ARP8/YOR141C Literature Guide 
Other names published for ARP8: YOR141C
ARP8 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Sequence Features
- Protein-Nucleic Acid Interactions
- Protein-protein Interactions
- Protein/Nucleic Acid Structure
- Substrates/Ligands/Cofactors
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
ARP8 - Protein-protein Interactions (10)
| Reference | Other Genes Addressed |
|---|---|
| Fasolo J, et al. (2011) Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes. Genes Dev 25(7):767-78 |
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| Fenn S, et al. (2011) Structural biochemistry of nuclear actin-related proteins 4 and 8 reveals their interaction with actin. EMBO J 30(11):2153-66 |
|
| Dai Z, et al. (2009) Genome-wide analysis of interactions between ATP-dependent chromatin remodeling and histone modifications. BMC Genomics 10:304 |
|
| Li Z, et al. (2008) Cdc34p Ubiquitin-Conjugating Enzyme Is a Component of the Tombusvirus Replicase Complex and Ubiquitinates p33 Replication Protein. J Virol 82(14):6911-26 |
|
| Shevchenko A, et al. (2008) Chromatin Central: towards the comparative proteome by accurate mapping of the yeast proteomic environment. Genome Biol 9(11):R167 |
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| Szerlong H, et al. (2008) The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases. Nat Struct Mol Biol 15(5):469-76 |
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| van Attikum H, et al. (2004) Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell 119(6):777-88 |
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| Shen X, et al. (2003) Involvement of actin-related proteins in ATP-dependent chromatin remodeling. Mol Cell 12(1):147-55 |
|
| Harata M, et al. (2000) Multiple actin-related proteins of Saccharomyces cerevisiae are present in the nucleus. J Biochem 128(4):665-71 |
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| Shen X, et al. (2000) A chromatin remodelling complex involved in transcription and DNA processing. Nature 406(6795):541-4 |
