The human homologue of the yeast splicing factor prp6p contains multiple TPR elements and is stably associated with the U5 snRNP via protein-protein interactions

This publication has 23 references indexed in Scilit:

• Functional interaction of a novel 15.5kD [U4/U6middle dotU5] tri-snRNP protein with the 5' stem-loop of U4 snRNA
  The EMBO Journal, 1999
• 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
  The EMBO Journal, 1999
• Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6middle dotU5] tri-snRNP
  The EMBO Journal, 1999
• Functional and structural characterization of the Prp3 binding domain of the yeast Prp4 splicing factor
  Journal of Molecular Biology, 1998
• The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions
  The EMBO Journal, 1998
• An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2
  The EMBO Journal, 1997
• Identification of an RNA-Dependent ATPase Activity in Mammalian U5 snRNPs
  Nucleic Acids Research, 1996
• The biochemical defects ofprp4-1andprp6-1yeast splicing mutants reveal that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP
  Nucleic Acids Research, 1993
• Immunoaffinity purification of a [U4/U6.U5] tri-snRNP from human cells.
  Genes & Development, 1991
• A repeating amino acid motif in CDC23 defines a family of proteins and a new relationship among genes required for mitosis and RNA synthesis
  Cell, 1990