Dependence of secretion and assembly of type 1 fimbrial subunits of Escherichia coli on normal protein export
about
Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coliFimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteriaReciprocal exchange of minor components of type 1 and F1C fimbriae results in hybrid organelles with changed receptor specificities.Immunoelectron microscopic analysis of elongation of type 1 fimbriae in Escherichia coli.Mapping of export signals of Pseudomonas aeruginosa pilin with alkaline phosphatase fusions.Cloning and expression of the pilin gene of Pseudomonas aeruginosa PAK in Escherichia coli.Kinetic analysis of the synthesis and assembly of type 1 fimbriae of Escherichia coliExpression of K99 adhesion antigen controlled by the Escherichia coli tryptophan operon promoterThe export systems of type 1 and F1C fimbriae are interchangeable but work in parental pairsPapD, a periplasmic transport protein in P-pilus biogenesis.The chaperone-assisted membrane release and folding pathway is sensed by two signal transduction systems
P2860
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P2860
Dependence of secretion and assembly of type 1 fimbrial subunits of Escherichia coli on normal protein export
description
1984 nî lūn-bûn
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1984年の論文
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name
Dependence of secretion and as ...... coli on normal protein export
@ast
Dependence of secretion and as ...... coli on normal protein export
@en
type
label
Dependence of secretion and as ...... coli on normal protein export
@ast
Dependence of secretion and as ...... coli on normal protein export
@en
prefLabel
Dependence of secretion and as ...... coli on normal protein export
@ast
Dependence of secretion and as ...... coli on normal protein export
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P2093
P2860
P1476
Dependence of secretion and as ...... coli on normal protein export
@en
P2093
B I Eisenstein
P J Bassford
P2860
P304
P407
P577
1984-09-01T00:00:00Z