Structural Basis of Toll-Like Receptor 3 Signaling with Double-Stranded RNA
To establish the molecular basis for ligand binding and signaling, the crystal structure of a complex between two mouse TLR3-ECDs and dsRNA is determined at 3.4 angstrom resolution.
Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae.
- T. Tsukiyama, J. Palmer, C. Landel, J. Shiloach, C. Wu
- BiologyGenes & Development
- 15 March 1999
It is demonstrated that the ATP-dependent chromatin-remodeling activities are essential for the in vivo functions of both ISW1 and ISW2 complexes.
Structure of the agonist-bound neurotensin receptor
- J. White, N. Noinaj, R. Grisshammer
- 13 September 2012
These findings provide the first insight into the binding mode of a peptide agonist to a GPCR and may support the development of non-peptide ligands that could be useful in the treatment of neurological disorders, cancer and obesity.
Growing E. coli to high cell density--a historical perspective on method development.
- J. Shiloach, R. Fass
- Biology, EngineeringBiotechnology Advances
- 1 July 2005
The molecular structure of the Toll-like receptor 3 ligand-binding domain.
The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors, including insertions in the LRRs and 11 N-linked glycans.
The efficacy of a Salmonella typhi Vi conjugate vaccine in two-to-five-year-old children.
The antibody responses and the efficacy suggest that the Vi-rEPA conjugate typhoid vaccine should be at least as protective in persons who are more than five years old.
CtIP maintains stability at common fragile sites and inverted repeats by end resection-independent endonuclease activity.
- Hailong Wang, Yongjiang Li, Xiaohua Wu
- BiologyMolecules and Cells
- 19 June 2014
Structures of the Multidrug Transporter P-glycoprotein Reveal Asymmetric ATP Binding and the Mechanism of Polyspecificity*♦
The linker-shortened mutant P-gp possesses basal ATPase activity and binds ATP only in its N-terminal nucleotide-binding domain, providing a mechanistic explanation for the polyspecificity of P- gp in substrate interactions.
Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction
- J. White, J. Grodnitzky, R. Grisshammer
- Biology, ChemistryProceedings of the National Academy of Sciences
- 17 July 2007
It is demonstrated by pharmacological and hydrodynamic experiments that purified neurotensin receptor NTS1, a class A GPCR, dimerizes in detergent solution in a concentration-dependent manner, with an apparent affinity in the low nanomolar range.
Modified Escherichia coli B (BL21), a superior producer of plasmid DNA compared with Escherichia coli K (DH5alpha).
- J. Phue, S. J. Lee, L. Trinh, J. Shiloach
- Biology, EngineeringBiotechnology and Bioengineering
- 1 November 2008
The produced plasmid, which was constructed for HIV clinical study, was found to have identical properties to the plasmids currently produced by E. coli DH5alpha, and production values, reaching 2 g/L were obtained using glucose as a carbon source.