scholarly article | Q13442814 |
P6179 | Dimensions Publication ID | 1014996622 |
P356 | DOI | 10.1023/A:1025880932197 |
P2888 | exact match | https://scigraph.springernature.com/pub.10.1023/a:1025880932197 |
P698 | PubMed publication ID | 14512737 |
P50 | author | Ramón Campos-Olivas | Q53513935 |
P2093 | author name string | Smita Mohanty | |
Sergey Zubkov | |||
P2860 | cites work | Sexual attraction in the silkworm moth: structure of the pheromone-binding-protein-bombykol complex | Q27621246 |
NMR structure reveals intramolecular regulation mechanism for pheromone binding and release | Q27636458 | ||
NMR structure of the unliganded Bombyx mori pheromone-binding protein at physiological pH | Q27639915 | ||
NMRPipe: a multidimensional spectral processing system based on UNIX pipes | Q27860859 | ||
NMR View: A computer program for the visualization and analysis of NMR data | Q27860951 | ||
Protein structure encodes the ligand binding specificity in pheromone binding proteins | Q30417419 | ||
Bacterial expression and photoaffinity labeling of a pheromone binding protein | Q36277971 | ||
NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori | Q36282032 | ||
NMR assignment of the A form of the pheromone-binding protein of Bombyx mori. | Q52586673 | ||
P433 | issue | 4 | |
P921 | main subject | Antheraea polyphemus | Q1758845 |
P304 | page(s) | 393-394 | |
P577 | publication date | 2003-12-01 | |
P1433 | published in | Journal of Biomolecular NMR | Q3186900 |
P1476 | title | 1H, 13C and 15N backbone assignments of the pheromone binding protein from the silk moth Antheraea polyphemus (ApolPBP). | |
P478 | volume | 27 |
Q52666391 | Disulfide connectivity and reduction in pheromone-binding proteins of the gypsy moth, Lymantria dispar. |
Q30873700 | Ligand binding turns moth pheromone-binding protein into a pH sensor: effect on the Antheraea polyphemus PBP1 conformation |
Q34384098 | Structural and functional difference of pheromone binding proteins in discriminating chemicals in the gypsy moth, Lymantria dispar |
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