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Rudd, M. D., Izban, M. G., Luse, D. S. (1994) The active site of RNA polymerase II participates in transcript cleavage within arrested ternary complexes. Proceedings of the National Academy of Sciences, 91 (17) 8057-8061 doi:10.1073/pnas.91.17.8057

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Reference TypeJournal (article/letter/editorial)
TitleThe active site of RNA polymerase II participates in transcript cleavage within arrested ternary complexes.
JournalProceedings of the National Academy of Sciences
AuthorsRudd, M. D.Author
Izban, M. G.Author
Luse, D. S.Author
Year1994 (August 16)Volume91
Issue17
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.91.17.8057Search in ResearchGate
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Mindat Ref. ID1543681Long-form Identifiermindat:1:5:1543681:4
GUID0
Full ReferenceRudd, M. D., Izban, M. G., Luse, D. S. (1994) The active site of RNA polymerase II participates in transcript cleavage within arrested ternary complexes. Proceedings of the National Academy of Sciences, 91 (17) 8057-8061 doi:10.1073/pnas.91.17.8057
Plain TextRudd, M. D., Izban, M. G., Luse, D. S. (1994) The active site of RNA polymerase II participates in transcript cleavage within arrested ternary complexes. Proceedings of the National Academy of Sciences, 91 (17) 8057-8061 doi:10.1073/pnas.91.17.8057
In(1994, August) Proceedings of the National Academy of Sciences Vol. 91 (17) Proceedings of the National Academy of Sciences

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Donahue, B. A., Yin, S., Taylor, J. S., Reines, D., Hanawalt, P. C. (1994) Transcript cleavage by RNA polymerase II arrested by a cyclobutane pyrimidine dimer in the DNA template. Proceedings of the National Academy of Sciences, 91 (18) 8502-8506 doi:10.1073/pnas.91.18.8502
Cipres-Palacin, G., Kane, C. M. (1994) Cleavage of the nascent transcript induced by TFIIS is insufficient to promote read-through of intrinsic blocks to elongation by RNA polymerase II. Proceedings of the National Academy of Sciences, 91 (17) 8087-8091 doi:10.1073/pnas.91.17.8087
Pal, M., Luse, D. S. (2003) The initiation-elongation transition: Lateral mobility of RNA in RNA polymerase II complexes is greatly reduced at +8/+9 and absent by +23. Proceedings of the National Academy of Sciences, 100 (10) 5700-5705 doi:10.1073/pnas.1037057100
Palangat, M., Renner, D. B., Price, D. H., Landick, R. (2005) A negative elongation factor for human RNA polymerase II inhibits the anti-arrest transcript-cleavage factor TFIIS. Proceedings of the National Academy of Sciences, 102 (42) 15036-15041 doi:10.1073/pnas.0409405102
Luse, Donal S. (2019) Insight into promoter clearance by RNA polymerase II. Proceedings of the National Academy of Sciences, 116 (45) 22426-22428 doi:10.1073/pnas.1916582116
Orlova, M., Newlands, J., Das, A., Goldfarb, A., Borukhov, S. (1995) Intrinsic transcript cleavage activity of RNA polymerase. Proceedings of the National Academy of Sciences, 92 (10) 4596-4600 doi:10.1073/pnas.92.10.4596
Altmann, C. R., Solow-Cordero, D. E., Chamberlin, M. J. (1994) RNA cleavage and chain elongation by Escherichia coli DNA-dependent RNA polymerase in a binary enzyme.RNA complex. Proceedings of the National Academy of Sciences, 91 (9) 3784-3788 doi:10.1073/pnas.91.9.3784
Surratt, C. K., Milan, S. C., Chamberlin, M. J. (1991) Spontaneous cleavage of RNA in ternary complexes of Escherichia coli RNA polymerase and its significance for the mechanism of transcription. Proceedings of the National Academy of Sciences, 88 (18) 7983-7987 doi:10.1073/pnas.88.18.7983
Cabart, P., Ujvari, A., Pal, M., Luse, D. S. (2011) Transcription factor TFIIF is not required for initiation by RNA polymerase II, but it is essential to stabilize transcription factor TFIIB in early elongation complexes. Proceedings of the National Academy of Sciences, 108 (38) 15786-15791 doi:10.1073/pnas.1104591108
Morrow, C. D., Warren, B., Lentz, M. R. (1987) Expression of enzymatically active poliovirus RNA-dependent RNA polymerase in Escherichia coli. Proceedings of the National Academy of Sciences, 84 (17) 6050-6054 doi:10.1073/pnas.84.17.6050
Gu, W., Wind, M., Reines, D. (1996) Increased accommodation of nascent RNA in a product site on RNA polymerase II during arrest. Proceedings of the National Academy of Sciences, 93 (14) 6935-6940 doi:10.1073/pnas.93.14.6935
 
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