Published in EMBO J on April 01, 1984
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Different exported proteins in E. coli show differences in the temporal mode of processing in vivo. Cell (1981) 2.87
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An estimation of the light-induced electrochemical potential difference of protons across the membrane of Halobacterium halobium. Biochim Biophys Acta (1976) 2.11
Modulation of folding pathways of exported proteins by the leader sequence. Science (1988) 2.10
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Evidence for multiple K+ export systems in Escherichia coli. J Bacteriol (1987) 1.78
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Specific cesium transport via the Escherichia coli Kup (TrkD) K+ uptake system. J Bacteriol (1989) 1.59
NAD+ binding to the Escherichia coli K(+)-uptake protein TrkA and sequence similarity between TrkA and domains of a family of dehydrogenases suggest a role for NAD+ in bacterial transport. Mol Microbiol (1993) 1.56
Identification of OmpT as the protease that hydrolyzes the antimicrobial peptide protamine before it enters growing cells of Escherichia coli. J Bacteriol (1998) 1.56
Evidence in support of a four transmembrane-pore-transmembrane topology model for the Arabidopsis thaliana Na+/K+ translocating AtHKT1 protein, a member of the superfamily of K+ transporters. Proc Natl Acad Sci U S A (2001) 1.50
K+-transport protein TrkA of Escherichia coli is a peripheral membrane protein that requires other trk gene products for attachment to the cytoplasmic membrane. J Biol Chem (1989) 1.49
Role of the leader peptide of maltose-binding protein in two steps of the export process. J Bacteriol (1988) 1.48
Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein. J Biol Chem (1988) 1.45
Processing in vivo of precursor maltose-binding protein in Escherichia coli occurs post-translationally as well as co-translationally. J Biol Chem (1981) 1.45
The effects of weak acids on potassium uptake by Escherichia coli K-12 inhibition by low cytoplasmic pH. Biochim Biophys Acta (1983) 1.40
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Accumulation of thallous ions (Tl+) as a measure of the electrical potential difference across the cytoplasmic membrane of bacteria. Biochemistry (1978) 1.32
The binding of carbon monoxide to cytochrome c oxidase. Eur J Biochem (1977) 1.31
Novel intermediates in the synthesis of maltose-binding protein in Escherichia coli. Eur J Biochem (1980) 1.28
Generation of a large, protonophore-sensitive proton motive force and pH difference in the acidophilic bacteria Thermoplasma acidophilum and Bacillus acidocaldarius. J Bacteriol (1985) 1.27
Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein. J Biol Chem (1995) 1.25
Nucleotide sequence and 3'-end deletion studies indicate that the K(+)-uptake protein kup from Escherichia coli is composed of a hydrophobic core linked to a large and partially essential hydrophilic C terminus. J Bacteriol (1993) 1.24
Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci (1994) 1.22
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Phenotypic properties of a unique rpoA mutation (phs) of Escherichia coli. J Bacteriol (1985) 1.18
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Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions. J Biol Chem (2000) 1.13
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Processing in vitro of precursor periplasmic proteins from Escherichia coli. Eur J Biochem (1978) 1.08
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Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein. Protein Sci (1997) 0.96
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A signal sequence mutant defective in export of ribose-binding protein and a corresponding pseudorevertant isolated without imposed selection. EMBO J (1985) 0.93
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