Maximal Efficiency of Coupling between ATP Hydrolysis and Translocation of Polypeptides Mediated by SecB Requires Two Protomers of SecA

Por Mao, Chunfeng, Hardy, Simon J. S., Randall, Linda L.
Publicado em 2009

Single-molecule observation of nucleotide induced conformational changes in basal SecA-ATP hydrolysis

Por Chada, Nagaraju, Chattrakun, Kanokporn, Marsh, Brendan P., Mao, Chunfeng, Bariya, Priya, King, Gavin M.
Publicado no Sci Adv (2018)

Dynamic Structure of the Translocon SecYEG in Membrane: DIRECT SINGLE MOLECULE OBSERVATIONS

Por Sanganna Gari, Raghavendar Reddy, Frey, Nathan C., Mao, Chunfeng, Randall, Linda L., King, Gavin M.
Publicado em 2013

Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling

Por Crane, Jennine M., Suo, Yuying, Lilly, Angela A., Mao, Chunfeng, Hubbell, Wayne L., Randall, Linda L.
Publicado em 2006

Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers

Por Sanganna Gari, Raghavendar Reddy, Chattrakun, Kanokporn, Marsh, Brendan P., Mao, Chunfeng, Chada, Nagaraju, Randall, Linda L., King, Gavin M.
Publicado no Sci Adv (2019)

Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species

Por Mao, Chunfeng, Cheadle, Carl E., Hardy, Simon J. S., Lilly, Angela A., Suo, Yuying, Sanganna Gari, Raghavendar Reddy, King, Gavin M., Randall, Linda L.
Publicado em 2013