Structure, Activity, and Function of Protein Methyltransferases

• Другие авторы: Jeltsch, Albert (Редактор), Dhayalan, Arunkumar (Редактор)
• Формат: Электронный ресурс Глава книги
• Язык: английский
• Опубликовано: Basel MDPI - Multidisciplinary Digital Publishing Institute 2022
• Предметы: Research & information: general; Biology, life sciences; Biochemistry; protein lysine methylation; H3K9 methylation; PKMT; enzyme specificity; enzyme regulation; heterochromatin; protein post-translational modification; NSD3; WHSC1L1; structure and function; protein arginine methylation; PRMT7; epigenetics; cancer; immunity; pluripotency; SETDB1; methyltransferase; schizophrenia; Huntington's disease; Rett syndrome; Prader-Willi syndrome; congenital heart diseases; inflammatory bowel disease; MLL2; structure; H3K4me3; chromatin regulation; disease; dystonia; NSD1; H3K36; SOTOS; NUP98-NSD1; AML; PRMT6; post-translational modification; H3R2me2a; SETD3; posttranslational modifications; protein histidine methylation; actin; polymerization; cytoskeleton; enteroviruses; oncogenesis; PRMT5; cardiovascular disease; neurodegenerative diseases; diabetes; inflammation; G9a; GLP; EHMT2; EHMT1; post translational modification; lysine methylation; N-terminal methylation; translation; eEF1A; METTL13; neuron; synapse; dendritic spine; actin cytoskeleton; GTPase; PRMT1; arginine methylation; H4R3 methylation; transcriptional regulation; cell signaling; DNA damage repair; PRMT2; SH3; SETMAR; Metnase; H3K36me2; Hsmar1; non-homologous end joining repair; NHEJ; transposase; transposable elements; histone; SET7/9; SETD7; lysine-specific methyltransferase (PKMT); cell proliferation; stress response; post-translational protein modification; n/a
• Online-ссылка: DOAB: download the publication; DOAB: description of the publication

This collection of review articles describes the structure, function and mechanism of individual protein methyltransferase enzymes including protein lysine methyltransferases, protein arginine methyltransferases, and also the less abundant protein histidine methyltransferases and protein N-terminal...