دورية أكاديمية

Special Issue "Structure, Activity, and Function of Protein Methyltransferases".

التفاصيل البيبلوغرافية
العنوان: Special Issue "Structure, Activity, and Function of Protein Methyltransferases".
المؤلفون: Dhayalan, Arunkumar1 (AUTHOR) arun.dbt@pondiuni.edu.in, Jeltsch, Albert2 (AUTHOR) arun.dbt@pondiuni.edu.in
المصدر: Life (2075-1729). Mar2022, Vol. 12 Issue 3, p405-N.PAG. 4p.
مصطلحات موضوعية: *METHYLTRANSFERASES, *PROTEIN arginine methyltransferases, *PROTEINS, *POST-translational modification
مستخلص: Protein methylation mainly occurs at lysine and arginine residues and is catalyzed by protein lysine methyltransferases (PKMTs) and protein arginine methyltransferases (PRMTs), respectively. (A) Schema depicting the methylation of proteins by various PMTs at lysine (K), arginine (R), and histidine (H) residues. Methylation also controls the activity of numerous non-histone proteins [[2], [4]], where it often plays key roles in the regulation of their (i) stability, (ii) enzymatic activity, (iii) sub-cellular distribution, and (iv) interactions with other proteins. A PubMed search for the terms "methylation" AND "lysine", "methylation" AND "arginine", or "methylation" AND "histidine" resulted in 622, 202 and 20 publications, respectively, for the year 2021 alone, suggesting that protein methylation research is a very exciting and active area of research. [Extracted from the article]
قاعدة البيانات: Academic Search Index
الوصف
تدمد:20751729
DOI:10.3390/life12030405