Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1 1 1Edited by P. E. Wright

This publication has 31 references indexed in Scilit:

• NMR of modular proteins
  Nature Structural & Molecular Biology, 1998
• Essential spaces defined by NMR structure ensembles and molecular dynamics simulation show significant overlap
  Proteins-Structure Function and Bioinformatics, 1998
• Solution Structure of the Epidermal Growth Factor (EGF)-like Module of Human Complement Protease C1r, an Atypical Member of the EGF Family
  Biochemistry, 1998
• Determining the structures of large proteins and protein complexes by NMR
  Trends in Biotechnology, 1998
• X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B.
  Proceedings of the National Academy of Sciences, 1995
• Antibodies inhibit the protease-mediated processing of a malaria merozoite surface protein.
  The Journal of Experimental Medicine, 1994
• Backbone dynamics of calmodulin studied by nitrogen-15 relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible
  Biochemistry, 1992
• Secondary processing of the Plasmodium falciparum merozoite surface protein-1 (MSP1) by a calcium-dependent membrane-bound serine protease: shedding of MSP133 as a noncovalently associated complex with other fragments of the MSP1
  Molecular and Biochemical Parasitology, 1992
• Proteolytic processing of thePlasmodium falciparum merozoite surface protein-1 produces a membrane-bound fragment containing two epidermal growth factor-like domains
  Molecular and Biochemical Parasitology, 1991
• A single fragment of a malaria merozoite surface protein remains on the parasite during red cell invasion and is the target of invasion-inhibiting antibodies.
  The Journal of Experimental Medicine, 1990