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RNA Biology|November 19, 2016
eIF4B stimulates eIF4A ATPase and unwinding activities by direct interaction through its 7-repeats regionAlexandra Zoi Andreou, Ulf Harms, Dagmar Klostermeier
The Journal of Biological Chemistry|February 25, 2014
The acidic C-terminal tail of the GyrA subunit moderates the DNA supercoiling activity of Bacillus subtilis gyraseMartin A Lanz, Mohamad Farhat, Dagmar Klostermeier
Biological Chemistry|September 15, 2009
The mechanism of ATP-dependent RNA unwinding by DEAD box proteinsManuel Hilbert, Anne R Karow, Dagmar Klostermeier
Biochemistry|March 23, 2005
The tertiary structure of the hairpin ribozyme is formed through a slow conformational searchGoran Pljevaljcić, Dagmar Klostermeier, David P Millar
The FEBS Journal|January 19, 2007
Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domainsAnne R Karow, Bettina Theissen, Dagmar Klostermeier
Nucleic Acids Research|January 25, 2017
Allosteric regulation of helicase core activities of the DEAD-box helicase YxiN by RNA binding to its RNA recognition motifBrighton Samatanga, Alexandra Z Andreou, Dagmar Klostermeier
Journal of Molecular Biology|June 28, 2020
A β-hairpin is a Minimal Latch that Supports Positive Supercoiling by Reverse GyraseFrederic Collin, Marine Weisslocker-Schaetzel, Dagmar Klostermeier
Nucleic Acids Research|November 11, 2010
eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanismManuel Hilbert, Fabian Kebbel, Airat Gubaev, et al.
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications|March 4, 2009
Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domainMarkus G Rudolph, Julia G Wittmann, Dagmar Klostermeier
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