Results 201 to 210 of about 8,158 (226)
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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.
William K. Berlin +3 more
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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 ...
Bin Fang +2 more
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Modeling the nucleoporins that form the hairy pores
Biochemical Society Transactions, 2020Sitting 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, 1991Proteins 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.
Maria Carmo-Fonseca, Eduard C. Hurt
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From nucleoporins to nuclear pore complexes
Current Opinion in Cell Biology, 1997One 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.
Ed Hurt, Valérie Doye
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Nucleoporins and nucleocytoplasmic transport in hematologic malignancies
Seminars in Cancer Biology, 2014Hematologic 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.
Nabeel R. Yaseen, Akiko Takeda
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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 +3 more
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Roles of the Nucleoporin Tpr in Cancer and Aging
2014Tpr 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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