Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.
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References (35)
Construction of Biologically Functional Bacterial Plasmids In Vitro
1973 • 1,699 citations
Intracellular protein topogenesis
1980 • 1,378 citations
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
1986 • 861 citations
Multiple Mechanisms of Protein Insertion into and Across Membranes
1985 • 720 citations
Topogenic signals in integral membrane proteins
1988 • 715 citations
Primary structure and transmembrane orientation of the murine anion exchange protein
1985 • 552 citations
Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptor.
1984 • 513 citations
The Assembly of Proteins into Biological Membranes: The Membrane Trigger Hypothesis
1979 • 408 citations
Secretion and Membrane Localization of Proteins inEscherichia Coli
1980 • 402 citations
Many Random Sequences Functionally Replace the Secretion Signal Sequence of Yeast Invertase
1987 • 375 citations
Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope.
1983 • 307 citations
Determinants of membrane protein topology.
1987 • 301 citations
Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane.
1985 • 292 citations
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
1988 • 263 citations
Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli.
1985 • 217 citations
Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli.
1983 • 214 citations
An internal signal sequence: The asialoglycoprotein receptor membrane anchor
1986 • 209 citations
An artificial anchor domain: hydrophobicity suffices to stop transfer
1985 • 206 citations
Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat protein.
1980 • 200 citations
The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme.
1982 • 179 citations
Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coli.
1988 • 163 citations
NH2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation.
1984 • 156 citations
The transmembrane segment of the human transferrin receptor functions as a signal peptide.
1986 • 151 citations
High-level expression of M13 gene II protein from an inducible polycistronic messenger RNA
1985 • 130 citations
Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein.
1987 • 113 citations
Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. Relation to the orientation of membrane proteins.
1988 • 100 citations
The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain
1986 • 92 citations
A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coli.
1987 • 90 citations
Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteins
1984 • 84 citations
Foreign transmembrane peptides replacing the internal signal sequence of transferrin receptor allow its translocation and membrane binding
1987 • 75 citations
Leader Peptidase of Escherichia coli : Critical Role of a Small Domain in Membrane Assembly
1987 • 72 citations
Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli.
1987 • 69 citations
The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membrane.
1986 • 68 citations
The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence.
1988 • 61 citations
The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assembly.
1987 • 47 citations
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