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Current Opinion in Microbiology|April 3, 2001
Transcription elongation complex: structure and functionN Korzheva, A MustaevProceedings of the National Academy of Sciences of the United States of America|April 16, 1996
Protein-RNA interactions in the active center of transcription elongation complexV Markovtsov, A Mustaev, A GoldfarbThe Journal of Biological Chemistry|June 30, 1995
Studies of the functional topography of the catalytic center of Escherichia coli primaseA A Mustaev, G N GodsonJournal of Applied Microbiology|June 25, 2013
Growth-inhibitory activity of natural and synthetic isothiocyanates against representative human microbial pathogensN Kurepina, B N Kreiswirth, A MustaevThe Journal of Biological Chemistry|February 1, 2000
Identification of RNA polymerase beta' subunit segment contacting the melted region of the lacUV5 promoterK Brodolin, A Mustaev, K Severinov, et al.Biochemistry|April 2, 1998
ATP cross-linked to Escherichia coli single-strand DNA-binding protein can be utilized by the catalytic center of primase as initiating nucleotide for primer RNA synthesis on phage G4oric templateG N Godson, A A Mustaev, W SunGenes & Development|September 29, 1999
A zinc-binding site in the largest subunit of DNA-dependent RNA polymerase is involved in enzyme assemblyD Markov, T Naryshkina, A Mustaev, et al.Cell|April 4, 1997
The RNA-DNA hybrid maintains the register of transcription by preventing backtracking of RNA polymeraseE Nudler, A Mustaev, E Lukhtanov, et al.FEBS Letters|July 21, 1999
Interaction with free beta' subunit unmasks DNA-binding domain of RNA polymerase sigma subunitA Kulbachinskiy, A Mustaev, A Goldfarb, et al.The Journal of Biological Chemistry|March 30, 2001
The beta ' subunit of Escherichia coli RNA polymerase is not required for interaction with initiating nucleotide but is necessary for interaction with rifampicinT Naryshkina, A Mustaev, S A Darst, et al.Pageof 6