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Article

Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide.

Nature - 1 Jan 2000

Kendall D A, Bock S C, Kaiser E T

Abstract excerpt

Proteins secreted by prokaryotic cells are synthesized as precursors containing an amino-terminal extension sequence or signal peptide. Although these signal peptides share little primary sequence homology, recent studies suggest that they function via common pathways during the transport process and that a common element may reside in their secondary structural characteristics. We are investigating the role of...

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Source

Identifiers

PMID: 3520341
DOI: 10.1038/321706a0

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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Idealization of the hydrophobic segment of the alkaline phosphatase signal peptide.PMID 3520341Read ↗

A comparative analysis of single- and multiple-residue substitutions in the alkaline phosphatase signal peptide.Semantic proximity Read ↗

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Juxtaposition of signal-peptide charge and core region hydrophobicity is critical for functional signal peptides.Semantic proximity Read ↗

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Enhancement of protein translocation across the membrane by specific mutations in the hydrophobic region of the signal peptide.Semantic proximity Read ↗

Signal peptide mutants of Escherichia coli.Semantic proximity Read ↗

The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity.Semantic proximity Read ↗

Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidase.Semantic proximity Read ↗

Prediction of signal peptide functional properties: a study of the orientation and angle of insertion of yeast invertase mutants and human apolipoprotein B signal peptide variants.Semantic proximity Read ↗

The amino-terminal charge and core region hydrophobicity interdependently contribute to the function of signal sequences.Semantic proximity Read ↗

Optimisation of signal peptide for recombinant protein secretion in bacterial hosts.Semantic proximity Read ↗

The role of the conserved box E residues in the active site of the Escherichia coli type I signal peptidase.Semantic proximity Read ↗

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