Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Alessandra Di Lorenzo"'
Autor:
Rama Kamesh Bikkavilli, Robert A. Winn, Vineet Gupta, Mark T. Bedford, Odile David, Alessandra Di Lorenzo, Jianqiang Bao, Michelle Van Scoyk, Su Yanlin, Samia Q. Khan, Pei-Ying Wu, Sreedevi Avasarala
List of PRMT6-associated proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d507490a4a476755a0aa0f2a9e198be
https://doi.org/10.1158/1541-7786.22517968
https://doi.org/10.1158/1541-7786.22517968
Autor:
Rama Kamesh Bikkavilli, Robert A. Winn, Vineet Gupta, Mark T. Bedford, Odile David, Alessandra Di Lorenzo, Jianqiang Bao, Michelle Van Scoyk, Su Yanlin, Samia Q. Khan, Pei-Ying Wu, Sreedevi Avasarala
Supplementary Figure 1. Increased expression of PRMT6 in non-small cell lung cancer.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dd408a96f7d67b49f15b1175c05bb99
https://doi.org/10.1158/1541-7786.22517971.v1
https://doi.org/10.1158/1541-7786.22517971.v1
Autor:
Rama Kamesh Bikkavilli, Robert A. Winn, Vineet Gupta, Mark T. Bedford, Odile David, Alessandra Di Lorenzo, Jianqiang Bao, Michelle Van Scoyk, Su Yanlin, Samia Q. Khan, Pei-Ying Wu, Sreedevi Avasarala
List of primers
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b533c2a6de733705a8bbd84017492a2
https://doi.org/10.1158/1541-7786.22517965.v1
https://doi.org/10.1158/1541-7786.22517965.v1
Autor:
Mark T. Bedford, Michelle Van Scoyk, Vineet Gupta, Rama Kamesh Bikkavilli, Odile David, Robert A. Winn, Alessandra Di Lorenzo, Samia Q. Khan, Su Yanlin, Pei Ying Wu, Jianqiang Bao, Sreedevi Avasarala
Publikováno v:
Mol Cancer Res
Increased expression of protein arginine methyl transferase 6 (PRMT6) correlates with worse prognosis in lung cancer cases. To interrogate the in vivo functions of PRMT6 in lung cancer, we developed a tamoxifen-inducible lung-targeted PRMT6 gain-of-f
Autor:
Yi Zhong, Alessandra Di Lorenzo, Manu M. Sebastian, Yue Lu, Yanzhong Yang, Mark T. Bedford, Kevin Lin, William J. Muller, Jianqiang Bao
Publikováno v:
Cancer Research. 79:21-32
Protein arginine methyltransferases (PRMT) are generally not mutated in diseased states, but they are overexpressed in a number of cancers, including breast cancer. To address the possible roles of PRMT overexpression in mammary gland tumorigenesis,
Autor:
Mark T. Bedford, Sandrine Jayne, Guozhen Gao, Michael O. Hottiger, Donghang Cheng, Alessandra Di Lorenzo, Stéphane Richard
Publikováno v:
J Biol Chem
CARM1 is a protein arginine methyltransferase (PRMT) that acts as a coactivator in a number of transcriptional programs. CARM1 orchestrates this coactivator activity in part by depositing the H3R17me2a histone mark in the vicinity of gene promoters t
Publikováno v:
Nucleic Acids Research
Protein arginine methyltransferase 6 (PRMT6) is a nuclear enzyme that modifies histone tails. To help elucidate the biological function of PRMT6 in vivo, we generated transgenic mice that ubiquitously express PRMT6 fused to the hormone-binding portio
Loss of the major Type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTs
Autor:
Surbhi Dhar, Michael J. Comb, Grace L. Huang, Mark T. Bedford, Ailan Guo, Alexander N. Patananan, Alessandra Di Lorenzo, Stéphane Richard, Vidyasiri Vemulapalli, Steven Clarke
Publikováno v:
Scientific Reports
Arginine methylation is a common posttranslational modification that is found on both histone and non-histone proteins. Three types of arginine methylation exist in mammalian cells: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA) and sym
Autor:
Alessandra Di Lorenzo, Mark T. Bedford
Publikováno v:
FEBS Letters. (13):2024-2031
Arginine methylation is a common posttranslational modification (PTM). This type of PTM occurs on both nuclear and cytoplasmic proteins, and is particularly abundant on shuttling proteins. In this review, we will focus on one aspect of this PTM: the