Zobrazeno 1 - 10 of 14 pro vyhledávání: '"S. L. Primo-Parmo"'
1
On the physiological role(s) of the paraoxonases
Autor: Robert C. Sorenson, Bert N. La Du, S. L. Primo-Parmo, Theodore J. Standiford, Scott S. Billecke, Mohamad Navab, Michael Aviram
Publikováno v: Chemico-Biological Interactions. :379-388
In recent years several lines of evidence have indicated that serum paraoxonase (PON1), and perhaps other mammalian paraoxonases, act as important guardians against cellular damage from toxic agents, such as organophosphates, oxidized lipids in the p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a35e372792cedcd3e2ce48798f0924c
https://doi.org/10.1016/s0009-2797(99)00049-6
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2
Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase
Autor: S. L. Primo-Parmo, Michael Aviram, Charles L. Bisgaier, Mira Rosenblat, Roger S. Newton, B N La Du
Publikováno v: Journal of Clinical Investigation. 101:1581-1590
HDL levels are inversely related to the risk of developing atherosclerosis. In serum, paraoxonase (PON) is associated with HDL, and was shown to inhibit LDL oxidation. Whether PON also protects HDL from oxidation is un- known, and was determined in t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d60b744e25a7963815f608a90fda74e
https://doi.org/10.1172/jci1649
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3
Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase
Autor: H Lightstone, S. L. Primo-Parmo, B N La Du
Publikováno v: Pharmacogenetics. 7:27-34
An unstable variant of human butyrylcholinesterase (BChE) is described in four apparently unrelated individuals sensitive to succinylcholine. Sequencing of genomic DNA revealed a single nucleotide substitution which results in the replacement of amin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b86ca54e0504e7ea49f92e3da7f18b60
https://doi.org/10.1097/00008571-199702000-00004
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4
Characterization of a soluble mouse liver enzyme capable of hydrolyzing diisopropyl phosphorofluoridate
Autor: J.A. Doorn, S. L. Primo-Parmo, C.S. Dunlop, Scott S. Billecke, Clarence A. Broomfield, B N La Du
Publikováno v: Chemico-biological interactions.
A novel mouse liver soluble fraction DFPase which has organophosphatase activities with sarin, soman and tabun, was purified and characterized. However, it lacks paraoxonase and arylesterase activities with paraoxon and phenyl acetate, respectively.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a28ce35aa25ba3cae4eafa6e25d8f16
https://pubmed.ncbi.nlm.nih.gov/10421459
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5
The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family
Autor: S. L. Primo-Parmo, John F. Teiber, Robert C. Sorenson, Bert N. La Du
Publikováno v: Genomics. 33(3)
A physiological role for paraoxonase (PON1) is still uncertain, but it catalyzes the hydrolysis of toxic organophosphates. Evidence that the human genome contains two PON1-like genes, designated PON2 and PON3, is presented here. Human PON1 and PON2 e
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6933bb72dc91360c6f459df2a0379ed1
https://pubmed.ncbi.nlm.nih.gov/8661009
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6
Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene
Autor: S L, Primo-Parmo, C F, Bartels, B, Wiersema, A F, van der Spek, J W, Innis, B N, La Du
Publikováno v: American journal of human genetics. 58(1)
The silent phenotype of human butyrylcholinesterase (BChE), present in most human populations in frequencies of approximately 1/100,000, is characterized by the complete absence of BChE activity or by activity
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c122df4760b610d627fe14cc51547c2b
https://pubmed.ncbi.nlm.nih.gov/8554068
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7
The genetic mapping and gene structure of mouse paraoxonase/arylesterase
Autor: S. L. Primo-Parmo, Robert C. Sorenson, Sally A. Camper, Bert N. La Du
Publikováno v: Genomics. 30(3)
The physiological role of mammalian paraoxonase/arylesterase is unknown. However, paraoxonase is an HDL-associated protein, and recent studies indicate that it may have anti-atherogenic functions. We describe the chromosomal localization and structur
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ed916490ffbedf924ab79b93ad5c364
https://pubmed.ncbi.nlm.nih.gov/8825627
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8
Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase
Autor: Oksana Lockridge, B N La Du, Robert C. Sorenson, Steve Adkins, S. L. Primo-Parmo, Chung-Liang Kuo
For three decades, mammalian paraoxonase (A-esterase, aromatic esterase, arylesterase; PON, EC 3.1.8.1) has been thought to be a cysteine esterase demonstrating structural and mechanistic homologies with the serine esterases (cholinesterases and carb
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6c274cfb648b5a1b13b5e1c849983e5
https://europepmc.org/articles/PMC41304/
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10
An improved method for butyrylcholinesterase phenotyping
Autor: Eleidi A. Chautard-Freire-Maia, Muriel M. Vieira, Geraldo Picheth, S. L. Primo-Parmo, Cyntia M.T. Fadel-Picheth
Publikováno v: Biochemical genetics. 32(3-4)
An improved method for the identification of butyrylcholinesterase phenotypes is proposed. It is based on modifications of a method that uses alpha-naphthyl acetate as substrate and DL-propranolol and Ro2-0683 as inhibitors. The proposed modification
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57d1789467f1756068001533bdabf4f5
https://pubmed.ncbi.nlm.nih.gov/7980387
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