Results 181 to 190 of about 14,867 (213)

Depletion of a Single Nucleoporin, Nup107, Prevents the Assembly of a Subset of Nucleoporins Into the Nuclear Pore Complex [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2003
The nuclear pore complex (NPC) is a protein assembly that contains several distinct subcomplexes. The mammalian nucleoporin (Nup)-107 is part of a hetero-oligomeric complex, that also contains Nup160, Nup133, Nup96, and the mammalian homolog of yeast Sec13p. We used transfection of HeLa cells with small interfering RNAs to specifically deplete mRNA for
Günter Blobel
exaly   +3 more sources

Nucleoporin Nup62 Maintains Centrosome Homeostasis [PDF]

Cell Cycle, 2013
Centrosomes are comprised of 2 orthogonally arranged centrioles surrounded by the pericentriolar material (PCM), which serves as the main microtubule organizing center of the animal cell. More importantly, centrosomes also control spindle polarity and orientation during mitosis.
Richard W Wong, Chieko Hashizume, Akiko Kobayashi   +2 more
exaly   +3 more sources

Some of the next articles are maybe not open access.

Related searches:

Nucleoporins and chromatin metabolism

Current Opinion in Cell Biology, 2016
Mounting 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, 1999
The 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, M R, Caracciolo, W K, Berlin, J A, Hanover   +3 more
openaire   +2 more sources

An Evaluation of Sialation of the Nucleoporin p62

Archives of Biochemistry and Biophysics, 1998
Many 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, 2011
A 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, Nelly, Panté, Andrew J, Mouland   +2 more
openaire   +2 more sources

From nucleoporins to nuclear pore complexes

Current Opinion in Cell Biology, 1997
One of the largest supramolecular assemblies in the eukaryotic cell, the nuclear pore complex, is now being dissected into its numerous molecular constituents. The combined use of biochemistry and genetics in yeast has made this rapid development possible.
V, Doye, E, Hurt
openaire   +2 more sources

Modeling the nucleoporins that form the hairy pores

Biochemical Society Transactions, 2020
Sitting on the nuclear envelope, nuclear pore complexes (NPCs) control the molecular transport between the nucleus and the cytoplasm. Without definite open or close states, the NPC uses a family of intrinsically disordered nucleoporins called FG-Nups to construct a selective permeability barrier whose functional structure is unclear.
Kai Huang, Igal Szleifer
openaire   +2 more sources

Across the nuclear pores with the help of nucleoporins

Chromosoma, 1991
Proteins targeted to specific intracellular organelles such as mitochondria or the endoplasmic reticulum are able to cross membranes. Yet, to enter or exit the nucleus, proteins and RNA must pass through nonmembranous "gates" of the nuclear envelope, the nuclear pore complexes.
M, Carmo-Fonseca, E C, Hurt
openaire   +2 more sources

Nucleoporins and nucleocytoplasmic transport in hematologic malignancies

Seminars in Cancer Biology, 2014
Hematologic malignancies are often associated with chromosomal rearrangements that lead to the expression of chimeric fusion proteins. Rearrangements of the genes encoding two nucleoporins, NUP98 and NUP214, have been implicated in the pathogenesis of several types of hematologic malignancies, particularly acute myeloid leukemia.
Akiko, Takeda, Nabeel R, Yaseen
openaire   +2 more sources