Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli

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Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. / Pedersen, P. A.

I: Molecular Microbiology, Bind 5, Nr. 5, 01.01.1991, s. 1073-1080.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Pedersen, PA 1991, 'Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli', Molecular Microbiology, bind 5, nr. 5, s. 1073-1080. https://doi.org/10.1111/j.1365-2958.1991.tb01879.x

APA

Pedersen, P. A. (1991). Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. Molecular Microbiology, 5(5), 1073-1080. https://doi.org/10.1111/j.1365-2958.1991.tb01879.x

Vancouver

Pedersen PA. Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. Molecular Microbiology. 1991 jan. 1;5(5):1073-1080. https://doi.org/10.1111/j.1365-2958.1991.tb01879.x

Author

Pedersen, P. A. / Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. I: Molecular Microbiology. 1991 ; Bind 5, Nr. 5. s. 1073-1080.

Bibtex

@article{11d41437794b4021b2a02dec395d5241,
title = "Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli",
abstract = "Several in‐frame linker insertions have been made in various positions in the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The effects of the linker insertions have been investigated with regard to the ability of the mutated fimbrial subunits to be exported to the surface of the bacterial cell and assembled into a fimbrial structure. The structure/function relationship of the subunit protein is discussed in the light of the phenotypes of the mutations constructed, secondary structure predictions, and hydrophilicity plots.",
author = "Pedersen, {P. A.}",
year = "1991",
month = jan,
day = "1",
doi = "10.1111/j.1365-2958.1991.tb01879.x",
language = "English",
volume = "5",
pages = "1073--1080",
journal = "Molecular Microbiology",
issn = "0950-382X",
publisher = "Wiley-Blackwell",
number = "5",

}

RIS

TY - JOUR

T1 - Structure‐function analysis of the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli

AU - Pedersen, P. A.

PY - 1991/1/1

Y1 - 1991/1/1

N2 - Several in‐frame linker insertions have been made in various positions in the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The effects of the linker insertions have been investigated with regard to the ability of the mutated fimbrial subunits to be exported to the surface of the bacterial cell and assembled into a fimbrial structure. The structure/function relationship of the subunit protein is discussed in the light of the phenotypes of the mutations constructed, secondary structure predictions, and hydrophilicity plots.

AB - Several in‐frame linker insertions have been made in various positions in the faeG gene encoding the K88ab fimbrial subunit protein from porcine enterotoxigenic Escherichia coli. The effects of the linker insertions have been investigated with regard to the ability of the mutated fimbrial subunits to be exported to the surface of the bacterial cell and assembled into a fimbrial structure. The structure/function relationship of the subunit protein is discussed in the light of the phenotypes of the mutations constructed, secondary structure predictions, and hydrophilicity plots.

UR - http://www.scopus.com/inward/record.url?scp=0025778608&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2958.1991.tb01879.x

DO - 10.1111/j.1365-2958.1991.tb01879.x

M3 - Journal article

C2 - 1683467

AN - SCOPUS:0025778608

VL - 5

SP - 1073

EP - 1080

JO - Molecular Microbiology

JF - Molecular Microbiology

SN - 0950-382X

IS - 5

ER -

ID: 227044196