The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia (Q27641813)

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6 November 2019

title

The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia (English)

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6 November 2019

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1 reference

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Benita Westerlund-Wikström

4

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6 November 2019

Adrian Goldman

6

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6 November 2019

author name string

Michael C Merckel

1

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6 November 2019

Jarna Tanskanen

2

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6 November 2019

Sanna Edelman

3

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6 November 2019

Timo K Korhonen

5

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6 November 2019

language of work or name

English

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publication date

1 August 2003

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Journal of Molecular Biology

6 November 2019

published in

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6 November 2019

volume

331

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6 November 2019

issue

4

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6 November 2019

page(s)

897-905

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Diarrheagenic Escherichia coli

6 November 2019

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The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine

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The gaf fimbrial gene cluster of Escherichia coli expresses a full-size and a truncated soluble adhesin protein

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X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli

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Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection

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The PapG protein is the alpha-D-galactopyranosyl-(1----4)-beta-D-galactopyranose-binding adhesin of uropathogenic Escherichia coli

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The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus

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Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor

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The solution structure of PapGII from uropathogenic Escherichia coli and its recognition of glycolipid receptors.

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Mechanism of N-acetylgalactosamine binding to a C-type animal lectin carbohydrate-recognition domain

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Characterization of glycoprotein glycan receptors for Escherichia coli F17 fimbrial lectin.

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Functions of cell surface heparan sulfate proteoglycans

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Mutational analysis of receptor binding mediated by the Dr family of Escherichia coli adhesins.

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How to measure and predict the molar absorption coefficient of a protein

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Modified Phased Translation Functions and their Application to Molecular-Fragment Location

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0022-2836(03)00841-6

2 references

Consolidated OpenCitations Corpus – April 2017

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12909017%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

1 reference

Consolidated OpenCitations Corpus – April 2017

2 references

Consolidated OpenCitations Corpus – April 2017