G Blobel
exaly   +3 more sources

Identification and characterization of a nuclear pore complex protein

Cell, 1986
We describe studies using a monoclonal antibody that recognizes a 62 kd protein (p62) of rat liver nuclei. This protein remains associated with the nuclear pore complex-lamina fraction resulting from treatment of nuclei with DNAase, RNAase, and nonionic detergent. Immunofluorescence revealed a strikingly punctate pattern of nuclear rim staining.
L I, Davis, G, Blobel
openaire   +2 more sources