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Cited by 1,013

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

TnphoA: a transposon probe for protein export signals.

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Manoil, C, Beckwith, J·1985·Proceedings of the National Academy of Sciences

Abstract

We constructed a derivative of transposon Tn5 that permits the generation of hybrid proteins composed of alkaline phosphatase (EC 3.1.3.1) lacking its signal peptide fused to amino-terminal sequences of other proteins. Such a hybrid gives alkaline phosphatase activity if the protein fused to alkaline phosphatase contributes sequences that promote export and thus compensate for the missing alkaline phosphatase signal peptide. Fusions to both a secreted periplasmic protein and a complex cytoplasmic membrane protein led to alkaline phosphatase activity. TnphoA fusions should help localize export signals within the structure of a protein, such as a transmembrane protein, as well as identify new chromosomal genes for secreted and transmembrane proteins.

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Metadata

Authors
Manoil, C., & Beckwith, J.
Venue
Proceedings of the National Academy of Sciences
Published
1985-12
Volume
82
Issue
23
Pages
8129-8133
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2095448507
Cited by
1,013
References
1
FWCI
16.26
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: TnphoA: a transposon probe for protein export signals. https://app.cochat.ai/papers/10.1073/pnas.82.23.8129
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Manoil, C., & Beckwith, J. (1985). TnphoA: a transposon probe for protein export signals. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.82.23.8129

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