YPRWTy1-3 Literature Guide Help

Other names published for YPRWTy1-3: Ty1

YPRWTy1-3 - Transcription (13)

ReferenceOther Genes Addressed
Aulds J, et al.  (2012) Global identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP). J Biol Chem 287(44):37089-97
Servant G, et al.  (2012) Tye7 regulates yeast Ty1 retrotransposon sense and antisense transcription in response to adenylic nucleotides stress. Nucleic Acids Res 40(12):5271-82
Matsuda E and Garfinkel DJ  (2009) Posttranslational interference of Ty1 retrotransposition by antisense RNAs. Proc Natl Acad Sci U S A 106(37):15657-62
Jiang YW  (2008) An essential role of Tap42-associated PP2A and 2A-like phosphatases in Ty1 transcriptional silencing of S. cerevisiae. Yeast 25(10):755-64
Heyman T, et al.  (2003) The central PPT of the yeast retrotransposon Ty1 is not essential for transposition. J Mol Biol 331(2):315-20
Cristofari G, et al.  (2002) A 5'-3' long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition. EMBO J 21(16):4368-79
Jiang YW  (2002) Transcriptional cosuppression of yeast Ty1 retrotransposons. Genes Dev 16(4):467-78
Lawler JF Jr, et al.  (2002) A nucleocapsid functionality contained within the amino terminus of the Ty1 protease that is distinct and separable from proteolytic activity. J Virol 76(1):346-54
Lawler JF Jr, et al.  (2002) Ty1 defect in proteolysis at high temperature. J Virol 76(9):4233-40
Uzun O and Gabriel A  (2001) A Ty1 reverse transcriptase active-site aspartate mutation blocks transposition but not polymerization. J Virol 75(14):6337-47
Wilhelm M, et al.  (1999) A sequence immediately upstream of the plus-strand primer is essential for plus-strand DNA synthesis of the Saccharomyces cerevisiae Ty1 retrotransposon. Nucleic Acids Res 27(23):4547-52
Lauermann V, et al.  (1995) Plus-strand strong-stop DNA synthesis in retrotransposon Ty1. J Virol 69(12):7845-50
Wilhelm M, et al.  (1994) Yeast Ty1 retrotransposon: the minus-strand primer binding site and a cis-acting domain of the Ty1 RNA are both important for packaging of primer tRNA inside virus-like particles. Nucleic Acids Res 22(22):4560-5