- LSM2
LSM2 homolog, U6 small nuclear RNA associated (S. cerevisiae), also known as LSM2, is a human
gene .cite web | title = Entrez Gene: LSM2 LSM2 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57819| accessdate = ]PBB_Summary
section_title =
summary_text = Sm-like proteins were identified in a variety of organisms based on sequence homology with the Sm protein family (see SNRPD2; MIM 601061). Sm-like proteins contain the Sm sequence motif, which consists of 2 regions separated by a linker of variable length that folds as a loop. The Sm-like proteins are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. [supplied by OMIM] cite web | title = Entrez Gene: LSM2 LSM2 homolog, U6 small nuclear RNA associated (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57819| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Olavesen MG, Snoek M, Campbell RD |title=Localization of a new gene adjacent to the HSP70 genes in human and mouse MHCs. |journal=Immunogenetics |volume=37 |issue= 5 |pages= 394–6 |year= 1993 |pmid= 8428774 |doi=
*cite journal | author=Achsel T, Brahms H, Kastner B, "et al." |title=A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. |journal=EMBO J. |volume=18 |issue= 20 |pages= 5789–802 |year= 1999 |pmid= 10523320 |doi= 10.1093/emboj/18.20.5789
*cite journal | author=Charroux B, Pellizzoni L, Perkinson RA, "et al." |title=Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. |journal=J. Cell Biol. |volume=147 |issue= 6 |pages= 1181–94 |year= 2000 |pmid= 10601333 |doi=
*cite journal | author=Friesen WJ, Dreyfuss G |title=Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN). |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26370–5 |year= 2000 |pmid= 10851237 |doi= 10.1074/jbc.M003299200
*cite journal | author=Hu RM, Han ZG, Song HD, "et al." |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543–8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997
*cite journal | author=Eystathioy T, Peebles CL, Hamel JC, "et al." |title=Autoantibody to hLSm4 and the heptameric LSm complex in anti-Sm sera. |journal=Arthritis Rheum. |volume=46 |issue= 3 |pages= 726–34 |year= 2002 |pmid= 11920408 |doi= 10.1002/art.10220
*cite journal | author=Jurica MS, Licklider LJ, Gygi SR, "et al." |title=Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. |journal=RNA |volume=8 |issue= 4 |pages= 426–39 |year= 2002 |pmid= 11991638 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ingelfinger D, Arndt-Jovin DJ, Lührmann R, Achsel T |title=The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. |journal=RNA |volume=8 |issue= 12 |pages= 1489–501 |year= 2003 |pmid= 12515382 |doi=
*cite journal | author=Xie T, Rowen L, Aguado B, "et al." |title=Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. |journal=Genome Res. |volume=13 |issue= 12 |pages= 2621–36 |year= 2004 |pmid= 14656967 |doi= 10.1101/gr.1736803
*cite journal | author=Lehner B, Semple JI, Brown SE, "et al." |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153–67 |year= 2004 |pmid= 14667819 |doi=
*cite journal | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Rush J, Moritz A, Lee KA, "et al." |title=Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. |journal=Nat. Biotechnol. |volume=23 |issue= 1 |pages= 94–101 |year= 2005 |pmid= 15592455 |doi= 10.1038/nbt1046
*cite journal | author=Stelzl U, Worm U, Lalowski M, "et al." |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209PBB_Controls
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