Literature Help
YNCN0008C Literature
All manually curated literature for the specified gene, organized by relevance to the gene and by
association with specific annotations to the gene in SGD. SGD gathers references via a PubMed search for
papers whose titles or abstracts contain “yeast” or “cerevisiae;” these papers are reviewed manually and
linked to relevant genes and literature topics by SGD curators.
- Unique References
- 51
- Aliases
-
tD(GUC)N
,
tRNA-Asp
Primary Literature
Literature that either focuses on the gene or contains information about function, biological role,
cellular location, phenotype, regulation, structure, or disease homologs in other species for the gene
or gene product.
No primary literature curated.
Related Literature
Genes that share literature (indicated by the purple circles) with the specified gene (indicated by yellow circle).
Reset
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Additional Literature
Papers that show experimental evidence for the gene or describe homologs in other species, but
for which the gene is not the paper’s principal focus.
No additional literature curated.
Download References (.nbib)
- Strassler SE, et al. (2023) tRNA m1G9 modification depends on substrate-specific RNA conformational changes induced by the methyltransferase Trm10. J Biol Chem 299(12):105443 PMID:37949221
- Zhang X, et al. (2014) Influence of Sequence and Covalent Modifications on Yeast tRNA Dynamics. J Chem Theory Comput 10(8):3473-3483 PMID:25136272
- Iben JR and Maraia RJ (2012) tRNAomics: tRNA gene copy number variation and codon use provide bioinformatic evidence of a new anticodon:codon wobble pair in a eukaryote. RNA 18(7):1358-72 PMID:22586155
- Qi X, et al. (2012) Retrotransposon profiling of RNA polymerase III initiation sites. Genome Res 22(4):681-92 PMID:22287102
- Yukawa Y, et al. (2011) A common sequence motif involved in selection of transcription start sites of Arabidopsis and budding yeast tRNA genes. Genomics 97(3):166-72 PMID:21147216
- Ouameur AA, et al. (2010) Probing tRNA interaction with biogenic polyamines. RNA 16(10):1968-79 PMID:20729276
- Ozanick SG, et al. (2009) Rex1p deficiency leads to accumulation of precursor initiator tRNAMet and polyadenylation of substrate RNAs in Saccharomyces cerevisiae. Nucleic Acids Res 37(1):298-308 PMID:19042972
- Zaborske JM, et al. (2009) Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p. J Biol Chem 284(37):25254-67 PMID:19546227
- Thompson DM, et al. (2008) tRNA cleavage is a conserved response to oxidative stress in eukaryotes. RNA 14(10):2095-103 PMID:18719243
- Wang B, et al. (2008) Complex ligand-induced conformational changes in tRNA(Asp) revealed by single-nucleotide resolution SHAPE chemistry. Biochemistry 47(11):3454-61 PMID:18290632
- Cieśla M, et al. (2007) Maf1 is involved in coupling carbon metabolism to RNA polymerase III transcription. Mol Cell Biol 27(21):7693-702 PMID:17785443
- Jakó E, et al. (2007) In silico detection of tRNA sequence features characteristic to aminoacyl-tRNA synthetase class membership. Nucleic Acids Res 35(16):5593-609 PMID:17704131
- Muller S, et al. (2007) Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:Psi55-synthase and RNA-guided RNA:Psi-synthase activities. Nucleic Acids Res 35(16):5610-24 PMID:17704128
- Goodenbour JM and Pan T (2006) Diversity of tRNA genes in eukaryotes. Nucleic Acids Res 34(21):6137-46 PMID:17088292
- Marck C, et al. (2006) The RNA polymerase III-dependent family of genes in hemiascomycetes: comparative RNomics, decoding strategies, transcription and evolutionary implications. Nucleic Acids Res 34(6):1816-35 PMID:16600899
- Conesa C, et al. (2005) Modulation of yeast genome expression in response to defective RNA polymerase III-dependent transcription. Mol Cell Biol 25(19):8631-42 PMID:16166643
- Fender A, et al. (2004) A yeast arginine specific tRNA is a remnant aspartate acceptor. Nucleic Acids Res 32(17):5076-86 PMID:15452274
- Behm-Ansmant I, et al. (2003) The Saccharomyces cerevisiae U2 snRNA:pseudouridine-synthase Pus7p is a novel multisite-multisubstrate RNA:Psi-synthase also acting on tRNAs. RNA 9(11):1371-82 PMID:14561887
- Giuliodori S, et al. (2003) A composite upstream sequence motif potentiates tRNA gene transcription in yeast. J Mol Biol 333(1):1-20 PMID:14516739
- Walter F, et al. (2002) Binding of tobramycin leads to conformational changes in yeast tRNA(Asp) and inhibition of aminoacylation. EMBO J 21(4):760-8 PMID:11847123
- Wittberger D, et al. (2000) Evaluation of uranyl photocleavage as a probe to monitor ion binding and flexibility in RNAs. J Mol Biol 300(2):339-52 PMID:10873469
- Auffinger P and Westhof E (1999) Singly and bifurcated hydrogen-bonded base-pairs in tRNA anticodon hairpins and ribozymes. J Mol Biol 292(3):467-83 PMID:10497015
- Auffinger P, et al. (1999) Molecular dynamics simulations of solvated yeast tRNA(Asp). Biophys J 76(1 Pt 1):50-64 PMID:9876122
- Matveeva O, et al. (1997) A rapid in vitro method for obtaining RNA accessibility patterns for complementary DNA probes: correlation with an intracellular pattern and known RNA structures. Nucleic Acids Res 25(24):5010-6 PMID:9396809
- Frugier M, et al. (1994) Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 33(33):9912-21 PMID:8060999
- Rudinger J, et al. (1994) Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu. Biochemistry 33(19):5682-8 PMID:8180193
- Edqvist J, et al. (1993) Pleiotrophic effects of point mutations in yeast tRNA(Asp) on the base modification pattern. Nucleic Acids Res 21(3):413-7 PMID:8441654
- Chow CS, et al. (1992) Recognition of tertiary structure in tRNAs by Rh(phen)2phi3+, a new reagent for RNA structure-function mapping. Biochemistry 31(4):972-82 PMID:1734973
- Haumont E, et al. (1987) Enzymatic formation of queuosine and of glycosyl queuosine in yeast tRNAs microinjected into Xenopus laevis oocytes. The effect of the anticodon loop sequence. Eur J Biochem 168(1):219-25 PMID:3117541
- Leroy JL, et al. (1985) Internal motions of transfer RNA: a study of exchanging protons by magnetic resonance. J Biomol Struct Dyn 2(5):915-39 PMID:2855781
- Westhof E, et al. (1985) Crystallographic refinement of yeast aspartic acid transfer RNA. J Mol Biol 184(1):119-45 PMID:3897553
- Keith G and Pixa G (1984) The nucleotide sequence of asparagine tRNA from brewer's yeast. Biochimie 66(9-10):639-43 PMID:6395902
- Figueroa N, et al. (1983) NMR study of slowly exchanging imino protons in yeast tRNAasp. Proc Natl Acad Sci U S A 80(14):4330-3 PMID:6348768
- Westhof E, et al. (1983) Loop stereochemistry and dynamics in transfer RNA. J Biomol Struct Dyn 1(2):337-55 PMID:6401114
- Roy S, et al. (1982) Nuclear overhauser effect study of yeast aspartate transfer ribonucleic acid. Biochemistry 21(24):6081-8 PMID:6758844
- Roy S and Redfield AG (1981) Nuclear Overhauser effect study and assignment of D stem and reverse-Hoogsteen base pair proton resonances in yeast tRNAAsp. Nucleic Acids Res 9(24):7073-83 PMID:6278454
- Giegé R, et al. (1980) [Crystallization of the complex formed between yeast aspartyl tRNA and its specific aminoacyl tRNA synthetase]. C R Seances Acad Sci D 291(4):393-6 PMID:6777057
- Robillard GT, et al. (1976) A study of secondary and tertiary solution structure of yeast tRNA(Asp) by nuclear magnetic resonance. Assignment of G.U ring NH and hydrogen-bonded base pair proton resonances. Biochemistry 15(9):1883-8 PMID:773428
Reviews
No reviews curated.
Gene Ontology Literature
Paper(s) associated with one or more GO (Gene Ontology) terms in SGD for the specified gene.
No gene ontology literature curated.
Interaction Literature
Paper(s) associated with evidence supporting a physical or genetic interaction between the
specified gene and another gene in SGD. Currently, all interaction evidence is obtained from
BioGRID.
No interaction literature curated.
Download References (.nbib)
- Ryckelynck M, et al. (2003) Yeast tRNA(Asp) charging accuracy is threatened by the N-terminal extension of aspartyl-tRNA synthetase. J Biol Chem 278(11):9683-90 PMID:12486031
- Sissler M, et al. (1996) Arginine aminoacylation identity is context-dependent and ensured by alternate recognition sets in the anticodon loop of accepting tRNA transcripts. EMBO J 15(18):5069-76 PMID:8890180