Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin
Open Access
- 1 December 1998
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 169 (1), 171-177
- https://doi.org/10.1111/j.1574-6968.1998.tb13314.x
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Biochemical evidence for a conserved interaction between bacterial transferrin binding protein A and transferrin binding protein BMicrobial Pathogenesis, 1998
- Characterization of thePasteurella haemolyticatransferrin receptor genes and the recombinant receptor proteinsMicrobial Pathogenesis, 1997
- Bacterial transferrin and lactoferrin receptorsTrends in Microbiology, 1996
- Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteinsJournal of Bacteriology, 1996
- Cholera Toxin Binding Affinity and Specificity for Gangliosides Determined by Surface Plasmon ResonanceBiochemistry, 1996
- Production of Lipidated Meningococcal Transferrin Binding Protein 2 in Escherichia coliProtein Expression and Purification, 1995
- Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrinJournal of Bacteriology, 1994
- Structure, function and flexibility of human lactoferrinInternational Journal of Biological Macromolecules, 1991
- Identification and characterization of the transferrin receptor from Neisseria meningitidisMolecular Microbiology, 1988
- Binding of apotransferrin to K562 cells: explanation of the transferrin cycle.Proceedings of the National Academy of Sciences, 1983