Arkady Mustaev
Rutgers Biomedical and Health Sciences
80 Papers
1.1K Citations
Arkady Mustaev is an academic researcher from Rutgers Biomedical and Health Sciences. The author has contributed to research in topics: RNA polymerase & Polymerase. The author has an hindex of 36, co-authored 78 publications. Previous affiliations of Arkady Mustaev include Public Health Research Institute & Rutgers University.
Chat about Author
Papers
Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase
Elizabeth A. Campbell,Nataliya Korzheva,Arkady Mustaev,Katsuhiko S. Murakami,Satish K. Nair,Alex Goldfarb,Seth A. Darst +6 more
TL;DR: The crystal structure of Thermus aquaticus core RNAP complexed with Rif explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length.
1.4K
Quinolones: Action and Resistance Updated
TL;DR: Quinolone resistance arises stepwise through selective amplification of mutants when drug concentrations are above the MIC and below the MPC, as observed with static agar plate assays, dynamic in vitro systems, and experimental infection of rabbits.
360
Mapping of Catalytic Residues in the RNA Polymerase Active Center
Evgeny Zaychikov,Emil Martin,Ludmila Denissova,Maxim Kozlov,Vadim Markovtsov,Mikhail Kashlev,Hermann Heumann,Vadim Nikiforov,Alex Goldfarb,Arkady Mustaev +9 more
TL;DR: The mutant RNAP is catalytically inactive but can bind promoters and form an open complex, but fails to support Fe2+-induced cleavage of DNA or protein.
170
TFB2 is a transient component of the catalytic site of the human mitochondrial RNA polymerase.
TL;DR: The data indicate that the transcriptional machinery in human mitochondria has evolved into a system that combines features inherited from self-sufficient, T7-like RNA polymerase and those typically found in systems comprising cellular multi-subunit polymerases, and provide insights into the molecular mechanisms of transcription regulation in mitochondria.
141
Donation of catalytic residues to RNA polymerase active center by transcription factor Gre
TL;DR: It is shown that Gre acts by providing two carboxylate residues for coordination of catalytic Mg2+ ion in the RNAP active center by using RNA-protein crosslinking in defined ternary elongating complexes, site-directed mutagenesis, discriminative biochemical assays, and docking of the two protein structures.
123