PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22898294-5 2012 Expression domain of brk during early blastdermal stages is defined through antagonistic interaction with dpp, and expression domains of dpp and brk in the early blastoderm include prospective hindgut domain. dipalmitoylphosphatidylserine 106-109 brinker Drosophila melanogaster 21-24 21385866-6 2011 We have previously shown that elimination of misspecified cells due to reduced Dpp signaling is achieved by the interaction of the co-repressor NAB with the transcriptional repressor Brk, which in turn induces Jun N-terminal kinase-dependent apoptosis. dipalmitoylphosphatidylserine 79-82 brinker Drosophila melanogaster 183-186 19270172-0 2009 The co-regulator dNAB interacts with Brinker to eliminate cells with reduced Dpp signaling. dipalmitoylphosphatidylserine 77-80 brinker Drosophila melanogaster 37-44 19270172-4 2009 Much of the regulation of transcriptional output by Dpp is mediated through repression of the transcriptional repressor Brinker (Brk), and thus through the activation of target genes. dipalmitoylphosphatidylserine 52-55 brinker Drosophila melanogaster 120-127 19270172-4 2009 Much of the regulation of transcriptional output by Dpp is mediated through repression of the transcriptional repressor Brinker (Brk), and thus through the activation of target genes. dipalmitoylphosphatidylserine 52-55 brinker Drosophila melanogaster 129-132 19270172-6 2009 At the molecular level, reduced Dpp signaling results in Brk upregulation that triggers apoptosis through activation of the JNK pathway. dipalmitoylphosphatidylserine 32-35 brinker Drosophila melanogaster 57-60 19270172-7 2009 Here we show that the transcriptional co-regulator dNAB is a Dpp target in the developing wing that interacts with Brk to eliminate cells with reduced Dpp signaling through the JNK pathway. dipalmitoylphosphatidylserine 61-64 brinker Drosophila melanogaster 115-118 19270172-7 2009 Here we show that the transcriptional co-regulator dNAB is a Dpp target in the developing wing that interacts with Brk to eliminate cells with reduced Dpp signaling through the JNK pathway. dipalmitoylphosphatidylserine 151-154 brinker Drosophila melanogaster 115-118 19270172-8 2009 We further show that both dNAB and Brk are required for cell elimination induced by differential dMyc expression, a process that depends on reduced Dpp transduction in outcompeted cells. dipalmitoylphosphatidylserine 148-151 brinker Drosophila melanogaster 35-38 19270172-9 2009 We propose a novel mechanism whereby the morphogen Dpp regulates the responsiveness to its own survival signal by inversely controlling the expression of a repressor, Brk, and its co-repressor, dNAB. dipalmitoylphosphatidylserine 51-54 brinker Drosophila melanogaster 167-170 18068697-6 2008 Together with gene expression data from these mutants and from brk mutants, our results suggest that there are two rounds of Dpp signaling in posterior spiracle development. dipalmitoylphosphatidylserine 125-128 brinker Drosophila melanogaster 63-66 17206277-5 2007 Repression of dpp requires a tri-partite complex of the WG mediators armadillo (ARM) and dTCF, and the co-repressor Brinker, (BRK), wherein ARM.dTCF and BRK bind to independent sites within the dpp locus. dipalmitoylphosphatidylserine 14-17 brinker Drosophila melanogaster 126-129 17206277-5 2007 Repression of dpp requires a tri-partite complex of the WG mediators armadillo (ARM) and dTCF, and the co-repressor Brinker, (BRK), wherein ARM.dTCF and BRK bind to independent sites within the dpp locus. dipalmitoylphosphatidylserine 14-17 brinker Drosophila melanogaster 153-156 17206277-5 2007 Repression of dpp requires a tri-partite complex of the WG mediators armadillo (ARM) and dTCF, and the co-repressor Brinker, (BRK), wherein ARM.dTCF and BRK bind to independent sites within the dpp locus. dipalmitoylphosphatidylserine 194-197 brinker Drosophila melanogaster 126-129 17206277-5 2007 Repression of dpp requires a tri-partite complex of the WG mediators armadillo (ARM) and dTCF, and the co-repressor Brinker, (BRK), wherein ARM.dTCF and BRK bind to independent sites within the dpp locus. dipalmitoylphosphatidylserine 194-197 brinker Drosophila melanogaster 153-156 16707253-2 2006 Through clonal analysis, we found that brinker (brk), a repressor of Dpp signaling, plays an important role in the Drosophila ovary, where its function is essential for dorsal appendage formation. dipalmitoylphosphatidylserine 69-72 brinker Drosophila melanogaster 39-46 16707253-2 2006 Through clonal analysis, we found that brinker (brk), a repressor of Dpp signaling, plays an important role in the Drosophila ovary, where its function is essential for dorsal appendage formation. dipalmitoylphosphatidylserine 69-72 brinker Drosophila melanogaster 48-51 11598015-0 2001 Brinker requires two corepressors for maximal and versatile repression in Dpp signalling. dipalmitoylphosphatidylserine 74-77 brinker Drosophila melanogaster 0-7 11598015-3 2001 Recent studies show that responses to graded Dpp activity also require an input from a complementary and opposing gradient of Brinker (Brk), a transcriptional repressor protein encoded by a Dpp target gene. dipalmitoylphosphatidylserine 45-48 brinker Drosophila melanogaster 126-133 11598015-3 2001 Recent studies show that responses to graded Dpp activity also require an input from a complementary and opposing gradient of Brinker (Brk), a transcriptional repressor protein encoded by a Dpp target gene. dipalmitoylphosphatidylserine 45-48 brinker Drosophila melanogaster 135-138 11598015-3 2001 Recent studies show that responses to graded Dpp activity also require an input from a complementary and opposing gradient of Brinker (Brk), a transcriptional repressor protein encoded by a Dpp target gene. dipalmitoylphosphatidylserine 190-193 brinker Drosophila melanogaster 126-133 11598015-3 2001 Recent studies show that responses to graded Dpp activity also require an input from a complementary and opposing gradient of Brinker (Brk), a transcriptional repressor protein encoded by a Dpp target gene. dipalmitoylphosphatidylserine 190-193 brinker Drosophila melanogaster 135-138 11598015-5 2001 By analysing transcriptional outcomes arising from the genetic removal of these corepressors, and by ectopically expressing Brk variants in the embryo, we demonstrate that these corepressors are alternatively used by Brk for repressing some Dpp-responsive genes, whereas for repressing other distinct target genes they are not required. dipalmitoylphosphatidylserine 241-244 brinker Drosophila melanogaster 217-220 11598015-6 2001 Our results show that Brk utilizes multiple means to repress its endogenous target genes, allowing repression of a multitude of complex Dpp target promoters. dipalmitoylphosphatidylserine 136-139 brinker Drosophila melanogaster 22-25