Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Andrei S. Zolotukhin"'
Autor:
Andrei S. Zolotukhin, Jenifer Bear, Michelle Mitchell, Guy R. Pilkington, Stuart F. J. Le Grice, George N. Pavlakis, Barbara K. Felber, Katarzyna J. Purzycka, Michal Legiewicz, Hiroaki Uranishi
Publikováno v:
Journal of Biological Chemistry. 285:42097-42104
Retrovirus replication requires specialized transport mechanisms to export genomic mRNA from the nucleus to the cytoplasm of the infected cell. This regulation is mediated by a combination of viral and/or cellular factors that interact with cis-actin
Autor:
Barbara K. Felber, Andrei S. Zolotukhin, Hiroaki Uranishi, George N. Pavlakis, Jenifer Bear, Susan Lindtner
Publikováno v:
Nucleic Acids Research
The conserved mRNA export receptor NXF1 (Mex67 in yeast) assembles with messenger ribonucleoproteins (mRNP) in the nucleus and guides them through the nuclear pore complex into the cytoplasm. The DEAD family RNA helicase Dbp5 is essential for nuclear
Autor:
Barbara K. Felber, Viraj Kulkarni, Cristina Bergamaschi, George N. Pavlakis, Gen-Mu Zhang, Andrei S. Zolotukhin, Candido Alicea, Rashmi Jalah, Margherita Rosati
Publikováno v:
J Immunol
The two known isoforms of IL-15 contain either a long signal peptide (LSP) or a short signal peptide (SSP), and are produced by alternatively spliced transcripts. It has been proposed that SSP IL-15 remains exclusively intracellular, and its function
Autor:
Barbara K. Felber, Susan Lindtner, Gen Mu Zhang, Jenifer Bear, Andrei S. Zolotukhin, Hiroaki Uranishi, Søren Warming, George N. Pavlakis, Neal G. Copeland, Nancy A. Jenkins
Publikováno v:
The Journal of Biological Chemistry
The human SPEN family proteins SHARP, RBM15/OTT1, and RBM15B/OTT3 share the structural domain architecture but show distinct functional properties. Here, we examined the function of OTT3 and compared it with its paralogues RBM15 and SHARP. We found t
Autor:
Andrei S. Zolotukhin, Martina Samiotaki, Hiroaki Uranishi, Jenifer Bear, George Panayotou, George N. Pavlakis, Viraj Kulkarni, Sergey Smulevitch, Barbara K. Felber, Susan Lindtner
Publikováno v:
Journal of Biological Chemistry. 281:36915-36928
Retroviruses/retroelements provide tools enabling the identification and dissection of basic steps for post-transcriptional regulation of cellular mRNAs. The RNA transport element (RTE) identified in mouse retrotransposons is functionally equivalent
Autor:
Andrei S. Zolotukhin, Wei Tan, Jenifer Bear, Barbara K. Felber, Sergey Smulevitch, Susan Lindtner, Irina Tretyakova
Publikováno v:
Nucleic Acids Research
TAP/hNXF1 is a key factor that mediates general cellular mRNA export from the nucleus, and its orthologs are structurally and functionally conserved from yeast to humans. Metazoans encode additional proteins that share homology and domain organizatio
Autor:
James G. Patton, Ivan N. Shatsky, Andrei S. Zolotukhin, Rui Peng, Daniel Michalowski, Barbara K. Felber, Sergey Smulevitch, Jenifer Bear, Abdulmaged M. Traish
Publikováno v:
Molecular and Cellular Biology. 23:6618-6630
Human immunodeficiency virus type 1 (HIV) gag/pol and env mRNAs contain cis-acting regulatory elements (INS) that impair stability, nucleocytoplasmic transport, and translation by unknown mechanisms. This downregulation can be counteracted by the vir
Publikováno v:
RNA. 6:1762-1772
Human TAP and Saccharomyces cerevisiae Mex67p belong to a family of proteins that mediate mRNA export. Computer searches identified previously two Caenorhabditis elegans genes, C15H11.3 and C115H11.6, that encode putative homologs of hTAP and Mex67p
Autor:
Jenifer Bear, Carlos Tabernero, Wei Tan, Barbara K. Felber, Andrei S. Zolotukhin, Eric A. Hudson
Publikováno v:
Molecular and Cellular Biology. 19:6306-6317
The nuclear export of the unspliced type D retrovirus mRNA depends on the cis-acting constitutive transport RNA element (CTE) that has been shown to interact with the human TAP (hTAP) protein promoting the export of the CTE-containing mRNAs. We repor
Publikováno v:
Journal of Biological Chemistry. 272:11356-11360
We identified a region in the human Ran GTPase-binding protein RanBP1 that shares similarities to the nuclear export signal of the inhibitor of the cAMP-dependent protein kinase. Mutational analysis confirmed that this region is responsible for the c