Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kristen M. Massimine"'
Autor:
Karen S. Anderson, R. Heiner Schirmer, Chloé E. Atreya, Worachart Sirawaraporn, Keith A. Joiner, Lanxuan T. Doan, Stephan Gromer, Michael T. McIntosh, Kristen M. Massimine, David A. Elliott
Publikováno v:
Antimicrobial Agents and Chemotherapy. 50:3132-3141
4′,5′-Dibromo-2′,7′-dinitrofluorescein, a red dye commonly referred to as eosin B, inhibits Toxoplasma gondii in both enzymatic and cell culture studies with a 50% inhibitory concentration (IC 50 ) of 180 μM. As a non-active-site inhibitor o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abf1484ad417d1d44c107525080ed966
https://doi.org/10.1128/aac.00621-06
https://doi.org/10.1128/aac.00621-06
Autor:
Chloé A. Atreya, Lanxuan T. Doan, Keith A. Joiner, Kristen M. Massimine, Isabelle Coppens, Karen S. Anderson, Timothy T. Stedman
Publikováno v:
Molecular and Biochemical Parasitology. 144:44-54
Folates are key elements in eukaryotic biosynthetic processes. The protozoan parasite Toxoplasma gondii possesses the enzymes necessary for de novo folate synthesis and has been suggested to lack alternative mechanisms for folate acquisition. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::822147c09e1b940db4c458ba8cacb0b8
https://doi.org/10.1016/j.molbiopara.2005.07.006
https://doi.org/10.1016/j.molbiopara.2005.07.006
Autor:
Kristen M, Massimine, Lanxuan T, Doan, Chloé A, Atreya, Timothy T, Stedman, Karen S, Anderson, Keith A, Joiner, Isabelle, Coppens
Publikováno v:
Molecular and biochemical parasitology. 144(1)
Folates are key elements in eukaryotic biosynthetic processes. The protozoan parasite Toxoplasma gondii possesses the enzymes necessary for de novo folate synthesis and has been suggested to lack alternative mechanisms for folate acquisition. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ca1c4f1f3f2599d816e2c5e167bfbeea
https://pubmed.ncbi.nlm.nih.gov/16159678
https://pubmed.ncbi.nlm.nih.gov/16159678
Autor:
Chloé E. Atreya, Isabelle Coppens, Antonia Dow, Keith A. Joiner, John J. Irwin, Eric F. Johnson, Karen S. Anderson, Valeska Stempliuk, Stephen M. Beverley, Kristen M. Massimine, Brian K. Shoichet
Publikováno v:
The Journal of biological chemistry. 278(16)
Protozoal parasites are unusual in that their thymidylate synthase (TS) and dihydrofolate reductase (DHFR) enzymes exist on a single polypeptide. In an effort to probe the possibility of substrate channeling between the TS and DHFR active sites and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc35c2b31a295b39e88746c17120a568
https://pubmed.ncbi.nlm.nih.gov/12556445
https://pubmed.ncbi.nlm.nih.gov/12556445