(Q39839578)

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.

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

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

PMC publication ID

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

PMC publication ID

15 September 2017

Braun V

2

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

Köster W

3

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

language of work or name

1 reference

based on heuristic

inferred from title

publication date

1 December 1995

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

Journal of Bacteriology

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

177

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

24

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

7186-7193

1 reference

Europe PubMed Central

PMC publication ID

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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Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein

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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1 reference

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1 reference

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1 reference

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Bacterial periplasmic binding protein tertiary structures

1 reference

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Maltose transport in membrane vesicles of Escherichia coli is linked to ATP hydrolysis

1 reference

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Bacterial periplasmic permeases belong to a family of transport proteins operating from Escherichia coli to human: Traffic ATPases

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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Iron(III) hydroxamate transport across the cytoplasmic membrane ofEscherichia coli

1 reference

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1 reference

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1 reference

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Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins

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.

1 reference

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Interaction between maltose-binding protein and the membrane-associated maltose transporter complex in Escherichia coli

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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Identifiers

10.1128/JB.177.24.7186-7193.1995

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

15 September 2017

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