Zobrazeno 1 - 8
of 8
pro vyhledávání: '"L. Krauth"'
Autor:
Maria Paz Clares, Francisco Olmo, Mario Inclán, R. L. Krauth-Siegel, Clotilde Marín, Kristína Urbanová, Conxa Soriano, Enrique García-España, María José Rosales, Roberto Tejero, Jorge González, Manuel Sánchez-Moreno
Publikováno v:
RSC Adv.. 4:65108-65120
The anti-chagasic activity of a series of eleven derivatives of aza-scorpiand-like macrocycles, some of them newly synthesised, was assayed. The four compounds with the best selectivity indices in vitro were subjected to in vivo assays. Tests in a mu
Publikováno v:
Journal of Medicinal Chemistry. 43:4812-4821
(2,2':6',2"-terpyridine)platinum(II) complexes possess pronounced cytostatic activities against trypanosomes and leishmania. As shown here, the complexes are irreversible inhibitors of trypanothione reductase (TR) from Trypanosoma cruzi, the causativ
Publikováno v:
Journal of Medicinal Chemistry. 39:1549-1554
A series of newly synthesized N10-arylisoalloxazinessome of which are known to be antimalarial agentswere studied as inhibitors of human glutathione reductase (GR; NADPH + GSSG + H+ ⇌ NADP+ + 2GSH)...
Autor:
R Schöneck, R L Krauth-Siegel
Publikováno v:
The FASEB Journal. 9:1138-1146
Trypanothione reductase (TR) is a flavoenzyme that has been found only in parasitic protozoa of the order Kinetoplastida. The enzyme catalyzes the NADPH-dependent reduction of glutathionylspermidine conjugates and is a key enzyme of the parasite's th
Publikováno v:
Journal of medicinal chemistry. 42(26)
Series of 9-amino and 9-thioacridines have been synthesized and studied as inhibitors of trypanothione reductase (TR) from Trypanosoma cruzi, the causative agent of Chagas' disease. The compounds are structural analogues of the acridine drug mepacrin
Autor:
H. Gallwitz, Ilme Schlichting, K. Schumacher, S. Bonse, A. Martinez-Cruz, R. L. Krauth-Siegel
Publikováno v:
Journal of Medicinal Chemistry
Ajoene ((E,Z)-4,5,9-trithiadodeca-1,6,11-triene 9-oxide), a garlic-derived natural compound, is a covalent inhibitor as well as a substrate of human glutathione reductase (GR) and Trypanosoma cruzi trypanothione reductase (TR). The 2.1-A resolution c
Publikováno v:
Biochemistry. 37(40)
Tyr114 and Tyr197 are highly conserved residues in the active site of human glutathione reductase, Tyr114 in the glutathione disulfide (GSSG) binding site and Tyr197 in the NADPH site. Mutation of either residue has profound effects on catalysis. Y19
Publikováno v:
ResearcherID
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