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Identification of an interaction between residue 6 of the natural peptide ligand and a distinct residue within the amino-terminal tail of the secretin receptor.
Dong M, Wang Y, Hadac EM, Pinon DI, Holicky E, Miller LJ. Dong M, et al. Among authors: wang y. J Biol Chem. 1999 Jul 2;274(27):19161-7. doi: 10.1074/jbc.274.27.19161. J Biol Chem. 1999. PMID: 10383421 Free article.
We recently used this technique to demonstrate the proximity between a residue within the carboxyl-terminal half of a secretin-like ligand and the amino-terminal domain of the secretin receptor (Dong, M., Wang, Y., Pinon, D. I., Hadac, E. M., and Miller, L. J. (1999 …
We recently used this technique to demonstrate the proximity between a residue within the carboxyl-terminal half of a secretin-like ligand a …
Escherichia coli transcription termination factor rho. II. Binding of oligonucleotide cofactors.
Wang Y, von Hippel PH. Wang Y, et al. J Biol Chem. 1993 Jul 5;268(19):13947-55. J Biol Chem. 1993. PMID: 8314761 Free article.
The relative binding affinities for rho of the oligonucleotide rho ATPase cofactors studied in the accompanying paper (Wang, Y., and von Hippel, P. H. (1993) J. Biol. Chem. 268, 13940-13946) have been determined by gel mobility shift and ultrafiltration binding anal …
The relative binding affinities for rho of the oligonucleotide rho ATPase cofactors studied in the accompanying paper (Wang, Y
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