Bert N. La Du

Hebei Normal University of Science and Technology

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Oksana Lockridge

University of Nebraska Medical Center

Vincent G. Zannoni

University of Michigan–Ann Arbor

Cynthia F. Bartels

Case Western Reserve University

Scott S. Billecke

Beaumont Health

S.L. Primo-Parmo

University of Michigan–Ann Arbor

H W Eckerson

University of Utah

Dragomir Draganov

Roche (Switzerland)

Robert C. Sorenson

University of Michigan–Ann Arbor

George A. Jacoby

Lahey Medical Center

J. Edwin Seegmiller

Institute on Aging

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University of Michigan–Ann Arbor

National Institutes of Health

University of California, Los Angeles

New York University

The University of Texas Southwestern Medical Center

University of Washington

Karolinska Institutet

Harvard University

University of British Columbia

Rutgers, The State University of New Jersey

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Characterization of a soluble mouse liver enzyme capable of hydrolyzing diisopropyl phosphorofluoridate

Chemico-Biological Interactions (1999)

Scott S. Billecke S.L. Primo-Parmo Cristina S. Dunlop Jonathan A. Doorn Bert N. La Du

Paraoxon

Arylesterase

Homology

10.1016/s0009-2797(99)00034-4

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Citations (38)

The effect of coenzyme Q10 on tyrosine metabolism in guinea pigs

Biochemical and Biophysical Research Communications (1962)

Vincent G. Zannoni George A. Jacoby Bert N. La Du

Electron acceptor

Muconic acid

Dioxygenase

Catechol

10.1016/0006-291x(62)90178-x

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Citations (7)

Nanoscale drug formulations for the treatment of Alzheimer's disease progression

RSC Advances (2025)

Liu Liqin Haini He Bert N. La Du Yang He

Alzheimer's disease (AD) is a devastating neurodegenerative disorder with no effective disease-modifying treatments.

10.1039/d4ra08128e

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Is Paraoxonase-3 Another HDL-Associated Protein Protective Against Atherosclerosis?

Arteriosclerosis Thrombosis and Vascular Biology (2001)

Bert N. La Du

Arteriosclerosis, Thrombosis, and Vascular Biology is the first report of expression of human paraoxonase-3 (PON3) and its ability to prevent the formation of mildly oxidized LDL and also to inactivate preformed mildly oxidized LDL.

Paraoxonase

Aryldialkylphosphatase

10.1161/01.atv.21.4.467

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Citations (20)

THE TYROSINE OXIDATION SYSTEM OF LIVER

Journal of Biological Chemistry (1951)

Bert N. La Du David M. Greenberg

10.1016/s0021-9258(18)56066-x

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Citations (66)

The enzymatic defect in histidinemia

Biochemical and Biophysical Research Communications (1962)

Bert N. La Du R. Rodney Howell George A. Jacoby J. Edwin Seegmiller Vincent G. Zannoni

Heterologous expression

Heterologous

10.1016/0006-291x(62)90323-6

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Citations (66)

Multiple Substrates for Paraoxonase-1 during Oxidation of Phosphatidylcholine by Peroxynitrite

Biochemical and Biophysical Research Communications (2002)

Zakaria Ahmed Amir Ravandi Graham F. Maguire Andrew Emili Dragomir Draganov

Lysophosphatidylcholine

Paraoxonase

Phosphocholine

10.1006/bbrc.2001.6150

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Citations (86)

Ascorbic Acid and the Oxidation of Tyrosine

Science (1953)

Bert N. La Du David M. Greenberg

Oxidation reduction

10.1126/science.117.3031.111

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Citations (43)

Molecular biology of human serum cholinesterase.

PubMed (1986)

Bert N. La Du Oksana Lockridge

More than 90% of the amino acid sequence of purified human serum cholinesterase has been determined in our laboratory. Purified enzyme was digested with several proteolytic enzymes; the resulting polypeptides were then separated, purified, and sequenced. Optimal sequence regions were identified and used as the basis for the synthesis of three 17-mer oligonucleotide probes. In addition, one long peptide of 58 amino acid residues was selected for construction of two unique sequence oligonucleotide probes of 39-mer and 53-mer; the peptide regions corresponding to the latter are six amino acids apart. The probes have been used to screen a human liver cDNA library and a human genomic library. Several positive clones to both types of probes have been identified. These are being characterized, and some of them have been or are now being sequenced. A high degree of homology in the amino acid sequence of the active center of human serum cholinesterase and that of acetylcholinesterase from the Torpedo fish has been noted. It appears that this region of cholinesterases has been conserved during evolution, and there may be an important, still unrecognized role for serum nonspecific cholinesterase in mammalian metabolism.

Cholinesterase

Sequence (biology)

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PROPERTIES OF PLASMA CHOLINESTERASE VARIANTS

Annals of the New York Academy of Sciences (1968)

Sandra W. Clark George Glaubiger Bert N. La Du

Annals

10.1111/j.1749-6632.1968.tb48253.x

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Citations (19)