S. Bagby

Publication List Details

Period

2001 - 2008

Number

30

Co-Authors

S. aureus IgG-binding proteins SpA and Sbi: Host speciticity and mechanisms of immune complex formation (2008)

Atkins, K. L., Burman, J. D., Chamberlain, E. S., Cooper, J. E., Poutrel, B., Bagby, S., ...

The evasion of the host immune response is central to the pathogenicity of Staphylococcus aureus, and is facilitated by the ability of the cell wall-associated protein A (SpA) to bind immunoglobulin...

Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens.

Bagby, S, Harvey, T S, Eagle, S G, Inouye, S, Ikura, M

The solution structure of Ca(2+)-loaded protein S (M(r) 18,792) from the Gram-negative soil bacterium Myxococcus xanthus has been determined by multidimensional heteronuclear NMR spectroscopy....

Subunit interactions change the heme active-site geometry in p-cresol methylhydroxylase.

McLendon, G L, Bagby, S, Charman, J A, Driscoll, P C, McIntire, W S, Mathews, F S, ...

The enzyme p-cresol methylhydroxylase [4-cresol: (acceptor) oxidoreductase (methyl-hydroxylating), EC 1.17.99.1] contains two subunits: a cytochrome c (electron transfer) subunit (cytochrome cpc) and...

Direct electrochemistry of two genetically distinct flavodoxins isolated from Azotobacter chroococcum grown under nitrogen-fixing conditions.

Bagby, S, Barker, P D, Hill, H A, Sanghera, G S, Dunbar, B, Ashby, G A, ...

Two genetically distinct flavodoxins, designated AcFldA and AcFldB, were isolated from Azotobacter chroococcum (MCD1155) grown under nitrogen-fixing conditions. AcFldA and AcFldB differ in their...

Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens.

Bagby, S, Harvey, T S, Eagle, S G, Inouye, S, Ikura, M

The solution structure of Ca(2+)-loaded protein S (M(r) 18,792) from the Gram-negative soil bacterium Myxococcus xanthus has been determined by multidimensional heteronuclear NMR spectroscopy....

Subunit interactions change the heme active-site geometry in p-cresol methylhydroxylase.

McLendon, G L, Bagby, S, Charman, J A, Driscoll, P C, McIntire, W S, Mathews, F S, ...

The enzyme p-cresol methylhydroxylase [4-cresol: (acceptor) oxidoreductase (methyl-hydroxylating), EC 1.17.99.1] contains two subunits: a cytochrome c (electron transfer) subunit (cytochrome cpc) and...

Direct electrochemistry of two genetically distinct flavodoxins isolated from Azotobacter chroococcum grown under nitrogen-fixing conditions.

Bagby, S, Barker, P D, Hill, H A, Sanghera, G S, Dunbar, B, Ashby, G A, ...

Two genetically distinct flavodoxins, designated AcFldA and AcFldB, were isolated from Azotobacter chroococcum (MCD1155) grown under nitrogen-fixing conditions. AcFldA and AcFldB differ in their...