Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Protein arginine methyltransferase 8"'
Publikováno v:
BMB Reports
Arginine methylation plays crucial roles in many cellular functions including signal transduction, RNA transcription, and regulation of gene expression. Protein arginine methyltransferase 8 (PRMT8), a unique brain-specific protein, is localized to th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6805c4c66d2bf4c8cbbc97f0f6720bb
https://doi.org/10.5483/bmbrep.2019.52.10.272
https://doi.org/10.5483/bmbrep.2019.52.10.272
Autor:
Chuck T. Chen, Celeste Yin-Chieh Wu, Garrett A. Clemons, Reggie Hui-Chao Lee, Hung Wen Lin, Jennifer I. Brown, Harlee E. Possoit, Christina H. Acosta, Alexandre Couto e Silva, Cristiane T. Citadin, Adam Frankel
Publikováno v:
J Neurochem
Protein arginine methyltransferases (PRMTs) are a family of enzymes involved in gene regulation and protein/histone modifications. PRMT8 is primarily expressed in the central nervous system, specifically within the cellular membrane and synaptic vesi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22c9591aa173a6bc875f6578c62eca10
https://pubmed.ncbi.nlm.nih.gov/34216036
https://pubmed.ncbi.nlm.nih.gov/34216036
Autor:
Joong-Gon Shin, Jee Wook Kim, Ihn-Geun Choi, Byung Lae Park, Young Min Choe, Hyung-Doo Shin, Boung Chul Lee
Publikováno v:
Neuropsychiatric Disease and Treatment. 15:83-94
Background Alcohol dependence (AD) is a common disorder that is influenced by genetic as well as environmental factors. A previous genome-wide association study (GWAS) of the Korean population performed by our research group identified a number of ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f5ccc60cfc600b7085b22fa4d749b072
https://doi.org/10.2147/ndt.s184067
https://doi.org/10.2147/ndt.s184067
Publikováno v:
Journal of Cancer
Objective: Cancer stem cells play a crucial role in tumor multidrug resistance and metastasis, which can produce heterogeneous tumor cells and have self-renewal ability. The related literature reported that PRMT8 was overexpressed in tumor stem cells
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aac79e61167bdca95df69860d687d0a6
http://europepmc.org/articles/PMC5929084
http://europepmc.org/articles/PMC5929084
Autor:
María Soledad Cosentino, Claudia Solari, Camila Vazquez Echegaray, Alina Grisel Sassone, Lino Barañao, Ariel Waisman, Marcos Francia, Jesica R. Canizo, Gustavo Sevlever, María Victoria Petrone, Alejandra Guberman, Carlos Luzzani, Santiago Gabriel Miriuka
Publikováno v:
Biochemical and Biophysical Research Communications. 473:194-199
Addition of methyl groups to arginine residues is catalyzed by a group of enzymes called Protein Arginine Methyltransferases (Prmt). Although Prmt1 is essential in development, its paralogue Prmt8 has been poorly studied. This gene was reported to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c03e3ef3b04ac5391eba7ce002d1fcbc
https://doi.org/10.1016/j.bbrc.2016.03.077
https://doi.org/10.1016/j.bbrc.2016.03.077
Autor:
Zoltán Papp, Tibor Hortobágyi, Zoltán Fekécs, Zsuzsanna Kolostyak, James J. Hickman, Antal Nógrádi, Xiufang Guo, Laszlo Nagy, Attila Pap, Bálint Rehó, György Vámosi, Dorothee Dormann, Gerardo Alvarado Contreras, Katalin Karolyi, Attila Horvath, Lu Lin Jiang, Huaxi Xu, Krisztián Pajer, Miklós Antal, Tatiana Sieler, Greta Kiss, Andreas Patsalos, Zsolt Keresztessy, Zsanett Sári, Zoltan Simandi
Aging contributes to cellular stress and neurodegeneration. Our understanding is limited regarding the tissue-restricted mechanisms providing protection in postmitotic cells throughout life. Here, we show that spinal cord motoneurons exhibit a high a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccc776efdc758edc2ca602d142b6c68c
https://europepmc.org/articles/PMC6113905/
https://europepmc.org/articles/PMC6113905/
Autor:
Tsutomu Matsui, Hao Hu, Meng-Chiao Ho, Wen-Hsuan W. Lin, Eric S.-W. Chen, Wei-Chao Lee, Yujun George Zheng, Ming-Daw Tsai, Tong-You Wade Wei, Wen-Ling Lin
Publikováno v:
Biochemistry
Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric dimethylation of various proteins, and their dysregulations often correlate with tumorigenesis or developmental deficiency. Recent studies have focused on the in vivo substrate id
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6935b91b6809e7a73378321de4e2e7cb
https://doi.org/10.1021/acs.biochem.5b00995
https://doi.org/10.1021/acs.biochem.5b00995
Autor:
Jinsoo Seo, Jay Penney, Li-Huei Tsai, Sara Elmsaouri, Oleg Kritskiy, Susan Chih-Chieh Su, Ping-Chieh Pao, Fan Gao
Publikováno v:
Society for Neuroscience
Diverse molecular mechanisms regulate synaptic composition and function in the mammalian nervous system. The multifunctional protein arginine methyltransferase 8 (PRMT8) possesses both methyltransferase and phospholipase activities. Here we examine t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a529b2dd344c5328ed922c09c4fa867b
https://europepmc.org/articles/PMC5588459/
https://europepmc.org/articles/PMC5588459/
Recent emphasis has been placed on the role of epigenetic regulators and epigenetic marks as biomarkers for cancer diagnosis and prognosis, and as therapeutic targets for treatment. One such class of regulators is the protein arginine methyltransfera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee2c2067cdedc776ef313dd5f9902fc7
https://europepmc.org/articles/PMC5403539/
https://europepmc.org/articles/PMC5403539/
Publikováno v:
Journal of Biological Chemistry. 282:36444-36453
Human protein arginine methyltransferase PRMT8 has been recently described as a type I enzyme in brain that is localized to the plasma membrane by N-terminal myristoylation. The amino acid sequence of human PRMT8 is almost 80% identical to human PRMT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f76d1b4969c31127eea6954740505a55
https://doi.org/10.1074/jbc.m704650200
https://doi.org/10.1074/jbc.m704650200