Results 191 to 200 of about 6,360 (219)
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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
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Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex

open access: yesCell, 2007
SummaryNuclear pore complexes (NPCs) form aqueous conduits in the nuclear envelope and gate the diffusion of large proteins between the cytoplasm and nucleoplasm.
Brian J Belmont
exaly   +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
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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
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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
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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
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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   +2 more
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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

Roles of the Nucleoporin Tpr in Cancer and Aging

2014
Tpr is a prominent architectural component of the nuclear pore complex that forms the basket-like structure on the nucleoplasmic side of the pore. Tpr, which stands for translocated promoter region, was originally described in the context of oncogenic fusions with the receptor tyrosine kinases Met, TRK, and Raf.
Chelsi J, Snow, Bryce M, Paschal
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Nucleoporin

2008
Sai-Juan Chen   +3 more
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