Other names published for BMH2: SCD3, YDR099W
BMH2 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
BMH2 - Primary Literature (53)
| Reference | Other Genes Addressed |
|---|---|
| Braun KA, et al. (2013) 14-3-3 (Bmh) Proteins Regulate Combinatorial Transcription following RNA Polymerase II Recruitment by Binding at Adr1-Dependent Promoters in Saccharomyces cerevisiae. Mol Cell Biol 33(4):712-24 | |
| 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 | |
| Clapp C, et al. (2012) 14-3-3 Protects against stress-induced apoptosis. Cell Death Dis 3():e348 | |
| Merhi A and Andre B (2012) Internal amino acids promote Gap1 permease ubiquitylation via TORC1/Npr1/14-3-3-dependent control of the Bul arrestin-like adaptors. Mol Cell Biol 32(22):4510-22 | |
| Parua PK, et al. (2012) Pichia pastoris 14-3-3 regulates transcriptional activity of the methanol inducible transcription factor Mxr1 by direct interaction. Mol Microbiol 85(2):282-98 | |
| Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76 | |
| 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 | |
| Gerber S, et al. (2010) Graphical analysis and experimental evaluation of Saccharomyces cerevisiae p(trk(1|2)) and p(bmh(1|2)) promoter region. Genome Inform 22(1):11-20 | |
| Ohlmeier S, et al. (2010) Protein phosphorylation in mitochondria - A study on fermentative and respiratory growth of Saccharomyces cerevisiae. Electrophoresis 31(17):2869-81 | |
| 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 | |
| Veisova D, et al. (2010) The C-terminal segment of yeast BMH proteins exhibits different structure compared to other 14-3-3 protein isoforms. Biochemistry 49(18):3853-61 | |
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| Martinez JS, et al. (2006) Acm1 is a negative regulator of the CDH1-dependent anaphase-promoting complex/cyclosome in budding yeast. Mol Cell Biol 26(24):9162-76 | |
| 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 | |
| Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 | |
| 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 |




