Structure of the InlB Leucine-Rich Repeats, a Domain that Triggers Host Cell Invasion by the Bacterial Pathogen L. monocytogenes
- 1 December 1999
- journal article
- Published by Elsevier in Molecular Cell
- Vol. 4 (6) , 1063-1072
- https://doi.org/10.1016/s1097-2765(00)80234-8
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Crystallography & NMR System: A New Software Suite for Macromolecular Structure DeterminationActa Crystallographica Section D-Biological Crystallography, 1998
- Interactions of Listeria monocytogenes with mammalian cells during entry and actin-based movement: bacterial factors, cellular ligands and signalingThe EMBO Journal, 1998
- The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cellsMolecular Microbiology, 1998
- [27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methodsPublished by Elsevier ,1997
- Identification and characterization of a novel PrfA-regulated gene in Listeria monocytogenes whose product, IrpA, is highly homologous to internalin proteins, which contain leucine-rich repeatsInfection and Immunity, 1997
- Phosphoinositide kinasesCurrent Opinion in Cell Biology, 1996
- Entry of Listeria monocytogenes into hepatocytes requires expression of InIB, a surface protein of the internalin multigene familyMolecular Microbiology, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Calmodulin structure refined at 1.7 Å resolutionJournal of Molecular Biology, 1992
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992