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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

GCN20 Gcn20p

GCN20, Gcn20p
Top mentioned proteins: ACID, GCN2, HAD, eIF2alpha, CAB
Papers on GCN20
eIF2 kinases mediate β-lapachone toxicity in yeast and human cancer cells.
Murguía et al., Rosario, Argentina. In Cell Cycle, 2014
eIF2α phosphorylation required Gcn1p, Gcn20p and Nde2p.
A chemical genomics study identifies Snf1 as a repressor of GCN4 translation.
Arndt et al., Pittsburgh, United States. In J Biol Chem, 2009
Snf1 functions upstream of Gcn20 to regulate control of GCN4 translation in S. cerevisiae
Genome-wide screening and identification of novel proteolytic cleavage targets of caspase-8 and -10 in vitro.
Ahn et al., Seoul, South Korea. In Int J Mol Med, 2008
Six putative caspase substrates, including five novel proteins (ABCF1, AKAP1, CPE, DOPEY1 and GOPC1) that may be targeted specifically by the initiator caspases 8 and 10 during the early stages of apoptosis, were identified.[caspase 10]
Heterologous expression of membrane and soluble proteins derepresses GCN4 mRNA translation in the yeast Saccharomyces cerevisiae.
Pedersen et al., Copenhagen, Denmark. In Eukaryot Cell, 2006
Derepression of GCN4 translation required phosphorylation of eIF-2alpha, the tRNA binding domain of Gcn2p, and the ribosome-associated proteins Gcn1p and Gcn20p.
Polyribosome binding by GCN1 is required for full activation of eukaryotic translation initiation factor 2{alpha} kinase GCN2 during amino acid starvation.
Hinnebusch et al., Bethesda, United States. In J Biol Chem, 2005
In Saccharomyces cerevisiae, activation of GCN2 by uncharged tRNAs in starved cells requires its direct interaction with both the GCN1.GCN20 regulatory complex and ribosomes.
The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assembly.
Hinnebusch et al., Bethesda, United States. In J Biol Chem, 2004
RLI1 is an essential yeast protein closely related in sequence to two soluble members of the ATP-binding cassette family of proteins that interact with ribosomes and function in translation elongation (YEF3) or translational control (GCN20).
Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2.
Hinnebusch et al., Bethesda, United States. In Genes Dev, 2002
These mutations also bypass the requirement for ribosome binding, dimerization, and association with the GCN1/GCN20 regulatory complex, suggesting that all of these functions facilitate tRNA binding to wild-type GCN2.
Comparative analysis of sequences encoding ABC systems in the genome of the microsporidian Encephalitozoon cuniculi.
Dassa et al., France. In Fems Microbiol Lett, 2002
Two proteins with duplicated ABC domains are clearly candidate to non-transport ABC systems: the first is homologous to mammalian RNase L inhibitor and the second to the yeast translation initiation regulator GCN20.
The ABC transporter genes of Plasmodium falciparum and drug resistance.
Peel, Rockville, United States. In Drug Resist Updat, 2001
To date, three full-length ABC transporter genes have been isolated from P. falciparum: two P-glycoprotein-like homologues, pfmdr1 and pfmdr2, and a homologue of the yeast GCN20 gene, pfgcn20.
Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells.
Hinnebusch et al., Bethesda, United States. In Embo J, 2001
GCN2 stimulates GCN4 translation in amino acid-starved cells by phosphorylating the alpha-subunit of translation initiation factor 2. GCN2 function in vivo requires the GCN1/GCN20 complex, which binds to the N-terminal domain of GCN2.
ABC50 interacts with eukaryotic initiation factor 2 and associates with the ribosome in an ATP-dependent manner.
Proud et al., Dundee, United Kingdom. In J Biol Chem, 2000
ABC50 is related to GCN20 and eEF3, two yeast ABC proteins that are not membrane-associated transporters and are instead implicated in mRNA translation and/or its control.
Association of GCN1-GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation.
Hinnebusch et al., Bethesda, United States. In Embo J, 2000
GCN2 function in vivo also requires GCN1 and GCN20, but it was unknown whether these latter proteins act directly to promote the stimulation of GCN2 by uncharged tRNA.
Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase.
Wek et al., Indianapolis, United States. In Mol Cell Biol, 2000
Furthermore, Gcn20p, a factor required for Gcn2 protein kinase stimulation of GCN4 expression in response to amino acid starvation, is not essential for GCN4 translational control in response to limitation for carbohydrates.
An inventory of the human ABC proteins.
Váradi et al., Budapest, Hungary. In Biochim Biophys Acta, 2000
At present the MDR/TAP, the ALD, the MRP/CFTR, the ABC1, the White, the RNAseL inhibitor, the ANSA, and the GCN20 subfamilies are identified.
Protein transport in the host cell cytoplasm and ATP-binding cassette proteins in Plasmodium falciparum-infected erythrocytes.
Schurr et al., Montréal, Canada. In Novartis Found Symp, 1998
PfGCN20 was found to complement the function of its yeast homologue Gcn20p by acting as part of the yeast translation regulatory pathway.
The human malaria parasite Plasmodium falciparum exports the ATP-binding cassette protein PFGCN20 to membrane structures in the host red blood cell.
Schurr et al., Montréal, Canada. In Mol Biochem Parasitol, 1998
PFGCN20 is a member of the ATP-binding cassette family of proteins that is closely related to the yeast translational regulator Gcn20p.
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