Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C‐terminal CXXM motif - Vorburger, K.; Kitten, G.T.; Nigg, E.A. (The EMBO journal, 1989)
Keywords: Animals; Biological and medical sciences; Cell-Free System; Cells, Cultured; Chick Embryo; Cysteine; DNA - genetics; Fibroblasts - metabolism; Fundamental and applied biological sciences. Psychology; Lamin Type A; Lamin Type B; Lamins; Mevalonic Acid - metabolism; Molecular and cellular biology; Molecular genetics; Mutation; Nuclear Proteins - biosynthesis; Nuclear Proteins - genetics; Peptide Mapping; Protein Biosynthesis; Protein Processing, Post-Translational; Protein-Tyrosine Kinases - genetics; Proto-Oncogene Proteins - genetics; Proto-Oncogene Proteins p21(ras); Reticulocytes - metabolism; Skin - metabolism; Transcription, Genetic; Transcription. Transcription factor. Splicing. Rna processing; Cell culture; Molecular processing; In vitro translation; Radiolabelling; Gel electrophoresis; Site directed mutagenesis; Posttranslational modification; Proteins; C terminal-Sequence; Peptide map; Vertebrata; Immunoprecipitation reaction; Complementary DNA; Structure activity relation; Proteolysis; Chicken; Reticulocyte; Aves