Other names published for SML1: YML058W
SML1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Physical Properties
- Protein Processing/Modification/Regulation
- Protein Sequence Features
- Protein-protein Interactions
- Protein/Nucleic Acid Structure
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Additional Information
SML1 - Protein-protein Interactions (8)
| Reference | Other Genes Addressed |
|---|---|
| Danielsson J, et al. (2008) The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer. Biochemistry 47(50):13428-37 | |
| Zhang Z, et al. (2007) Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1. Proc Natl Acad Sci U S A 104(7):2217-22 | |
| Gupta V, et al. (2004) Sml1p is a dimer in solution: characterization of denaturation and renaturation of recombinant Sml1p. Biochemistry 43(26):8568-78 | |
| Zhao X and Rothstein R (2002) The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1. Proc Natl Acad Sci U S A 99(6):3746-51 | |
| Georgieva B, et al. (2000) Damage response and dNTP regulation: the interaction between ribonucleotide reductase and its inhibitor, Sml1. Cold Spring Harb Symp Quant Biol 65():343-6 | |
| Zhao X, et al. (2000) Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality. Mol Cell Biol 20(23):9076-83 | |
| Chabes A, et al. (1999) Yeast Sml1, a protein inhibitor of ribonucleotide reductase. J Biol Chem 274(51):36679-83 | |
| Zhao X, et al. (1998) A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools. Mol Cell 2(3):329-40 |



