Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA

Por Randall, Linda L, Henzl, Michael T
Publicado em 2010

Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli

Por Findik, Bahar T., Randall, Linda L.
Publicado no PLoS One (2017)

Coassembly of SecYEG and SecA Fully Restores the Properties of the Native Translocon

Por Bariya, Priya, Randall, Linda L.
Publicado no J Bacteriol (2018)

The Sec System: Protein Export in Escherichia coli

Por Crane, Jennine M., Randall, Linda L.
Publicado no EcoSal Plus (2017)

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

Orientation of SecA and SecB in Complex, Derived from Disulfide Cross-Linking

Por Suo, Yuying, Hardy, Simon J. S., Randall, Linda L.
Publicado em 2011

The Basis of Asymmetry in the SecA-SecB Complex

Por Suo, Yuying, Hardy, Simon J. S., Randall, Linda L.
Publicado no J Mol Biol (2014)

Penetration into membrane of amino‐terminal region of SecA when associated with SecYEG in active complexes

Por Findik, Bahar T., Smith, Virginia F., Randall, Linda L.
Publicado no Protein Sci (2018)

Assembly In Vivo of Enterotoxin from Escherichia coli: Formation of the B Subunit Oligomer

Por Hirst, Timothy R., Hardy, Simon J. S., Randall, Linda L.
Publicado em 1983

Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export

Por Patel, Chetan N., Smith, Virginia F., Randall, Linda L.
Publicado em 2006

Complex behavior in solution of homodimeric SecA

Por Woodbury, Ronald L., Hardy, Simon J.S., Randall, Linda L.
Publicado em 2002

Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands

Por Lilly, Angela A, Crane, Jennine M, Randall, Linda L
Publicado em 2009

Characterization of Interactions Between Proteins Using Site-Directed Spin Labeling and Electron Paramagnetic Resonance Spectroscopy

Por Crane, Jennine M., Lilly, Angela A., Randall, Linda L.
Publicado no Methods Mol Biol (2010)

Sites of interaction between SecA and the chaperone SecB, two proteins involved in export

Por Randall, Linda L., Crane, Jennine M., Liu, Gseping, Hardy, Simon J.S.
Publicado em 2004

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

Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins

Por Randall, Linda L., Topping, Traci B., Hardy, Simon J. S., Pavlov, Michael Y., Freistroffer, David V., Ehrenberg, Måns
Publicado em 1997

SecA the motor of the secretion machine binds diverse partners on one interactive surface

Por Cooper, Dylan B., Smith, Virginia F., Crane, Jennine M., Roth, Hilary C., Lilly, Angela A., Randall, Linda L.
Publicado em 2008

Glass is a Viable Substrate for Precision Force Microscopy of Membrane Proteins

Por Chada, Nagaraju, Sigdel, Krishna P., Gari, Raghavendar Reddy Sanganna, Matin, Tina Rezaie, Randall, Linda L., King, Gavin M.
Publicado no Sci Rep (2015)

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)