Biochemical Analysis of Arginine Methylation in Transcription

التفاصيل البيبلوغرافية
العنوان: Biochemical Analysis of Arginine Methylation in Transcription
المؤلفون: Tini, Marc, Naeem, Hina, Torchia, Joseph
المصدر: Physiology and Pharmacology Publications
بيانات النشر: Scholarship@Western
سنة النشر: 2008
المجموعة: The University of Western Ontario: Scholarship@Western
مصطلحات موضوعية: Animals, Antibody Specificity, Arginine, Baculoviridae, Biochemistry, Biological Assay, Biotinylation, Cell Extracts, Chromatin Immunoprecipitation, Histone Acetyltransferases, Humans, Mass Spectrometry, Methylation, Methyltransferases, Nuclear Receptor Coactivator 3, Peptides, Protein-Arginine N-Methyltransferases, Recombinant Fusion Proteins, Staining and Labeling, Trans-Activators, Transcription, Genetic, Medical Biochemistry, Medical Physiology
الوصف: Protein arginine methylation has emerged as an important mechanism for regulating the functions of proteins involved in diverse aspects of gene regulation such as transcriptional activation and repression, mRNA processing and nuclear-cytoplasmic shuttling. This modification is catalyzed by the PRMT family of enzymes which utilize intracellular S-adenosyl methionine as a cofactor to dimethylate-specific arginines found within many target proteins.The establishment of in vitro biochemical assays as well as the development of modification-specific antibodies, and more recently mass spectrometry, have increased our understanding of the mechanism of catalysis of the PRMT family of enzymes. In the following discussion, we present some of the more commonly used in vivo and in vitro techniques which can be utilized to study the mechanism of arginine methylation and its role in transcription.
نوع الوثيقة: book part
اللغة: unknown
العلاقة: https://ir.lib.uwo.ca/physpharmpub/24Test
DOI: 10.1007/978-1-59745-190-1_16
الإتاحة: https://doi.org/10.1007/978-1-59745-190-1_16Test
https://ir.lib.uwo.ca/physpharmpub/24Test
رقم الانضمام: edsbas.323810F3
قاعدة البيانات: BASE