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Kent, R. B., Guterman, S. K. (1982) Pyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity. Proceedings of the National Academy of Sciences, 79 (13) 3992-3996 doi:10.1073/pnas.79.13.3992

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Reference TypeJournal (article/letter/editorial)
TitlePyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity.
JournalProceedings of the National Academy of Sciences
AuthorsKent, R. B.Author
Guterman, S. K.Author
Year1982 (July 1)Volume79
Issue13
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.79.13.3992Search in ResearchGate
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Mindat Ref. ID1421373Long-form Identifiermindat:1:5:1421373:9
GUID0
Full ReferenceKent, R. B., Guterman, S. K. (1982) Pyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity. Proceedings of the National Academy of Sciences, 79 (13) 3992-3996 doi:10.1073/pnas.79.13.3992
Plain TextKent, R. B., Guterman, S. K. (1982) Pyrophosphate inhibition of rho ATPase: a mechanism of coupling to RNA polymerase activity. Proceedings of the National Academy of Sciences, 79 (13) 3992-3996 doi:10.1073/pnas.79.13.3992
In(1982, July) Proceedings of the National Academy of Sciences Vol. 79 (13) Proceedings of the National Academy of Sciences

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Das, A., Merril, C., Adhya, S. (1978) Interaction of RNA polymerase and rho in transcription termination: coupled ATPase. Proceedings of the National Academy of Sciences, 75 (10) 4828-4832 doi:10.1073/pnas.75.10.4828
Jin, D. J., Burgess, R. R., Richardson, J. P., Gross, C. A. (1992) Termination efficiency at rho-dependent terminators depends on kinetic coupling between RNA polymerase and rho. Proceedings of the National Academy of Sciences, 89 (4) 1453-1457 doi:10.1073/pnas.89.4.1453
Carroll, S. B., Stollar, B. D. (1982) Inhibitory monoclonal antibody to calf thymus RNA polymerase II blocks formation of enzyme-DNA complexes. Proceedings of the National Academy of Sciences, 79 (23) 7233-7237 doi:10.1073/pnas.79.23.7233
Jove, R., Manley, J. L. (1982) Transcription initiation by RNA polymerase II is inhibited by S-adenosylhomocysteine. Proceedings of the National Academy of Sciences, 79 (19) 5842-5846 doi:10.1073/pnas.79.19.5842
Vishwakarma, Rishi K., Qayyum, M. Zuhaib, Babitzke, Paul, Murakami, Katsuhiko S. (2023) Allosteric mechanism of transcription inhibition by NusG-dependent pausing of RNA polymerase. Proceedings of the National Academy of Sciences, 120 (7) doi:10.1073/pnas.2218516120
Fisher, R., Blumenthal, T. (1982) An interaction between gramicidin and the sigma subunit of RNA polymerase. Proceedings of the National Academy of Sciences, 79 (4) 1045-1048 doi:10.1073/pnas.79.4.1045
Goodno, C. C., Taylor, E. W. (1982) Inhibition of actomyosin ATPase by vanadate. Proceedings of the National Academy of Sciences, 79 (1) 21-25 doi:10.1073/pnas.79.1.21
Blumenthal, R. M., Reeh, S., Pedersen, S. (1976) Regulation of transcription factor rho and the alpha subunit of RNA polymerase in Escherichia coli B/r. Proceedings of the National Academy of Sciences, 73 (7) 2285-2288 doi:10.1073/pnas.73.7.2285
Biebricher, C. K., Druminski, M. (1980) Inhibition of RNA polymerase activity by the Escherichia coli protein biosynthesis elongation factor Ts. Proceedings of the National Academy of Sciences, 77 (2) 866-869 doi:10.1073/pnas.77.2.866
Cohen, S. N., Yielding, K. L. (1965) Inhibition of DNA and RNA polymerase reactions by chloroquine. Proceedings of the National Academy of Sciences, 54 (2) 521-527 doi:10.1073/pnas.54.2.521
Grummt, I. (1982) Nucleotide sequence requirements for specific initiation of transcription by RNA polymerase I. Proceedings of the National Academy of Sciences, 79 (22) 6908-6911 doi:10.1073/pnas.79.22.6908
 
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