New Results
Purification of the mammalian NgBR/hCIT cis-prenyltransferase complex: Identification of a conserved carboxyterminal RxG motif crucial for enzymatic activity
Kariona A. Grabińska, Ban H. Edani, Eon Joo Park, Jan R. Kraehling, View ORCID ProfileWilliam C. Sessa
doi: https://doi.org/10.1101/139675
Kariona A. Grabińska
Department of Pharmacology and Vascular Biology and Therapeutics Program (VBT), Yale University School of Medicine, New Haven, CT 06520, USA
Ban H. Edani
Department of Pharmacology and Vascular Biology and Therapeutics Program (VBT), Yale University School of Medicine, New Haven, CT 06520, USA
Eon Joo Park
Department of Pharmacology and Vascular Biology and Therapeutics Program (VBT), Yale University School of Medicine, New Haven, CT 06520, USA
Jan R. Kraehling
Department of Pharmacology and Vascular Biology and Therapeutics Program (VBT), Yale University School of Medicine, New Haven, CT 06520, USA
William C. Sessa
Department of Pharmacology and Vascular Biology and Therapeutics Program (VBT), Yale University School of Medicine, New Haven, CT 06520, USA
Article usage
Posted May 18, 2017.
Purification of the mammalian NgBR/hCIT cis-prenyltransferase complex: Identification of a conserved carboxyterminal RxG motif crucial for enzymatic activity
Kariona A. Grabińska, Ban H. Edani, Eon Joo Park, Jan R. Kraehling, William C. Sessa
bioRxiv 139675; doi: https://doi.org/10.1101/139675
Subject Area
Subject Areas
- Biochemistry (13349)
- Bioengineering (10169)
- Bioinformatics (32519)
- Biophysics (16733)
- Cancer Biology (13818)
- Cell Biology (19633)
- Clinical Trials (138)
- Developmental Biology (10618)
- Ecology (15716)
- Epidemiology (2067)
- Evolutionary Biology (20020)
- Genetics (13215)
- Genomics (18345)
- Immunology (13453)
- Microbiology (31486)
- Molecular Biology (13116)
- Neuroscience (68630)
- Paleontology (508)
- Pathology (2127)
- Pharmacology and Toxicology (3668)
- Physiology (5723)
- Plant Biology (11764)
- Synthetic Biology (3301)
- Systems Biology (8025)
- Zoology (1812)