Structure, Activity, and Function of Protein Methyltransferases
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...
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| Year of Publication: | 2022 |
| Language: | English |
| Physical Description: | 1 electronic resource (292 p.) |
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| 100 | 1 | |a Jeltsch, Albert |4 edt | |
| 245 | 1 | 0 | |a Structure, Activity, and Function of Protein Methyltransferases |
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| 300 | |a 1 electronic resource (292 p.) | ||
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| 520 | |a 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. | ||
| 546 | |a English | ||
| 650 | 7 | |a Research & information: general |2 bicssc | |
| 650 | 7 | |a Biology, life sciences |2 bicssc | |
| 650 | 7 | |a Biochemistry |2 bicssc | |
| 653 | |a protein lysine methylation | ||
| 653 | |a H3K9 methylation | ||
| 653 | |a PKMT | ||
| 653 | |a enzyme specificity | ||
| 653 | |a enzyme regulation | ||
| 653 | |a heterochromatin | ||
| 653 | |a protein post-translational modification | ||
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| 653 | |a WHSC1L1 | ||
| 653 | |a structure and function | ||
| 653 | |a protein arginine methylation | ||
| 653 | |a PRMT7 | ||
| 653 | |a epigenetics | ||
| 653 | |a cancer | ||
| 653 | |a immunity | ||
| 653 | |a pluripotency | ||
| 653 | |a SETDB1 | ||
| 653 | |a methyltransferase | ||
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| 653 | |a Huntington's disease | ||
| 653 | |a Rett syndrome | ||
| 653 | |a Prader-Willi syndrome | ||
| 653 | |a congenital heart diseases | ||
| 653 | |a inflammatory bowel disease | ||
| 653 | |a MLL2 | ||
| 653 | |a structure | ||
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| 653 | |a chromatin regulation | ||
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| 653 | |a H3K36 | ||
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| 653 | |a protein histidine methylation | ||
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| 653 | |a lysine methylation | ||
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| 653 | |a GTPase | ||
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| 653 | |a arginine methylation | ||
| 653 | |a H4R3 methylation | ||
| 653 | |a transcriptional regulation | ||
| 653 | |a cell signaling | ||
| 653 | |a DNA damage repair | ||
| 653 | |a PRMT2 | ||
| 653 | |a SH3 | ||
| 653 | |a SETMAR | ||
| 653 | |a Metnase | ||
| 653 | |a H3K36me2 | ||
| 653 | |a Hsmar1 | ||
| 653 | |a non-homologous end joining repair | ||
| 653 | |a NHEJ | ||
| 653 | |a transposase | ||
| 653 | |a transposable elements | ||
| 653 | |a histone | ||
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| 776 | |z 3-0365-4139-X | ||
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| 700 | 1 | |a Dhayalan, Arunkumar |4 edt | |
| 700 | 1 | |a Jeltsch, Albert |4 oth | |
| 700 | 1 | |a Dhayalan, Arunkumar |4 oth | |
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