Pub. Date : 2009 Sep 29
PMID : 19681600
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Effect of thioredoxin deletion and p53 cysteine replacement on human p53 activity in wild-type and thioredoxin reductase null yeast. | Cysteine | tumor protein p53 | Homo sapiens |
| 2 | Substitutions at Zn-coordinating cysteines C176, C238, or C242 resulted in p53 inactivation. | Cysteine | tumor protein p53 | Homo sapiens |
| 3 | Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. | Cysteine | tumor protein p53 | Homo sapiens |
| 4 | Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. | Cysteine | tumor protein p53 | Homo sapiens |
| 5 | Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. | Cysteine | tumor protein p53 | Homo sapiens |
| 6 | Unexpectedly, substitution at cysteine C275 also inactivated p53, which was the first evidence for a non-zinc-coordinating cysteine being essential for p53 function. | Cysteine | tumor protein p53 | Homo sapiens |
| 7 | Cysteine substitutions at six positions (C124, C135, C141, C182, C229, and C277) neither inactivated p53 nor relieved the requirement for thioredoxin reductase. | Cysteine | tumor protein p53 | Homo sapiens |
| 8 | The results suggested that p53 dependence on thioredoxin reductase either was indirect, perhaps mediated by an upstream activator of p53, or was due to oxidation of one or more of the four essential cysteines. | Cysteine | tumor protein p53 | Homo sapiens |