Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Narsimha R. Munagala"'
Autor:
Narsimha R. Munagala, Ching C. Wang
Publikováno v:
Molecular and Biochemical Parasitology. 127:143-149
Trichomonas vaginalis, a parasitic protozoan and the causative agent of trichomoniasis, lacks de novo purine nucleotide synthesis and possesses a unique purine salvage pathway, consisting of a bacterial type purine nucleoside phosphorylase and a puri
Autor:
Narsimha R. Munagala, Ching C. Wang
Publikováno v:
Biochemistry. 41:10382-10389
Trichomonas vaginalis is a parasitic protozoan and the causative agent of trichomoniasis. Its primary purine salvage system, consisting of a purine nucleoside phosphorylase (PNP) and a purine nucleoside kinase, presents potential targets for designin
Autor:
Narsimha R. Munagala, Ching C. Wang
Publikováno v:
Molecular Microbiology. 44:1073-1079
Giardia lamblia is an anaerobic binucleate flagellated protozoan known to lack de novo synthesis of purine nucleotides. Our previous metabolic studies indicated two major parallel pathways mediated by adenine phosphoribosyltransferase (APRT) and guan
Publikováno v:
European Journal of Biochemistry. 259:565-571
Publikováno v:
Antimicrobial Agents and Chemotherapy. 45:2571-2576
Parasitic protozoa lack the ability to synthesize purine nucleotides de novo, relying instead on purine salvage enzymes for their survival. Guanine phosphoribosyltransferase (GPRT) from the protozoan parasite Giardia lamblia is a potential target for
Autor:
Vern L. Schramm, Richard H. Furneaux, Steven C. Almo, Narsimha R. Munagala, Caroline M. Li, Ching C. Wang, Peter C. Tyler, Charles Grubmeyer, Wuxian Shi
Publikováno v:
Biochemistry. 39:6781-6790
Giardia lamblia, the protozoan parasite responsible for giardiasis, requires purine salvage from its host for RNA and DNA synthesis. G. lamblia expresses an unusual purine phosphoribosyltransferase with a high specificity for guanine (GPRTase). The e
Publikováno v:
Biochemistry. 39:4684-4691
All parasitic protozoa lack the ability to synthesize purine nucleotides de novo, relying instead on purine salvage enzymes for their survival. Hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRT) from the protozoan parasite Tritrichomona
Autor:
Ching C. Wang, Narsimha R. Munagala
Publikováno v:
Biochemistry. 37:16612-16619
The hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been proven to be a target for potential anti-tritrichomonial chemotherapy. Using a structure-based approach, the base-binding region of the active
Publikováno v:
Biochemistry. 40(14)
The hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase), a type I PRTase, from Tritrichomonas foetus, is a potential target for antitritrichomonal chemotherapy. Structural data on all the type I PRTases reveal a highly flexible, 11-14
Autor:
Irwin D. Kuntz, Connie M. Oshiro, Robert J. Fletterick, Solomon Mpoke, A. Geoffrey SkillmanJr., Ronald M. A. Knegtel, Ching C. Wang, Shinichi Katakura, John R. Somoza, Narsimha R. Munagala
Publikováno v:
Molecular Modeling and Prediction of Bioactivity ISBN: 9781461368571
Most protozoan parasites, such as Leishmania, Plasmodium, Toxoplasma and Trypanosoma, rely on a salvage pathway for their supply of purine ribonucleotides (Wang, 1984). Inhibition of this pathway therefore presents an interesting approach in the figh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::71ca296113e4619b0ae3f7dae4560421
https://doi.org/10.1007/978-1-4615-4141-7_86
https://doi.org/10.1007/978-1-4615-4141-7_86