Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
By Z. Böcskei, Colin R. Groom, Darren R. Flower, C. Wright, S. Phillips, A. Cavaggioni, J. Findlay, A. North. 1992
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- Jane Hurst
- R. Beynon
- M. Redaelli
- C. Mucignat-Caretta
- A. Cavaggioni
- Scott D. Sharrow
- E. Ferrari
- M. Novotny
Citations in the corpus
- Development and validation of a genetic algorithm for flexible docking. (1997, unknown): “, 1993), 1MUP (BoÈcskei et al., 1992), 3CLA (Leslie, 1990) and 2R07 (Badger et al.”
- Polymorphism in Major Urinary Proteins: Molecular Heterogeneity in a Wild Mouse Population (2002, methodology): “PDB (Bocskei et al., 1992)] was used to generate these views of the protein.”
- Differential binding between volatile ligands and major urinary proteins due to genetic variation in mice. (2012, unknown): “Although the chemical properties of VOCs and MUPs are different, they appear to interact closely since MUPs, a member of the lipocalin family, have a hydrophobic pocket that sequesters some volatile ligands [6].”
- Mice recognize recent urine scent marks by the molecular composition. (2008, unknown): “Key words: behavior, mouse, olfaction, scent, time”
- Odorant binding and conformational changes of a rat odorant-binding protein. (2004, background): “…c 1 [PDB code 1EW3 (Lascombe et al., 2000)] and bovine Bos d 2 [PDB code 1BJ7 (Rouvinen et al., 1999)] allergens, mouse major urinary protein [PDB code 1MUP (Bocskei et al., 1992)], porcine OBP [PDB code 1A3Y (Spinelli et al., 1998)] and hamster aphrodisin [PDB code 1E5P (Vincent et al., 2001)].”
- 3D domain swapping: As domains continue to swap (2002, background): “Major urinary protein monomer (Bocskei et al. 1992) 1MUP 166 126–130 Rodent pheromone transporter”
- Pheromone binding by polymorphic mouse major urinary proteins (2002, background): “X-ray structures of MUPs isolated from urine (Bocskei et al. 1992) and liver (Timm et al.”
- Ligands of Urinary Lipocalins from the Mouse: Uptake of Environmentally Derived Chemicals (1998, background): “Natural ligands bound to MUPs.”
- Major Urinary Proteins on Nanodiamond-Based Resonators Toward Artificial Olfaction (2016, background): “MUPs are ligand binding proteins (LBP) excreted in mice urine [9].”
- The X-ray structure of a recombinant major urinary protein at 1.75 A resolution. A comparative study of X-ray and NMR-derived structures. (2001, methodology): “Three distinct families of pheromone receptors were identi®ed in the VNO (Ryba & Tirindelli, 1997; Krieger et al., 1999; Martini et al., 2001), namely the V1R and V3R families speci®c for small hydrophobic molecules and the V2R family activated by pheromones of proteic nature.”