Published in Proc Natl Acad Sci U S A on July 01, 2013
Membrane chaperone SecDF plays a role in the secretion of Listeria monocytogenes major virulence factors. J Bacteriol (2013) 0.86
Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation. Elife (2016) 0.83
The pilus usher controls protein interactions via domain masking and is functional as an oligomer. Nat Struct Mol Biol (2015) 0.81
Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking. J Biol Chem (2016) 0.78
The basis of asymmetry in the SecA:SecB complex. J Mol Biol (2014) 0.78
Glass is a Viable Substrate for Precision Force Microscopy of Membrane Proteins. Sci Rep (2015) 0.76
Protein translocation: what's the problem? Biochem Soc Trans (2016) 0.76
Capturing the bacterial holo-complex. Proc Natl Acad Sci U S A (2014) 0.75
X-ray structure of a protein-conducting channel. Nature (2003) 9.20
Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli. Cell (1986) 5.09
The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation. Cell (1990) 4.78
Protein translocation across the bacterial cytoplasmic membrane. Annu Rev Biochem (2008) 4.07
The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins. Cell (1990) 4.00
Structure of a complex of the ATPase SecA and the protein-translocation channel. Nature (2008) 3.73
Structure of the E. coli protein-conducting channel bound to a translating ribosome. Nature (2005) 3.10
Orientation of membrane vesicles from Escherichia coli prepared by different procedures. J Membr Biol (1974) 2.66
Conformational transition of Sec machinery inferred from bacterial SecYE structures. Nature (2008) 2.48
Identification of a new gene (secA) and gene product involved in the secretion of envelope proteins in Escherichia coli. J Bacteriol (1982) 2.27
Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel. Cell (2007) 2.17
Three-dimensional structure of the bacterial protein-translocation complex SecYEG. Nature (2002) 2.16
Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli. J Biol Chem (1991) 1.90
No specific recognition of leader peptide by SecB, a chaperone involved in protein export. Science (1990) 1.75
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc Natl Acad Sci U S A (2010) 1.57
SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study. Biochemistry (1992) 1.52
Structure and function of a membrane component SecDF that enhances protein export. Nature (2011) 1.51
Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding. J Biol Chem (1992) 1.49
Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding. J Biol Chem (1997) 1.43
Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli. J Biol Chem (1995) 1.39
Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. J Mol Biol (2005) 1.39
SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm. Mol Microbiol (1996) 1.39
Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE. Biochemistry (1999) 1.38
A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation. J Biol Chem (1996) 1.38
Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli. Biochim Biophys Acta (1992) 1.37
Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes. J Biol Chem (2003) 1.28
Structure of the SecY complex unlocked by a preprotein mimic. Cell Rep (2012) 1.16
SecA, the motor of the secretion machine, binds diverse partners on one interactive surface. J Mol Biol (2008) 1.13
The oligomeric state and arrangement of the active bacterial translocon. J Biol Chem (2010) 1.09
Bacterial protein translocation requires only one copy of the SecY complex in vivo. J Cell Biol (2012) 1.08
Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms. J Bacteriol (1998) 1.06
The oligomeric distribution of SecYEG is altered by SecA and translocation ligands. J Mol Biol (2005) 1.05
Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase. Proc Natl Acad Sci U S A (2012) 1.02
Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking. J Biol Chem (2011) 1.02
Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export. Protein Sci (2006) 1.01
Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase. J Biol Chem (2000) 1.01
A single copy of SecYEG is sufficient for preprotein translocation. EMBO J (2011) 0.99
Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA. J Bacteriol (2008) 0.96
Translocase-bound SecA is largely shielded from the phospholipid acyl chains. Biochemistry (1998) 0.89
Orientation of SecA and SecB in complex, derived from disulfide cross-linking. J Bacteriol (2010) 0.87
Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations. J Biol Chem (2013) 0.84
Multiple SecA molecules drive protein translocation across a single translocon with SecG inversion. J Biol Chem (2011) 0.82
Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB. J Bacteriol (1995) 0.81
Using a low denaturant model to explore the conformational features of translocation-active SecA. Biochemistry (2012) 0.78
Complex behavior in solution of homodimeric SecA. Protein Sci (2002) 1.83
Stabilization of an optical microscope to 0.1 nm in three dimensions. Appl Opt (2007) 1.71
Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. J Mol Biol (2005) 1.39
Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export. J Mol Biol (2005) 1.34
SecA, the motor of the secretion machine, binds diverse partners on one interactive surface. J Mol Biol (2008) 1.13
Clustering requires modified methyl-accepting sites in low-abundance but not high-abundance chemoreceptors of Escherichia coli. Mol Microbiol (2005) 1.09
Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling. J Mol Biol (2006) 1.05
Routine and timely sub-picoNewton force stability and precision for biological applications of atomic force microscopy. Nano Lett (2012) 1.03
Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export. Protein Sci (2006) 1.01
Back-scattered detection provides atomic-scale localization precision, stability, and registration in 3D. Opt Express (2007) 0.96
Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA. J Bacteriol (2008) 0.96
Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands. Protein Sci (2009) 0.95
Sites of interaction between SecA and the chaperone SecB, two proteins involved in export. Protein Sci (2004) 0.94
Orientation of SecA and SecB in complex, derived from disulfide cross-linking. J Bacteriol (2010) 0.87
Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations. J Biol Chem (2013) 0.84
Heparinoids activate a protease, secreted by mucosa and tumors, via tethering supplemented by allostery. ACS Chem Biol (2014) 0.80
Three-dimensional atomic force microscopy: interaction force vector by direct observation of tip trajectory. Nano Lett (2013) 0.80
Label-free optical imaging of membrane patches for atomic force microscopy. Opt Express (2010) 0.78
Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy. Methods Mol Biol (2010) 0.78
Single-Molecule Peptide-Lipid Affinity Assay Reveals Interplay between Solution Structure and Partitioning. Langmuir (2017) 0.75