| First Author | Mustafa AK | Year | 2009 |
| Journal | Sci Signal | Volume | 2 |
| Issue | 96 | Pages | ra72 |
| PubMed ID | 19903941 | Mgi Jnum | J:182483 |
| Mgi Id | MGI:5315686 | Doi | 10.1126/scisignal.2000464 |
| Citation | Mustafa AK, et al. (2009) H2S signals through protein S-sulfhydration. Sci Signal 2(96):ra72 |
| abstractText | Hydrogen sulfide (H2S), a messenger molecule generated by cystathionine gamma-lyase, acts as a physiologic vasorelaxant. Mechanisms whereby H2S signals have been elusive. We now show that H2S physiologically modifies cysteines in a large number of proteins by S-sulfhydration. About 10 to 25% of many liver proteins, including actin, tubulin, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), are sulfhydrated under physiological conditions. Sulfhydration augments GAPDH activity and enhances actin polymerization. Sulfhydration thus appears to be a physiologic posttranslational modification for proteins. |
