BMH2/YDR099W Literature Guide Help

Other names published for BMH2: SCD3, YDR099W

BMH2 - Non-Fungal Related Genes/Proteins (21)

ReferenceOther Genes Addressed
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
Owen JR, et al.  (2012) Induction of expression of a 14-3-3 gene in response to copper exposure in the marine alga, Fucus vesiculosus. Ecotoxicology 21(1):124-38
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
Engels K, et al.  (2011) 14-3-3 proteins regulate exonuclease 1-dependent processing of stalled replication forks. PLoS Genet 7(4):e1001367
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
Clokie S, et al.  (2009) The interaction between casein kinase Ialpha and 14-3-3 is phosphorylation dependent. FEBS J 276(23):6971-84
Fischer A, et al.  (2009) Regulation of RAF Activity by 14-3-3 Proteins: RAF KINASES ASSOCIATE FUNCTIONALLY WITH BOTH HOMO- AND HETERODIMERIC FORMS OF 14-3-3 PROTEINS. J Biol Chem 284(5):3183-94
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
Yao Y, et al.  (2007) Molecular analysis and expression patterns of the 14-3-3 gene family from Oryza sativa. J Biochem Mol Biol 40(3):349-57
Kjarland E, et al.  (2006) Does isoform diversity explain functional differences in the 14-3-3 protein family? Curr Pharm Biotechnol 7(3):217-23
van Heusden GP and Yde Steensma H  (2006) Yeast 14-3-3 proteins. Yeast 23(3):159-71
Callejo M, et al.  (2002) The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307. J Biol Chem 277(41):38416-23
Kleppe R, et al.  (2001) Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association. J Neurochem 77(4):1097-107
Athwal GS, et al.  (2000) Modulation of 14-3-3 protein interactions with target polypeptides by physical and metabolic effectors. Plant Cell Physiol 41(4):523-33
Roth D, et al.  (1999) Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae. FEBS Lett 460(3):411-6
Knetsch ML, et al.  (1997) Isolation of a Dictyostelium discoideum 14-3-3 homologue. Biochim Biophys Acta 1357(2):243-8
Moorhead G, et al.  (1996) Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr Biol 6(9):1104-13
van Heusden GP, et al.  (1996) Four Arabidopsis thaliana 14-3-3 protein isoforms can complement the lethal yeast bmh1 bmh2 double disruption. FEBS Lett 391(3):252-6
Conklin DS, et al.  (1995) 14-3-3 proteins associate with cdc25 phosphatases. Proc Natl Acad Sci U S A 92(17):7892-6
Gelperin D, et al.  (1995) 14-3-3 proteins: potential roles in vesicular transport and Ras signaling in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 92(25):11539-43
van Heusden GP, et al.  (1995) The 14-3-3 proteins encoded by the BMH1 and BMH2 genes are essential in the yeast Saccharomyces cerevisiae and can be replaced by a plant homologue. Eur J Biochem 229(1):45-53