Other names published for BMH2: SCD3, YDR099W
BMH2 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Other Features
- Strains/Constructs
- Techniques and Reagents
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
BMH2 - Strains/Constructs (43)
| Reference | Other Genes Addressed |
|---|---|
| Becuwe M, et al. (2012) A molecular switch on an arrestin-like protein relays glucose signaling to transporter endocytosis. J Cell Biol 196(2):247-59 | |
| Dengjel J, et al. (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035 | |
| Zahradka J, et al. (2012) Yeast 14-3-3 proteins participate in the regulation of cell cation homeostasis via interaction with Nha1 alkali-metal-cation/proton antiporter. Biochim Biophys Acta 1820(7):849-58 | |
| Engels K, et al. (2011) 14-3-3 proteins regulate exonuclease 1-dependent processing of stalled replication forks. PLoS Genet 7(4):e1001367 | |
| Panni S, et al. (2011) Combining peptide recognition specificity and context information for the prediction of the 14-3-3-mediated interactome in S. cerevisiae and H. sapiens. Proteomics 11(1):128-43 | |
| Parua PK, et al. (2010) 14-3-3 (Bmh) Proteins Inhibit Transcription Activation by Adr1 through Direct Binding to Its Regulatory Domain. Mol Cell Biol 30(22):5273-83 | |
| Akiyoshi B, et al. (2009) Quantitative proteomic analysis of purified yeast kinetochores identifies a PP1 regulatory subunit. Genes Dev 23(24):2887-99 | |
| Clokie S, et al. (2009) The interaction between casein kinase Ialpha and 14-3-3 is phosphorylation dependent. FEBS J 276(23):6971-84 | |
| Wang C, et al. (2009) Deleting the 14-3-3 protein Bmh1 extends life span in Saccharomyces cerevisiae by increasing stress response. Genetics 183(4):1373-84 | |
| Yahyaoui W and Zannis-Hadjopoulos M (2009) 14-3-3 proteins function in the initiation and elongation steps of DNA replication in Saccharomyces cerevisiae. J Cell Sci 122(Pt 24):4419-26 | |
| Demmel L, et al. (2008) Nucleocytoplasmic shuttling of the Golgi phosphatidylinositol 4-kinase pik1 is regulated by 14-3-3 proteins and coordinates Golgi function with cell growth. Mol Biol Cell 19(3):1046-61 | |
| Grandin N and Charbonneau M (2008) Budding yeast 14-3-3 proteins contribute to the robustness of the DNA damage and spindle checkpoints. Cell Cycle 7(17):2749-61 | |
| Panni S, et al. (2008) Role of 14-3-3 proteins in the regulation of neutral trehalase in the yeast Saccharomyces cerevisiae. FEMS Yeast Res 8(1):53-63 | |
| Seitomer E, et al. (2008) Analysis of Saccharomyces cerevisiae null allele strains identifies a larger role for DNA damage versus oxidative stress pathways in growth inhibition by selenium. Mol Nutr Food Res 52(11):1305-15 | |
| Walter W, et al. (2008) 14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation. Mol Cell Biol 28(8):2840-9 | |
| Wu X and Jiang YW (2008) Overproduction of non-translatable mRNA silences. The transcription of Ty1 retrotransposons in S. cerevisiae via functional inactivation of the nuclear cap-binding complex and subsequent hyperstimulation of the TORC1 pathway. Yeast 25(5):327-47 | |
| Bruckmann A, et al. (2007) Post-Transcriptional Control of the Saccharomyces cerevisiae Proteome by 14-3-3 Proteins. J Proteome Res 6(5):1689-1699 | |
| Dial JM, et al. (2007) Inhibition of APCCdh1 activity by Cdh1/Acm1/Bmh1 ternary complex formation. J Biol Chem 282(8):5237-48 | |
| Gasser B, et al. (2007) Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl Environ Microbiol 73(20):6499-507 | |
| Kakiuchi K, et al. (2007) Proteomic analysis of in vivo 14-3-3 interactions in the yeast Saccharomyces cerevisiae. Biochemistry 46(26):7781-92 | |
| Lottersberger F, et al. (2007) Functional and physical interactions between yeast 14-3-3 proteins, acetyltransferases, and deacetylases in response to DNA replication perturbations. Mol Cell Biol 27(9):3266-81 | |
| Usui T and Petrini JH (2007) The Saccharomyces cerevisiae 14-3-3 proteins Bmh1 and Bmh2 directly influence the DNA damage-dependent functions of Rad53. Proc Natl Acad Sci U S A 104(8):2797-802 | |
| Yahyaoui W, et al. (2007) Deletion of the cruciform binding domain in CBP/14-3-3 displays reduced origin binding and initiation of DNA replication in budding yeast. BMC Mol Biol 8():27 | |
| Lottersberger F, et al. (2006) The Saccharomyces cerevisiae 14-3-3 proteins are required for the G1/S transition, actin cytoskeleton organization and cell wall integrity. Genetics 173(2):661-75 | |
| Michelsen K, et al. (2006) A multimeric membrane protein reveals 14-3-3 isoform specificity in forward transport in yeast. Traffic 7(7):903-16 | |
| Hwang GW, et al. (2005) Overexpression of Bop3 confers resistance to methylmercury in Saccharomyces cerevisiae through interaction with other proteins such as Fkh1, Rts1, and Msn2. Biochem Biophys Res Commun 330(2):378-85 | |
| Tomas-Cobos L, et al. (2005) TOR kinase pathway and 14-3-3 proteins regulate glucose-induced expression of HXT1, a yeast low-affinity glucose transporter. Yeast 22(6):471-9 | |
| Wanke V, et al. (2005) Regulation of G0 entry by the Pho80-Pho85 cyclin-CDK complex. EMBO J 24(24):4271-8 | |
| Bruckmann A, et al. (2004) Regulation of transcription by Saccharomyces cerevisiae 14-3-3 proteins. Biochem J 382(Pt 3):867-75 | |
| Dombek KM, et al. (2004) The Reg1-interacting proteins, Bmh1, Bmh2, Ssb1, and Ssb2, have roles in maintaining glucose repression in Saccharomyces cerevisiae. J Biol Chem 279(37):39165-74 |





