Results 181 to 190 of about 6,849 (214)
Identification of New FG-Repeat Nucleoporins With Amyloid Properties
Amyloids are fibrillar protein aggregates with a cross-β structure. More than two hundred different proteins with amyloid or amyloid-like properties are already known.
Xenia V Sukhanova +2 more
exaly +2 more sources
Interaction of Nucleoporins With Nuclear Transport Receptors: A Structural Perspective
Soluble nuclear transport receptors and stationary nucleoporins are at the heart of the nucleocytoplasmic transport machinery. A subset of nucleoporins contains characteristic and repetitive FG (phenylalanine-glycine) motifs, which are the basis for the ...
Ralf Ficner +2 more
exaly +2 more sources
Interaction Between NTF2 and xFxFG-Containing Nucleoporins Is Required to Mediate Nuclear Import of RanGDP [PDF]
Nuclear transport factor 2 (NTF2) is a small, homodimeric protein that binds to both RanGDP and xFxFG repeat-containing nucleoporins, such as yeast Nsp1p and vertebrate p62.
Murray Stewart +2 more
exaly +2 more sources
The death of yeast treated with hydrogen peroxide (H2O2) shares a number of morphological and biochemical features with mammalian apoptosis. In this study, we report that the permeability of yeast nuclear envelopes (NE) increased during H2O2-induced cell
David S Goldfarb, Michael F Rexach
exaly +2 more sources
The Part and the Whole: Functions of Nucleoporins in Nucleocytoplasmic Transport
The nuclear pore complex (NPC) functions as a selective gate that allows passage of certain molecules into and out of the nucleus and restricts that of others.
Sarah Wälde, Ralph H Kehlenbach
exaly +2 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Nucleoporins and chromatin metabolism
Current Opinion in Cell Biology, 2016Mounting evidence has implicated a group of proteins termed nucleoporins, or Nups, in various processes that regulate chromatin structure and function. Nups were first recognized as building blocks for nuclear pore complexes, but several members of this group of proteins also reside in the cytoplasm and within the nucleus.
Christopher, Ptak, Richard W, Wozniak
openaire +2 more sources
Phosphorylation and Glycosylation of Nucleoporins
Archives of Biochemistry and Biophysics, 1999The nuclear pore complex mediates macromolecular transport between the nucleus and cytoplasm. Many nuclear pore components (nucleoporins) are modified by both phosphate and O-linked N-acetylglucosamine (O-GlcNAc). Among its many functions, protein phosphorylation plays essential roles in cell cycle progression. The role of O-GlcNAc addition is unknown.
M W, Miller +3 more
openaire +2 more sources
An Evaluation of Sialation of the Nucleoporin p62
Archives of Biochemistry and Biophysics, 1998Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine. These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm. The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex ...
B, Fang, J A, Hanover, M W, Miller
openaire +2 more sources
Examining the Requirements for Nucleoporins by HIV-1
Future Microbiology, 2011A hallmark of HIV type 1 and other lentiviruses is their ability to infect and replicate in nondividing cells by commandeering host nuclear transport factors. During the early stages of infection, this is expected to permit the safe passage of viral preintegration complexes (PICs) through nuclear pores.
Anne, Monette +2 more
openaire +2 more sources

