Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB. (Q39839578)

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English	Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB.	scientific article

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scholarly article

1 reference

Europe PubMed Central

15 September 2017

Ferrichrome transport in Escherichia coli K-12: altered substrate specificity of mutated periplasmic FhuD and interaction of FhuD with the integral membrane protein FhuB. (English)

1 reference

Europe PubMed Central

15 September 2017

Escherichia coli

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membrane protein

1 reference

based on heuristic

inferred from title

author name string

Rohrbach MR

1

1 reference

Europe PubMed Central

15 September 2017

Braun V

2

1 reference

Europe PubMed Central

15 September 2017

Köster W

3

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Europe PubMed Central

15 September 2017

language of work or name

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inferred from title

publication date

1 December 1995

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Europe PubMed Central

15 September 2017

Journal of Bacteriology

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Europe PubMed Central

15 September 2017

177

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Europe PubMed Central

15 September 2017

24

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Europe PubMed Central

15 September 2017

7186-7193

1 reference

Europe PubMed Central

15 September 2017

Insertion derivatives containing segments of up to 16 amino acids identify surface- and periplasm-exposed regions of the FhuA outer membrane receptor of Escherichia coli K-12.

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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Functions in outer and inner membranes of Escherichia coli for ferrichrome transport

1 reference

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1 reference

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1 reference

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1 reference

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fhuC and fhuD genes for iron (III)-ferrichrome transport into Escherichia coli K-12

1 reference

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The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis

1 reference

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1 reference

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Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport

1 reference

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An aspartate deletion mutation defines a binding site of the multifunctional FhuA outer membrane receptor of Escherichia coli K-12.

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Identifiers

10.1128/JB.177.24.7186-7193.1995

1 reference

Europe PubMed Central

15 September 2017

1 reference

Europe PubMed Central

15 September 2017

1 reference

Europe PubMed Central

15 September 2017

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