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A unified theory of gene expression
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Orphanides G., Reinberg D. A unified theory of gene expression. Cell. 108:2002;439-451.
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Cell
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Orphanides, G.1
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0036591882
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The mRNA assembly line: Transcription and processing machines in the same factory
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Bentley D. The mRNA assembly line: transcription and processing machines in the same factory. Curr. Opin. Cell Biol. 14:2002;336-342.
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Bentley, D.1
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0037154964
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A conserved mRNA export machinery coupled to pre-mRNA splicing
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Reed R., Hurt E. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell. 108:2002;523-531.
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Cell
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Reed, R.1
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0037041395
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An extensive network of coupling among gene expression machines
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Maniatis T., Reed R. An extensive network of coupling among gene expression machines. Nature. 416:2002;499-506.
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Nature
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Maniatis, T.1
Reed, R.2
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0037154967
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Integrating mRNA processing with transcription
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Proudfoot N.J., Furger A., Dye M.J. Integrating mRNA processing with transcription. Cell. 108:2002;501-512.
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Cell
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Proudfoot, N.J.1
Furger, A.2
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0036196670
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Protein and RNA export from the nucleus
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Lei E.P., Silver P.A. Protein and RNA export from the nucleus. Dev. Cell. 2:2002;261-272.
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Dev. Cell
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Lei, E.P.1
Silver, P.A.2
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0037222090
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Co-transcriptional monitoring of mRNP formation
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Jensen T.H., Rosbash M. Co-transcriptional monitoring of mRNP formation. Nat. Struct. Biol. 10:2003;10-12.
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Nat. Struct. Biol.
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Jensen, T.H.1
Rosbash, M.2
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8
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0036861279
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A novel family of nuclear transport receptors mediates the export of messenger RNA to the cytoplasm
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Izaurralde E. A novel family of nuclear transport receptors mediates the export of messenger RNA to the cytoplasm. Eur. J. Cell. Biol. 81:2002;577-584.
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Eur. J. Cell. Biol.
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Izaurralde, E.1
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10
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0036826885
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5′ exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly
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The authors explored formation of the EJC. The data show that a set of proteins contacts the exon during splicing and that extensive remodeling then occurs in this region as the exon junction is formed.
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Reichert V.L., Le Hir H., Jurica M.S., Moore M.J. 5′ exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly. Genes. Dev. 16:2002;2778-2791 The authors explored formation of the EJC. The data show that a set of proteins contacts the exon during splicing and that extensive remodeling then occurs in this region as the exon junction is formed.
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Genes. Dev.
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Reichert, V.L.1
Le Hir, H.2
Jurica, M.S.3
Moore, M.J.4
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11
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0036645697
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The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
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Lejeune F., Ishigaki Y., Li X., Maquat L.E. The exon junction complex is detected on CBP80-bound but not eIF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling. EMBO J. 21:2002;3536-3545.
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EMBO J.
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Lejeune, F.1
Ishigaki, Y.2
Li, X.3
Maquat, L.E.4
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12
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0036829415
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Intron status and 3′-end formation control cotranscriptional export of mRNA
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Lei E.P., Silver P.A. Intron status and 3′-end formation control cotranscriptional export of mRNA. Genes Dev. 16:2002;2761-2766.
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Genes Dev.
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Lei, E.P.1
Silver, P.A.2
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14
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0037175374
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REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export
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Gatfield D., Izaurralde E. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J. Cell Biol. 159:2002;579-588.
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J. Cell Biol.
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Gatfield, D.1
Izaurralde, E.2
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15
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0037118052
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TREX is a conserved complex coupling transcription with messenger RNA export
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A new complex containing mRNA export factors and transcription factors is identified in yeast and mammals. The complex may function in the co-transcriptional loading of mRNA export factors.
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Strasser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.et al. TREX is a conserved complex coupling transcription with messenger RNA export. Nature. 417:2002;304-308 A new complex containing mRNA export factors and transcription factors is identified in yeast and mammals. The complex may function in the co-transcriptional loading of mRNA export factors.
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Nature
, vol.417
, pp. 304-308
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Strasser, K.1
Masuda, S.2
Mason, P.3
Pfannstiel, J.4
Oppizzi, M.5
Rodriguez-Navarro, S.6
Rondon, A.G.7
Aguilera, A.8
Struhl, K.9
Reed, R.10
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16
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0036645687
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The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability
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Jimeno S., Rondon A.G., Luna R., Aguilera A. The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J. 21:2002;3526-3535.
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EMBO J.
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Jimeno, S.1
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Aguilera, A.4
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0036469913
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The connection between transcription and genomic instability
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Aguilera A. The connection between transcription and genomic instability. EMBO J. 21:2002;195-201.
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EMBO J.
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Aguilera, A.1
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18
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0036889334
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Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p
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This study shows that the THO/TREX complex component Hpr1 interacts with the mRNA export factor Sub2 and plays a role in recruiting Sub2 to the mRNA during transcription. The study also shows links between the TREX complex and the nuclear exosome, suggesting that proper mRNP formation is co-transcriptionally monitored
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Zenklusen D., Vinciguerra P., Wyss J.C., Stutz F. Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p. Mol. Cell Biol. 22:2002;8241-8253 This study shows that the THO/TREX complex component Hpr1 interacts with the mRNA export factor Sub2 and plays a role in recruiting Sub2 to the mRNA during transcription. The study also shows links between the TREX complex and the nuclear exosome, suggesting that proper mRNP formation is co-transcriptionally monitored.
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(2002)
Mol. Cell Biol.
, vol.22
, pp. 8241-8253
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Zenklusen, D.1
Vinciguerra, P.2
Wyss, J.C.3
Stutz, F.4
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19
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18744370194
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The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores
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Sac3 is identified as a new mRNA export factor. Sac3 was shown to interact with specific proteins, leading to the proposal that Sac3 is loaded onto mRNA co-transcriptionally and later functions to dock the mRNP at the nuclear pore
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Fischer T., Strasser K., Racz A., Rodriguez-Navarro S., Oppizzi M., Ihrig P., Lechner J., Hurt E. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. EMBO J. 21:2002;5843-5852 Sac3 is identified as a new mRNA export factor. Sac3 was shown to interact with specific proteins, leading to the proposal that Sac3 is loaded onto mRNA co-transcriptionally and later functions to dock the mRNP at the nuclear pore.
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EMBO J.
, vol.21
, pp. 5843-5852
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Fischer, T.1
Strasser, K.2
Racz, A.3
Rodriguez-Navarro, S.4
Oppizzi, M.5
Ihrig, P.6
Lechner, J.7
Hurt, E.8
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20
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0037342695
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Sac3 is an mRNA export factor that localizes to the cytoplasmic fibrils of the nuclear pore complex
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This study also identifies Sac3 as a new mRNA export factor. The authors show that Sac3 localizes to the cytoplasmic fibrils and may play a role in a terminal step of mRNP translocation
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Lei E.P., Stern C.A., Fahrenkrog B., Krebber H., Moy T.I., Aebi U., Silver P.A. Sac3 is an mRNA export factor that localizes to the cytoplasmic fibrils of the nuclear pore complex. Mol. Biol. Cell. 14:2002;836-847 This study also identifies Sac3 as a new mRNA export factor. The authors show that Sac3 localizes to the cytoplasmic fibrils and may play a role in a terminal step of mRNP translocation.
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(2002)
Mol. Biol. Cell
, vol.14
, pp. 836-847
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Lei, E.P.1
Stern, C.A.2
Fahrenkrog, B.3
Krebber, H.4
Moy, T.I.5
Aebi, U.6
Silver, P.A.7
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21
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0036889142
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Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation
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This study reports a link between the TREX complex and the nuclear exosome, providing further evidence for the author's proposal that the exosome monitors proper mRNP formation co-transcriptionally
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Libri D., Dower K., Boulay J., Thomsen R., Rosbash M., Jensen T.H. Interactions between mRNA export commitment, 3′-end quality control, and nuclear degradation. Mol. Cell Biol. 22:2002;8254-8266 This study reports a link between the TREX complex and the nuclear exosome, providing further evidence for the author's proposal that the exosome monitors proper mRNP formation co-transcriptionally.
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Mol. Cell Biol.
, vol.22
, pp. 8254-8266
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Libri, D.1
Dower, K.2
Boulay, J.3
Thomsen, R.4
Rosbash, M.5
Jensen, T.H.6
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22
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0037180825
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The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila
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This study is the first to show that the nuclear exosome is recruited to actively transcribed genes. The elongation factors Spt5 and Spt6 are in a complex with the exosome and may play a role in recruiting it to active genes. The study further strengthens the notion that proper mRNP formation is monitored during transcription
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Andrulis E.D., Werner J., Nazarian A., Erdjument-Bromage H., Tempst P., Lis J.T. The RNA processing exosome is linked to elongating RNA polymerase II in Drosophila. Nature. 420:2002;837-841 This study is the first to show that the nuclear exosome is recruited to actively transcribed genes. The elongation factors Spt5 and Spt6 are in a complex with the exosome and may play a role in recruiting it to active genes. The study further strengthens the notion that proper mRNP formation is monitored during transcription.
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(2002)
Nature
, vol.420
, pp. 837-841
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Andrulis, E.D.1
Werner, J.2
Nazarian, A.3
Erdjument-Bromage, H.4
Tempst, P.5
Lis, J.T.6
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23
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0036252704
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T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export
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This study shows that 3′-end formation plays a key role in mRNA export in yeast
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Dower K., Rosbash M. T7 RNA polymerase-directed transcripts are processed in yeast and link 3′ end formation to mRNA nuclear export. RNA. 8:2002;686-697 This study shows that 3′-end formation plays a key role in mRNA export in yeast.
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(2002)
RNA
, vol.8
, pp. 686-697
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Dower, K.1
Rosbash, M.2
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24
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0036723624
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Coupling of termination, 3′ processing, and mRNA export
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These authors report that termination and 3′ end processing are coupled to mRNA export in yeast
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Hammell C.M., Gross S., Zenklusen D., Heath C.V., Stutz F., Moore C., Cole C.N. Coupling of termination, 3′ processing, and mRNA export. Mol. Cell Biol. 22:2002;6441-6457 These authors report that termination and 3′ end processing are coupled to mRNA export in yeast.
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Mol. Cell Biol.
, vol.22
, pp. 6441-6457
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Hammell, C.M.1
Gross, S.2
Zenklusen, D.3
Heath, C.V.4
Stutz, F.5
Moore, C.6
Cole, C.N.7
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25
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0036829065
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U1 snRNA associates with TFIIH and regulates transcriptional initiation
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Kwek K.Y., Murphy S., Furger A., Thomas B., O'Gorman W., Kimura H., Proudfoot N.J., Akoulitchev A. U1 snRNA associates with TFIIH and regulates transcriptional initiation. Nat. Struct. Biol. 9:2002;800-805.
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Nat. Struct. Biol.
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Kwek, K.Y.1
Murphy, S.2
Furger, A.3
Thomas, B.4
O'Gorman, W.5
Kimura, H.6
Proudfoot, N.J.7
Akoulitchev, A.8
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26
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0037064150
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Coordinate regulation of transcription and splicing by steroid receptor coregulators
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Auboeuf D., Honig A., Berget S.M., O'Malley B.W. Coordinate regulation of transcription and splicing by steroid receptor coregulators. Science. 298:2002;416-419.
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(2002)
Science
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, pp. 416-419
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Auboeuf, D.1
Honig, A.2
Berget, S.M.3
O'Malley, B.W.4
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27
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0036829698
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Promoter proximal splice sites enhance transcription
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Furger A., O'Sullivan J.M., Binnie A., Lee B.A., Proudfoot N.J. Promoter proximal splice sites enhance transcription. Genes Dev. 16:2002;2792-2799.
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Genes Dev.
, vol.16
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Furger, A.1
O'Sullivan, J.M.2
Binnie, A.3
Lee, B.A.4
Proudfoot, N.J.5
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28
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0037062415
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Regulation of alternative splicing by a transcriptional enhancer through RNA pol II elongation
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Kadener S., Fededa J.P., Rosbash M., Kornblihtt A.R. Regulation of alternative splicing by a transcriptional enhancer through RNA pol II elongation. Proc. Natl. Acad. Sci. U.S.A. 99:2002;8185-8190.
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Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 8185-8190
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Kadener, S.1
Fededa, J.P.2
Rosbash, M.3
Kornblihtt, A.R.4
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29
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0036242097
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Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis
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Jurica M.S., Licklider L.J., Gygi S.R., Grigorieff N., Moore M.J. Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA. 8:2002;426-439.
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(2002)
RNA
, vol.8
, pp. 426-439
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Jurica, M.S.1
Licklider, L.J.2
Gygi, S.R.3
Grigorieff, N.4
Moore, M.J.5
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30
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0037168541
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Protein composition of human prespliceosomes isolated by a tobramycin affinity-selection method
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Hartmuth K., Urlaub H., Vornlocher H.P., Will C.L., Gentzel M., Wilm M., Luhrmann R. Protein composition of human prespliceosomes isolated by a tobramycin affinity-selection method. Proc. Natl. Acad. Sci. U.S.A. 99:2002;16719-16724.
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(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
, pp. 16719-16724
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Hartmuth, K.1
Urlaub, H.2
Vornlocher, H.P.3
Will, C.L.4
Gentzel, M.5
Wilm, M.6
Luhrmann, R.7
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31
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0037068447
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Comprehensive proteomic analysis of the human spliceosome
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Zhou Z., Licklider L.J., Gygi S.P., Reed R. Comprehensive proteomic analysis of the human spliceosome. Nature. 419:2002;182-185.
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(2002)
Nature
, vol.419
, pp. 182-185
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Zhou, Z.1
Licklider, L.J.2
Gygi, S.P.3
Reed, R.4
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32
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0036674269
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Large-scale proteomic analysis of the human spliceosome
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Rappsilber J., Ryder U., Lamond A.I., Mann M. Large-scale proteomic analysis of the human spliceosome. Genome. Res. 12:2002;1231-1245.
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(2002)
Genome. Res.
, vol.12
, pp. 1231-1245
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Rappsilber, J.1
Ryder, U.2
Lamond, A.I.3
Mann, M.4
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