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Cited by 288

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

Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane.

Open access
Inouye, S, Wang, S, Sekizawa, J, Halegoua, S, Inouye, M·1977·Proceedings of the National Academy of Sciences

Abstract

The messenger RNA for the lipoprotein of the E. coli outer membrane was found to code for a putative precursor, prolipoprotein, which has 20 additional amino acid residues extending from the amino terminus of the lipoprotein. Using the prolipoprotein synthesized in an E. coli cell-free system directed by purified messenger RNA for the lipoprotein, the complete amino acid sequence of the amino-terminal precursor region was determined to be as follows: (formula: see text). It was also found that the prolipoprotein that accumulates in toluene-treated cells has the same sequence. The significance of the amino acid sequence is discussed in terms of the mechanism of biosynthesis and assembly of the lipoprotein in the E. coli outer membrane.

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Metadata

Authors
Inouye, S., Wang, S., Sekizawa, J., Halegoua, S., & Inouye, M.
Venue
Proceedings of the National Academy of Sciences
Published
1977-03
Volume
74
Issue
3
Pages
1004-1008
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2053793124
Cited by
288
References
1
FWCI
31.55
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane. https://app.cochat.ai/papers/10.1073/pnas.74.3.1004
The paper
Inouye, S., Wang, S., Sekizawa, J., Halegoua, S., & Inouye, M. (1977). Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.74.3.1004

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