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Del Priore V., Heath C., Snay C., MacMillan A., Gorsch L., Dagher S., and Cole C. A structure/function analysis of Rat7p/Nup159p, an essential nucleoporin of Saccharomyces cerevisiae. J Cell Sci 110 (1997) 2987-2999
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Del Priore, V.1
Heath, C.2
Snay, C.3
MacMillan, A.4
Gorsch, L.5
Dagher, S.6
Cole, C.7
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42
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0034695924
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The yeast nuclear pore complex: composition, architecture, and transport mechanism
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Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., and Chait B.T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148 (2000) 635-651
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Rout, M.P.1
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Hjertaas, K.4
Zhao, Y.5
Chait, B.T.6
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43
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9744266768
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The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore
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The authors show that the N-terminal region of Nup159, to which Dbp5 binds, is a seven-bladed β propeller, a structure also found in the metazoan ortholog, NUP214. They demonstrate that Dbp5 binds to blades 5-7. Point mutations that render this association temperature-sensitive result in reduced growth and a block to mRNA export, consistent with earlier findings with a Nup159 mutant lacking its N-terminal third.
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Weirich C.S., Erzberger J.P., Berger J.M., and Weis K. The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Mol Cell 16 (2004) 749-760. The authors show that the N-terminal region of Nup159, to which Dbp5 binds, is a seven-bladed β propeller, a structure also found in the metazoan ortholog, NUP214. They demonstrate that Dbp5 binds to blades 5-7. Point mutations that render this association temperature-sensitive result in reduced growth and a block to mRNA export, consistent with earlier findings with a Nup159 mutant lacking its N-terminal third.
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(2004)
Mol Cell
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Weirich, C.S.1
Erzberger, J.P.2
Berger, J.M.3
Weis, K.4
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44
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0029047324
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A conditional allele of the novel repeat-containing yeast nucleoporin Rat7/Nup159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes
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Gorsch L.C., Dockendorff T.C., and Cole C.N. A conditional allele of the novel repeat-containing yeast nucleoporin Rat7/Nup159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J Cell Biol 129 (1995) 939-955
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Gorsch, L.C.1
Dockendorff, T.C.2
Cole, C.N.3
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45
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0029816713
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The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the Rat7/Nup159 nucleoporin, is required for efficient mRNA export
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Del Priore V., Snay C.A., Bahr A., and Cole C.N. The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7-1 temperature-sensitive allele of the Rat7/Nup159 nucleoporin, is required for efficient mRNA export. Mol Biol Cell 7 (1996) 1601-1621
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Del Priore, V.1
Snay, C.A.2
Bahr, A.3
Cole, C.N.4
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46
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0029745374
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An RNA-export mediator with an essential nuclear export signal
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Murphy R., and Wente S.R. An RNA-export mediator with an essential nuclear export signal. Nature 383 (1996) 357-360
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Nature
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Murphy, R.1
Wente, S.R.2
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Modularity within the architecture of the nuclear pore complex
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Schwartz T.U. Modularity within the architecture of the nuclear pore complex. Curr Opin Struct Biol 15 (2005) 221-226
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Curr Opin Struct Biol
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Schwartz, T.U.1
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48
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0033569797
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The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p
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Strahm Y., Fahrenkrog B., Zenklusen D., Rychner E., Kantor J., Rosbach M., and Stutz F. The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J 18 (1999) 5761-5777
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EMBO J
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Strahm, Y.1
Fahrenkrog, B.2
Zenklusen, D.3
Rychner, E.4
Kantor, J.5
Rosbach, M.6
Stutz, F.7
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49
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9844219734
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Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p
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Saavedra C.A., Hammell C.M., Heath C.V., and Cole C.N. Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p. Genes Dev 11 (1997) 2845-2856
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Genes Dev
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Saavedra, C.A.1
Hammell, C.M.2
Heath, C.V.3
Cole, C.N.4
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50
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2442694192
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The nuclear pore complex and the DEAD box protein Rat8p/Dbp5p have nonessential features which appear to facilitate mRNA export following heat shock
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This paper defines a role for Nup42 during cellular heat stress. In cells lacking Nup42, both the DEAD-box helicase Dbp5 and the nuclear-pore-associated protein Gle1 show dramatically reduced binding to NPCs following heat shock.
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Rollenhagen C., Hodge C.A., and Cole C.N. The nuclear pore complex and the DEAD box protein Rat8p/Dbp5p have nonessential features which appear to facilitate mRNA export following heat shock. Mol Cell Biol 24 (2004) 4869-4879. This paper defines a role for Nup42 during cellular heat stress. In cells lacking Nup42, both the DEAD-box helicase Dbp5 and the nuclear-pore-associated protein Gle1 show dramatically reduced binding to NPCs following heat shock.
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(2004)
Mol Cell Biol
, vol.24
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Rollenhagen, C.1
Hodge, C.A.2
Cole, C.N.3
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52
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10944261830
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Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway
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Miller A.L., Suntharalingam M., Johnson S.L., Audhya A., Emr S.D., and Wente S.R. Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway. J Biol Chem 279 (2004) 51022-51032
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Miller, A.L.1
Suntharalingam, M.2
Johnson, S.L.3
Audhya, A.4
Emr, S.D.5
Wente, S.R.6
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53
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0033516604
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A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export
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York J.D., Odom A.R., Murphy R., Ives E.B., and Wente S.R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285 (1999) 96-100
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York, J.D.1
Odom, A.R.2
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Ives, E.B.4
Wente, S.R.5
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54
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27944474017
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The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim
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This paper presents evidence that at least one function of DEAD-box helicase Dbp5 in vivo is the removal of the mRNA export receptor Mex67 from the mRNP following its translocation through the nuclear pore.
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Lund M.K., and Guthrie C. The DEAD-box protein Dbp5p is required to dissociate Mex67p from exported mRNPs at the nuclear rim. Mol Cell 20 (2005) 645-651. This paper presents evidence that at least one function of DEAD-box helicase Dbp5 in vivo is the removal of the mRNA export receptor Mex67 from the mRNP following its translocation through the nuclear pore.
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(2005)
Mol Cell
, vol.20
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Lund, M.K.1
Guthrie, C.2
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55
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0036500482
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The mRNA export factor Dbp5 is associated with Balbiani ring mRNP from gene to cytoplasm
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Zhao J., Jin S.B., Bjorkroth B., Wieslander L., and Daneholt B. The mRNA export factor Dbp5 is associated with Balbiani ring mRNP from gene to cytoplasm. EMBO J 21 (2002) 1177-1187
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Zhao, J.1
Jin, S.B.2
Bjorkroth, B.3
Wieslander, L.4
Daneholt, B.5
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56
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0037884974
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An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components
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Estruch F., and Cole C.N. An early function during transcription for the yeast mRNA export factor Dbp5p/Rat8p suggested by its genetic and physical interactions with transcription factor IIH components. Mol Biol Cell 14 (2003) 1664-1676
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Mol Biol Cell
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Estruch, F.1
Cole, C.N.2
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57
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0034719392
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The DExH protein NPH-II is a processive and directional motor for unwinding RNA
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Jankowsky E., Gross C.H., Shuman S., and Pyle A.M. The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403 (2000) 447-451
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Nature
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Jankowsky, E.1
Gross, C.H.2
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Pyle, A.M.4
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