X-ray structure of glutathione S-transferase from the malarial parasite Plasmodium falciparum
GSTs catalyze the conjugation of glutathione with a wide variety of hydrophobic compounds, generally resulting in nontoxic products that can be readily eliminated. In contrast to many other organisms, the malarial parasite Plasmodium falciparum possesses only one GST isoenzyme (PfGST). This GST is h...
保存先:
| 出版年: | Proc Natl Acad Sci U S A |
|---|---|
| 主要な著者: | , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2003
|
| 主題: | |
| オンライン・アクセス: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC283505/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/14623980/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.2333763100 |
| タグ: |
タグなし, このレコードへの初めてのタグを付けませんか!
|
