05077nam 2201489z- 450 991056647960332120220506(CKB)5680000000037584(oapen)https://directory.doabooks.org/handle/20.500.12854/81233(oapen)doab81233(EXLCZ)99568000000003758420202205d2022 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierStructure, Activity, and Function of Protein MethyltransferasesBaselMDPI - Multidisciplinary Digital Publishing Institute20221 online resource (292 p.)3-0365-4139-X 3-0365-4140-3 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 end methyltransferases. The topics covered in the individual reviews include structural aspects (domain architecture, homologs and paralogs, and structure), biochemical properties (mechanism, sequence specificity, product specificity, regulation, and histone and non-histone substrates), cellular features (subcellular localization, expression patterns, cellular roles and function, biological effects of substrate protein methylation, connection to cell signaling pathways, and connection to chromatin regulation) and their role in diseases. This review book is a useful resource for scientists working on protein methylation and protein methyltransferases and those interested in joining this emerging research field.BiochemistrybicsscBiology, life sciencesbicsscResearch & information: generalbicsscactinactin cytoskeletonAMLarginine methylationcancercardiovascular diseasecell proliferationcell signalingchromatin regulationcongenital heart diseasescytoskeletondendritic spinediabetesdiseaseDNA damage repairdystoniaeEF1AEHMT1EHMT2enterovirusesenzyme regulationenzyme specificityepigeneticsG9aGLPGTPaseH3K36H3K36me2H3K4me3H3K9 methylationH3R2me2aH4R3 methylationheterochromatinhistoneHsmar1Huntington's diseaseimmunityinflammationinflammatory bowel diseaselysine methylationlysine-specific methyltransferase (PKMT)methyltransferaseMetnaseMETTL13MLL2N-terminal methylationn/aneurodegenerative diseasesneuronNHEJnon-homologous end joining repairNSD1NSD3NUP98-NSD1oncogenesisPKMTpluripotencypolymerizationpost translational modificationpost-translational modificationpost-translational protein modificationposttranslational modificationsPrader-Willi syndromePRMT1PRMT2PRMT5PRMT6PRMT7protein arginine methylationprotein histidine methylationprotein lysine methylationprotein post-translational modificationRett syndromeschizophreniaSET7/9SETD3SETD7SETDB1SETMARSH3SOTOSstress responsestructurestructure and functionsynapsetranscriptional regulationtranslationtransposable elementstransposaseWHSC1L1BiochemistryBiology, life sciencesResearch & information: generalJeltsch Albertedt1265472Dhayalan ArunkumaredtJeltsch AlbertothDhayalan ArunkumarothBOOK9910566479603321Structure, Activity, and Function of Protein Methyltransferases3031722UNINA