LSM2/YBL026W Literature Guide Help

Other names published for LSM2: SMX5, SNP3, YBL026W

LSM2 - Primary Literature (26)

ReferenceOther Genes Addressed
Nadler-Holly M, et al.  (2012) Interactions of subunit CCT3 in the yeast chaperonin CCT/TRiC with Q/N-rich proteins revealed by high-throughput microscopy analysis. Proc Natl Acad Sci U S A 109(46):18833-8
Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
Galao RP, et al.  (2010) LSm1-7 complexes bind to specific sites in viral RNA genomes and regulate their translation and replication. RNA 16(4):817-27
Sobti M, et al.  (2010) Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA. Biochemistry 49(11):2335-45
Chowdhury A and Tharun S  (2008) lsm1 mutations impairing the ability of the Lsm1p-7p-Pat1p complex to preferentially bind to oligoadenylated RNA affect mRNA decay in vivo. RNA 14(10):2149-58
Karaduman R, et al.  (2008) Structure of yeast U6 snRNPs: Arrangement of Prp24p and the LSm complex as revealed by electron microscopy. RNA 14(12):2528-2537
Reijns MA, et al.  (2008) A role for Q/N-rich aggregation-prone regions in P-body localization. J Cell Sci 121(Pt 15):2463-72
Tharun S  (2008) Purification and analysis of the decapping activator Lsm1p-7p-Pat1p complex from yeast. Methods Enzymol 448:41-55
Chowdhury A, et al.  (2007) The decapping activator Lsm1p-7p-Pat1p complex has the intrinsic ability to distinguish between oligoadenylated and polyadenylated RNAs. RNA 13(7):998-1016
Garrey SM, et al.  (2006) An extended RNA binding site for the yeast branch point-binding protein and the role of its zinc knuckle domains in RNA binding. J Biol Chem 281(37):27443-53
Fernandez CF, et al.  (2004) An Lsm2-Lsm7 complex in Saccharomyces cerevisiae associates with the small nucleolar RNA snR5. Mol Biol Cell 15(6):2842-52
Kufel J, et al.  (2004) Nuclear pre-mRNA decapping and 5' degradation in yeast require the Lsm2-8p complex. Mol Cell Biol 24(21):9646-57
Kufel J, et al.  (2003) Lsm Proteins are required for normal processing and stability of ribosomal RNAs. J Biol Chem 278(4):2147-56
Kufel J, et al.  (2002) Lsm proteins are required for normal processing of pre-tRNAs and their efficient association with La-homologous protein Lhp1p. Mol Cell Biol 22(14):5248-56
Ryan DE, et al.  (2002) The 5' and 3' domains of yeast U6 snRNA: Lsm proteins facilitate binding of Prp24 protein to the U6 telestem region. RNA 8(8):1011-33
He W and Parker R  (2001) The yeast cytoplasmic LsmI/Pat1p complex protects mRNA 3' termini from partial degradation. Genetics 158(4):1445-55
Pannone BK, et al.  (2001) Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics 158(1):187-96
Stevens SW, et al.  (2001) Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae. RNA 7(11):1543-53
Bouveret E, et al.  (2000) A Sm-like protein complex that participates in mRNA degradation. EMBO J 19(7):1661-71
Fromont-Racine M, et al.  (2000) Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins. Yeast 17(2):95-110
Tharun S, et al.  (2000) Yeast Sm-like proteins function in mRNA decapping and decay. Nature 404(6777):515-8
Gottschalk A, et al.  (1999) Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6.U5] tri-snRNP. EMBO J 18(16):4535-48
Mayes AE, et al.  (1999) Characterization of Sm-like proteins in yeast and their association with U6 snRNA. EMBO J 18(15):4321-31
Salgado-Garrido J, et al.  (1999) Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J 18(12):3451-62
Stevens SW and Abelson J  (1999) Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins. Proc Natl Acad Sci U S A 96(13):7226-31
Seraphin B  (1995) Sm and Sm-like proteins belong to a large family: identification of proteins of the U6 as well as the U1, U2, U4 and U5 snRNPs. EMBO J 14(9):2089-98