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Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.

Data up to Jan 2025

Published1989
Citations48
References35

Total Citations Per Year

Abstract

References (35)

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The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domain

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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

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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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Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent… (1989) – The EMBO Journal | Metascience Observatory Explorer