GoPubMed Proteins lists recent and important papers and reviews for
proteins. Page last changed on 19 Dec 2016.
DPR1, RAM1, Frodo, Dact1, Dapper, Dapper1
The protein encoded by this gene belongs to the dapper family, characterized by the presence of PDZ-binding motif at the C-terminus. It interacts with, and positively regulates dishevelled-mediated signaling pathways during development. Depletion of this mRNA from xenopus embryos resulted in loss of notochord and head structures, and mice lacking this gene died shortly after birth from severe posterior malformations. Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jan 2012] (from
Harrison et al., Ithaca, United States. In Plant Physiol, Dec 2015
Here, we provide a detailed characterization of an insertion allele of Medicago truncatula Reduced Arbuscular Mycorrhiza1 (RAM1), ram1-3, which reveals that RAM1 is not necessary to enable hyphopodium formation or hyphal entry into the root but is essential to support arbuscule branching.
Sakurada et al., Kashiwa, Japan. In J Forensic Sci, Sep 2015
In this study, we report the development of a real-time polymerase chain reaction-based method for identifying semen that can simply and rapidly analyze the semen-specific unmethylated region of the DACT1 gene.
Küster et al., Hannover, Germany. In Bmc Genomics, 2014
Using complex gene expression fingerprints as molecular phenotypes, this study primarily intended to shed light on the importance of the GRAS TFs NSP1 and RAM1 for LCO-activated gene expression during pre-symbiotic signaling.
Harris et al., Vancouver, Canada. In Birth Defects Res A Clin Mol Teratol, 2012
Rare putative mutations in the PCP genes VANGL2, SCRIB, DACT1, and CELSR1 cumulatively contributed to over 20% of cases with craniorachischisis, a rare defect; no contributing variants were found for PRICKLE1 or PTK7.
Gibbs et al., Point Pedro, Sri Lanka. In Mol Microbiol, 1994
The initial genetic analysis of prenyl protein transferases was in S. cerevisiae with the isolation and subsequent characterization of mutations in the RAM1, RAM2, CDC43 and BET2 genes, each of which encodes a prenyl protein transferase subunit.
Brown et al., Dallas, United States. In Cell, 1991
The rat beta subunit shows 37% sequence identity with the protein encoded by the yeast DPR1/RAM1 gene, indicating that DPR1/RAM1 is the yeast counterpart of the peptide-binding subunit of the mammalian farnesyltransferase.