(Q28904965)

7 March 2017

title

The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen (English)

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7 March 2017

main subject

Staphylococcus aureus

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E. R. Wann

1

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7 March 2017

S. Gurusiddappa

series ordinal

2

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7 March 2017

M. Hook

series ordinal

3

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7 March 2017

language of work or name

English

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publication date

5 May 2000

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Journal of Biological Chemistry

7 March 2017

published in

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7 March 2017

volume

275

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7 March 2017

issue

18

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7 March 2017

page(s)

13863–13871

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MSCRAMM-mediated adherence of microorganisms to host tissues.

7 March 2017

cites work

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Staphylococcus aureus expresses a major histocompatibility complex class II analog

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Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides

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Two different genes encode fibronectin binding proteins in Staphylococcus aureus. The complete nucleotide sequence and characterization of the second gene

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Structure of the cell wall anchor of surface proteins in Staphylococcus aureus

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Ace is a collagen-binding MSCRAMM from Enterococcus faecalis

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Protein F, a fibronectin-binding protein of Streptococcus pyogenes, also binds human fibrinogen: isolation of the protein and mapping of the binding region

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Protein F, a fibronectin-binding protein, is an adhesin of the group A streptococcus Streptococcus pyogenes

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Fibronectin-binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin alpha5beta1.

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