Zobrazeno 1 - 10 of 49 pro vyhledávání: '"D L, Vander Jagt"'
1
Selective Inhibitors of Human Lactate Dehydrogenases and Lactate Dehydrogenase from the Malarial Parasite Plasmodium falciparum
Autor: M T Makler, Lorraine M. Deck, Brian B. Chamblee, Robert C. Piper, Lucy A. Hunsaker, Jose E. Torres, V M Hernandez, Robert E. Royer, R R Malone, D L Vander Jagt
Publikováno v: Journal of Medicinal Chemistry. 41:3879-3887
Derivatives of the sesquiterpene 8-deoxyhemigossylic acid (2, 3-dihydroxy-6-methyl-4-(1-methylethyl)-1-naphthoic acid) were synthesized that contained altered alkyl groups in the 4-position and contained alkyl or aralkyl groups in the 7-position. The
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::700d8ffe950b15cc3a138873f4a53d0b
https://doi.org/10.1021/jm980334n
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2
Glyoxalase II: Molecular characteristics, kinetics and mechanism
Autor: D L Vander Jagt
Publikováno v: Biochemical Society Transactions. 21:522-527
The mechanism that has been proposed for glyoxalase II [36] is summarized in Figure 3. It involves direct nucleophilic attack of an active-site histidine on the thiol ester substrate to form an acyl-imidazole intermediate which then rapidly hydrolyse
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e5cacef658ff5366ac9e958dcccdd6
https://doi.org/10.1042/bst0210522
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4
Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications
Autor: B Robinson, D L Vander Jagt, K K Taylor, Lucy A. Hunsaker
Publikováno v: Journal of Biological Chemistry. 267:4364-4369
The substrate specificities of human aldose reductase and aldehyde reductase toward trioses, triose phosphates, and related three-carbon aldehydes and ketones were evaluated. Both enzymes are able to catalyze the NADPH-dependent reduction of all of t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::be00ea5f5bad067bb9aa02d37955d4c7
https://doi.org/10.1016/s0021-9258(18)42844-x
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5
Aldose reductase from human skeletal and heart muscle. Interconvertible forms related by thiol-disulfide exchange
Autor: D L Vander Jagt, K K Taylor, B Robinson, Lucy A. Hunsaker
Publikováno v: Journal of Biological Chemistry. 265:20982-20987
Aldose reductase was purified from human skeletal and heart muscle by a rapid and efficient scheme involving Red Sepharose chromatography, chromatofocusing on Pharmacia PBE 94, and hydroxylapatite high pressure liquid chromatography. The scheme affor
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e9f630b0849f542017e8de47f01f4863
https://doi.org/10.1016/s0021-9258(17)45314-2
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6
Aldehyde and aldose reductases from human placenta. Heterogeneous expression of multiple enzyme forms
Autor: Lucy A. Hunsaker, L. A. Stangebye, Lorraine M. Deck, D L Vander Jagt, B Robinson
Publikováno v: Journal of Biological Chemistry. 265:10912-10918
Aldehyde reductase (ALR1) and aldose reductase (ALR2) were purified from human placenta by a rapid and efficient scheme that included rapid extraction of both reductases from 100,000 x g supernatant material with Red Sepharose followed by purificatio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::db0d5dec9098ce83ade44ae8f57bb46b
https://doi.org/10.1016/s0021-9258(19)38533-3
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7
Selective active site inhibitors of human lactate dehydrogenases A4, B4, and C4
Autor: Y, Yu, J A, Deck, L A, Hunsaker, L M, Deck, R E, Royer, E, Goldberg, D L, Vander Jagt
Publikováno v: Biochemical pharmacology. 62(1)
Human lactate dehydrogenases (LDH-A4, -B4, and -C4) are highly homologous with 84-89% sequence similarities and 69-75% amino acid identities. Active site residues are especially conserved. Gossypol, a natural product from cotton seed, is a non-select
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cd38d3298ce72c4efaf9165d328e5711
https://pubmed.ncbi.nlm.nih.gov/11377399
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10
Z-2 microsatellite allele is linked to increased expression of the aldose reductase gene in diabetic nephropathy
Autor: V O, Shah, M, Scavini, J, Nikolic, Y, Sun, S, Vai, J K, Griffith, R I, Dorin, C, Stidley, M, Yacoub, D L, Vander Jagt, R P, Eaton, P G, Zager
Publikováno v: The Journal of clinical endocrinology and metabolism. 83(8)
Epidemiological studies support the hypothesis that genetic factors modulate the risk for diabetic nephropathy (DN). Aldose reductase (ALDR1), the rate-limiting enzyme in the polyol pathway, is a potential candidate gene. The present study explores t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a85f5906937cb24e75920815a722eade
https://pubmed.ncbi.nlm.nih.gov/9709964
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