The NusA N-terminal domain is necessary and sufficient for enhancement of transcriptional pausing via interaction with the RNA exit channel of RNA polymerase. - Abstract - Europe PMC
Two-step metal affinity purification of double-tagged (NusA–His6) fusion proteins | Nature Protocols
Addgene: pET His6 NusA TEV LIC cloning vector (1N)
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Two-step metal affinity purification of double-tagged (NusA–His6) fusion proteins | Nature Protocols
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New trends and affinity tag designs for recombinant protein purification - ScienceDirect
Two-step metal affinity purification of double-tagged (NusA–His6) fusion proteins | Nature Protocols
Antitermination - an overview | ScienceDirect Topics
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1. Comparison of protein expression and solubility properties among... | Download Scientific Diagram
Structural basis for the interaction of Escherichia coli NusA with protein N of phage λ | PNAS
Escherichia coli transcription termination factor NusA: heat-induced oligomerization and chaperone activity | Scientific Reports
