Crystal structure of a complex between anthrax toxin and its host cell receptor
- 4 July 2004
- journal article
- Published by Springer Nature in Nature
- Vol. 430 (7002) , 905-908
- https://doi.org/10.1038/nature02763
Abstract
Nature is the international weekly journal of science: a magazine style journal that publishes full-length research papers in all disciplines of science, as well as News and Views, reviews, news, features, commentaries, web focuses and more, covering all branches of science and how science impacts upon all aspects of society and life.Keywords
This publication has 31 references indexed in Scilit:
- TEM8 Interacts with the Cleaved C5 Domain of Collagen α3(VI)Cancer Research, 2004
- Binding of Anthrax Toxin to Its Receptor Is Similar to α Integrin-Ligand InteractionsJournal of Biological Chemistry, 2003
- Anthrax toxin: structures, functions and tumour targetingExpert Opinion on Biological Therapy, 2003
- Structures of the αL I Domain and Its Complex with ICAM-1 Reveal a Shape-Shifting Pathway for Integrin RegulationPublished by Elsevier ,2003
- ARP⧸wARP and Automatic Interpretation of Protein Electron Density MapsPublished by Elsevier ,2003
- Anthrax toxin: structures, functions and tumour targetingExpert Opinion on Biological Therapy, 2003
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Reduced surface: An efficient way to compute molecular surfacesBiopolymers, 1996
- Reduced surface: An efficient way to compute molecular surfacesBiopolymers, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994