Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation (Q35434247)

8 August 2017

title

Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation (English)

1 reference

8 August 2017

0 references

1 reference

Yi Ding

1

1 reference

8 August 2017

L Miya Fujimoto

series ordinal

2

1 reference

8 August 2017

Yong Yao

series ordinal

3

1 reference

8 August 2017

Francesca M Marassi

series ordinal

4

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8 August 2017

language of work or name

1 reference

13 January 2015

1 reference

Journal of Biomolecular NMR

8 August 2017

published in

1 reference

8 August 2017

volume

61

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8 August 2017

issue

3-4

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8 August 2017

page(s)

275-286

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Influence of the lipid membrane environment on structure and activity of the outer membrane protein Ail from Yersinia pestis

8 August 2017

cites work

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Ail proteins of Yersinia pestis and Y. pseudotuberculosis have different cell binding and invasion activities

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Ail protein binds ninth type III fibronectin repeat (9FNIII) within central 120-kDa region of fibronectin to facilitate cell binding by Yersinia pestis

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Ail binding to fibronectin facilitates Yersinia pestis binding to host cells and Yop delivery

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https://pubmed.ncbi.nlm.nih.gov/25578899

12 December 2020

10.1007/S10858-014-9893-4

Identifiers

DOI

1 reference

8 August 2017

1 reference

8 August 2017

1 reference