Preferential Modification of Nuclear Proteins by a Novel Ubiquitin-like Molecule
Open Access
- 1 May 1997
- journal article
- Published by Elsevier
- Vol. 272 (22), 14001-14004
- https://doi.org/10.1074/jbc.272.22.14001
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.The Journal of cell biology, 1996
- Protein Degradation or Regulation: Ub the JudgeCell, 1996
- Nucleocytoplasmic TransportScience, 1996
- Conjugation of the 15-kDa Interferon-induced Ubiquitin Homolog Is Distinct from That of UbiquitinJournal of Biological Chemistry, 1996
- Cyclin Ubiquitination: The destructive end of mitosisCell, 1995
- MIF2 is required for mitotic spindle integrity during anaphase spindle elongation in Saccharomyces cerevisiae.The Journal of cell biology, 1993
- THE UBIQUITIN-CONJUGATION SYSTEMAnnual Review of Genetics, 1992
- THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATIONAnnual Review of Biochemistry, 1992
- An antibody reacting with splenic red pulp macrophages in the sera of patients with rheumatic diseasesClinical Immunology and Immunopathology, 1991
- The yeast RNA1 gene product necessary for RNA processing is located in the cytosol and apparently excluded from the nucleus.The Journal of cell biology, 1990