Parvulin (Par14), a Peptidyl-Prolyl cis-trans Isomerase, Is a Novel rRNA Processing Factor That Evolved in the Metazoan Lineage

This publication has 27 references indexed in Scilit:

• Mitotic occupancy and lineage-specific transcriptional control of rRNA genes by Runx2
  Nature, 2007
• Cell Surface Labeling and Mass Spectrometry Reveal Diversity of Cell Surface Markers and Signaling Molecules Expressed in Undifferentiated Mouse Embryonic Stem Cells
  Molecular & Cellular Proteomics, 2005
• STEM: A Software Tool for Large-Scale Proteomic Data Analyses
  Journal of Proteome Research, 2005
• Cytokinesis: The Central Spindle Takes Center Stage
  Current Biology, 2004
• NMR solution structure of h Par14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator h Pin1 but indicates a different functionality of the protein 1 1Edited by A. Fersht
  Journal of Molecular Biology, 2000
• Identification of Eukaryotic Parvulin Homologues: A New Subfamily of Peptidylprolyl cis–trans Isomerases
  Biochemical and Biophysical Research Communications, 1999
• Expanding the Eukaryote's Cast of Chaperones
  Science, 1996
• Components of the Nucleolar Processing Complex (Pre-rRNA, Fibrillarin, and Nucleolin) Colocalize during Mitosis and Are Incorporated to Daughter Cell Nucleoli
  Experimental Cell Research, 1995
• Fate of specific nucleolar perichromosomal proteins during mitosis: Cellular distribution and association with U3 snoRNA
  Biology of the Cell, 1994
• A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin
  Nature, 1989