DbpA is a region-specific RNA helicase

Por Moore, Anthony F.T., Gentry, Riley C., Koculi, Eda
Publicado no Biopolymers (2017)

Charge density of divalent metal cations determines RNA stability

Por Koculi, Eda, Hyeon, Changbong, Thirumalai, D., Woodson, Sarah A.
Publicado em 2007

Nuclear Magnetic Resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL

Por Koculi, Eda, Horst, Reto, Horwich, Arthur L, Wüthrich, Kurt
Publicado em 2011

Folding path of P5abc RNA involves direct coupling of secondary and tertiary structures

Por Koculi, Eda, Cho, Samuel S., Desai, Ravi, Thirumalai, D., Woodson, Sarah A.
Publicado em 2012

The DbpA catalytic core unwinds double-helix substrates by directly loading on them

Por Childs, Jared J., Gentry, Riley C., Moore, Anthony F.T., Koculi, Eda
Publicado no RNA (2016)

Kinetics and Thermodynamics of DbpA Protein’s C-Terminal Domain Interaction with RNA

Por López de Victoria, Aliana, Moore, Anthony F. T., Gittis, Apostolos G., Koculi, Eda
Publicado no ACS Omega (2017)

Time course of large ribosomal subunit assembly in E. coli cells overexpressing a helicase inactive DbpA protein

Por Gentry, Riley C., Childs, Jared J., Gevorkyan, Jirair, Gerasimova, Yulia V., Koculi, Eda
Publicado no RNA (2016)