A Quantitative Description of the Binding States and In Vitro Function of Antitermination Protein N of Bacteriophage λ
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference52 articles.
1. Lytic mode of lambda development;Friedman,1983
2. Transcriptional antitermination;Greenblatt;Nature,1993
3. Components of multiprotein–RNA complex that controls transcriptional elongation in Escherichia coli phage lambda;Das;Methods Enzymol.,1996
4. Quantitative dissection of a transcriptional control system: the N-dependent antitermination complex of phage λ as a regulatory paradigm;Van Gilst;Methods Enzymol.,2000
5. Coliphage λ nutL−: a unique class of mutants defective in the site of gene N product utilization for antitermination of leftward transcription;Salstrom;J. Mol. Biol.,1978
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1. HK022 Nun Requires Arginine-Rich Motif Residues Distinct from λ N;Journal of Bacteriology;2015-11-15
2. Phage λ—New Insights into Regulatory Circuits;Bacteriophages, Part A;2012
3. The Antitermin ation Activity of Bacteriophage λ N Protein is Controlled by the Kinetics of an RNA-Looping-Facilitated Interaction with the Transcription Complex;Journal of Molecular Biology;2008-12
4. Bacteriophage P22 Antitermination boxB Sequence Requirements Are Complex and Overlap with Those of λ;Journal of Bacteriology;2008-06-15
5. Mechanisms of physiological regulation of RNA synthesis in bacteria: new discoveries breaking old schemes;Journal of Applied Genetics;2007-09
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