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Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W
scientific journal article
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scholarly article
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PubMed
PubMed ID
8331069
retrieved
24 January 2017
title
Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W
(English)
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PubMed
PubMed ID
8331069
retrieved
24 January 2017
main subject
Pseudomonas aeruginosa
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author name string
D. N. Nunn
series ordinal
1
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stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
S. Lory
series ordinal
2
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stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
language of work or name
English
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publication date
1 July 1993
1 reference
stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
published in
Journal of Bacteriology
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stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
volume
175
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stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
page(s)
4375–4382
1 reference
stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
issue
14
1 reference
stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
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Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase
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Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu
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Protein secretion in Pseudomonas aeruginosa
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Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase
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Structural characterization of protein secretion genes of the bacterial phytopathogen Xanthomonas campestris pathovar campestris: relatedness to secretion systems of other gram-negative bacteria
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Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria
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The Aeromonas hydrophila exeE gene, required both for protein secretion and normal outer membrane biogenesis, is a member of a general secretion pathway
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An enzyme with type IV prepilin peptidase activity is required to process components of the general extracellular protein secretion pathway of Klebsiella oxytoca
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2 June 2018
Heme biosynthesis in Rhizobium. Identification of a cloned gene coding for delta-aminolevulinic acid synthetase from Rhizobium meliloti
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reference URL
https://pubmed.ncbi.nlm.nih.gov/8331069
retrieved
12 December 2020
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inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/JB.175.14.4375-4382.1993
0 references
PMCID
204877
0 references
PubMed ID
8331069
1 reference
stated in
PubMed
PubMed ID
8331069
retrieved
24 January 2017
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