Structural basis for substrate loading in bacterial RNA polymerase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature05931.pdf
Reference42 articles.
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3. Landick, R. NTP-entry routes in multi-subunit RNA polymerases. Trends Biochem. Sci. 30, 651–654 (2005)
4. Svetlov, V., Vassylyev, D. G. & Artsimovitch, I. Discrimination against deoxyribonucleotide substrates by bacterial RNA polymerase. J. Biol. Chem. 279, 38087–38090 (2004)
5. Kettenberger, H., Armache, K. J. & Cramer, P. Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Mol. Cell 16, 955–965 (2004)
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