In the above article [de Kruijf P, van Heteren J, Lim HD, Conti PGM, van der Lee MMC, Bosch L, Ho K-K, Auld D, Ohlmeyer M, Smit MJ, Wijkmans JCHM, Zaman GJR, Smit MJ, and Leurs R (2009) J Pharmacol Exp Ther 329:783–790], several text corrections were not incorporated at final stages of production. The corrections appear below.
On page 783, affiliation line, Martine J.S. is affiliated with Leiden/Amsterdam Center for Drug Research, Division of Medicinal Chemistry, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands, and Martin J.S. is affiliated with Schering-Plough Research Institute, Oss, The Netherlands.
On page 784, right column, under Materials and Methods, line 26, the citation of Goldman et al., 1996 should be moved from “pcDNA3-hCXCR1 cDNA” and placed after “pcDNA3-hCXCR2 cDNA” (line 25).
On page 785, right column, the last sentence beginning “Bound radioactivity...” should read “Bound radioactivity was determined using a Tri-Carb 1900 Hewlett Packard counter (PerkinElmer Life and Analytical Sciences) or a Micro-Beta counter (PerkinElmer Life and Analytical Sciences).
On page 785, legend to Fig. 1, “... compound 1, compound 2, and compound 3 belong to the thiazolpyrimidine class.” should read “... compound 1, compound 2, and compound 3 belong to the imidazolylpyrimidine class.”
On page 787, legend to Fig. 3, sentence beginning “Data of triplicate determinations...” should read “Data of triplicate determinations from a representative experiment (n = 3–6) are expressed as the percentage of β-galactosidase activity in response to 7.6 nM CXCL8 ± S.E.M. (A). Relationship between the pKi values as determined in 125I-CXCL8 binding assay and the antagonistic potency as determined in the β-arrestin2 recruitment assay is shown (r2 = 0.73) (B).
On page 788, legend to Fig. 5, the square brackets enclosing 125I-CXCL8 should be removed (twice total).
On page 789, right column, line 2, the sentence beginning “Hence, of the CXCR2 antagonists...” should read “Hence, all the CXCR2 antagonists of the different chemical classes tested in this study displace and antagonize CXCL8, most probably via a noncompetitive, allosteric mechanism.”
The online version has been corrected in departure from the print version.
The printer regrets these errors and apologizes for any confusion or inconvenience they may have caused.
- The American Society for Pharmacology and Experimental Therapeutics