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Properties of the retained N-terminal hydrophobic leader sequence in human serum paraoxonase/arylesterase.
Sorenson RC, Aviram M, Bisgaier CL, Billecke S, Hsu C, La Du BN. Sorenson RC, et al. Among authors: la du bn. Chem Biol Interact. 1999 May 14;119-120:243-9. doi: 10.1016/s0009-2797(99)00033-2. Chem Biol Interact. 1999. PMID: 10421458
Location of disulfide bonds within the sequence of human serum cholinesterase.
Lockridge O, Adkins S, La Du BN. Lockridge O, et al. Among authors: la du bn. J Biol Chem. 1987 Sep 25;262(27):12945-52. J Biol Chem. 1987. PMID: 3115973
Apolipoprotein A-I promotes the formation of phosphatidylcholine core aldehydes that are hydrolyzed by paraoxonase (PON-1) during high density lipoprotein oxidation with a peroxynitrite donor.
Ahmed Z, Ravandi A, Maguire GF, Emili A, Draganov D, La Du BN, Kuksis A, Connelly PW. Ahmed Z, et al. Among authors: la du bn. J Biol Chem. 2001 Jul 6;276(27):24473-81. doi: 10.1074/jbc.M010459200. Epub 2001 Apr 24. J Biol Chem. 2001. PMID: 11320081
Baculovirus-mediated expression and purification of human serum paraoxonase 1A.
Brushia RJ, Forte TM, Oda MN, La Du BN, Bielicki JK. Brushia RJ, et al. Among authors: la du bn. J Lipid Res. 2001 Jun;42(6):951-8. J Lipid Res. 2001. PMID: 11369803
Paraoxonase active site required for protection against LDL oxidation involves its free sulfhydryl group and is different from that required for its arylesterase/paraoxonase activities: selective action of human paraoxonase allozymes Q and R.
Aviram M, Billecke S, Sorenson R, Bisgaier C, Newton R, Rosenblat M, Erogul J, Hsu C, Dunlop C, La Du B. Aviram M, et al. Arterioscler Thromb Vasc Biol. 1998 Oct;18(10):1617-24. doi: 10.1161/01.atv.18.10.1617. Arterioscler Thromb Vasc Biol. 1998. PMID: 9763535
Human serum paraoxonase (PON 1) is inactivated by oxidized low density lipoprotein and preserved by antioxidants.
Aviram M, Rosenblat M, Billecke S, Erogul J, Sorenson R, Bisgaier CL, Newton RS, La Du B. Aviram M, et al. Free Radic Biol Med. 1999 Apr;26(7-8):892-904. doi: 10.1016/s0891-5849(98)00272-x. Free Radic Biol Med. 1999. PMID: 10232833
Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities.
Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN. Draganov DI, et al. Among authors: la du bn. J Lipid Res. 2005 Jun;46(6):1239-47. doi: 10.1194/jlr.M400511-JLR200. Epub 2005 Mar 16. J Lipid Res. 2005. PMID: 15772423 Free article.
Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3.
Teiber JF, Draganov DI, La Du BN. Teiber JF, et al. Among authors: la du bn. Biochem Pharmacol. 2003 Sep 15;66(6):887-96. doi: 10.1016/s0006-2952(03)00401-5. Biochem Pharmacol. 2003. PMID: 12963475
Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH.
Teiber JF, Draganov DI, La Du BN. Teiber JF, et al. Among authors: la du bn. J Lipid Res. 2004 Dec;45(12):2260-8. doi: 10.1194/jlr.M400213-JLR200. Epub 2004 Sep 1. J Lipid Res. 2004. PMID: 15342686 Free article.
Studies on human serum paraoxonase/arylesterase.
La Du BN, Adkins S, Kuo CL, Lipsig D. La Du BN, et al. Chem Biol Interact. 1993 Jun;87(1-3):25-34. doi: 10.1016/0009-2797(93)90022-q. Chem Biol Interact. 1993. PMID: 8393742
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