PRMT1 is an important factor for medulloblastoma cell proliferation and survival

Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored. By examining the publicly available databases of pediatric brain tumor co...

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Published inBiochemistry and biophysics reports Vol. 32; p. 101364
Main Authors Gu, Xiao, He, Miao, Lebedev, Timofey, Lin, Cheng-Han, Hua, Zhong-Yan, Zheng, Y. George, Li, Zhi-Jie, Yang, Jer-Yen, Li, Xing-Guo
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LanguageEnglish
Published Netherlands Elsevier B.V 01.12.2022
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Abstract Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored. By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma. •PRMT1 is predominantly expressed in medulloblastoma among pediatric brain tumors and correlates with poor patient survival.•PRMT1 knockdown suppressed medulloblastoma cell growth and induced apoptosis.•The diamidine compounds reduced medulloblastoma cell viability and induced medulloblastoma cell apoptosis.
AbstractList Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored. By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma.Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored. By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma.
Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma.
Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored. By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma. •PRMT1 is predominantly expressed in medulloblastoma among pediatric brain tumors and correlates with poor patient survival.•PRMT1 knockdown suppressed medulloblastoma cell growth and induced apoptosis.•The diamidine compounds reduced medulloblastoma cell viability and induced medulloblastoma cell apoptosis.
Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored. By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma.
Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma, the most common malignant pediatric brain tumor, remains unexplored . By examining the publicly available databases of pediatric brain tumor collection, we found that PRMT1 was predominantly expressed in medulloblastomas across all the pediatric brain tumors and that the high-level expression of PRMT1 correlated with poor survival of medulloblastoma patients. To determine the role of PRMT1 in medulloblastoma cells, we established an inducible knockdown system and demonstrated that PRMT1 depletion decreased medulloblastoma cell proliferation and induced cell apoptosis. Furthermore, the diamidine compounds, previously shown to exhibit selective PRMT1 inhibition, suppressed medulloblastoma cell viability in a dose-dependent manner. Finally, we observed induction of medulloblastoma cell apoptosis by the potent diamidine compounds at low micromolar concentrations. Together, our results suggest that PRMT1 could be an actionable therapeutic target in medulloblastoma. • PRMT1 is predominantly expressed in medulloblastoma among pediatric brain tumors and correlates with poor patient survival. • PRMT1 knockdown suppressed medulloblastoma cell growth and induced apoptosis. • The diamidine compounds reduced medulloblastoma cell viability and induced medulloblastoma cell apoptosis.
ArticleNumber 101364
Author Li, Zhi-Jie
Lebedev, Timofey
Zheng, Y. George
Hua, Zhong-Yan
Lin, Cheng-Han
Li, Xing-Guo
He, Miao
Yang, Jer-Yen
Gu, Xiao
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10.1016/j.neo.2017.05.002
10.1007/s00018-019-03145-x
10.1186/s13046-019-1064-8
10.3390/cells10010124
10.1093/nar/gkz200
10.1038/s41389-020-0237-9
10.1038/s41598-019-52291-6
10.1016/j.ccell.2019.05.014
10.5483/BMBRep.2012.45.8.022
10.1021/acschemneuro.7b00258
10.1016/j.jbiotec.2016.07.028
10.3390/ijms22052622
10.1186/s12885-019-6291-z
10.3389/fonc.2020.00226
10.1039/C6MD00573J
10.1016/j.ccell.2019.07.003
10.1038/s41580-019-0155-x
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Keywords PRMT1 inhibitors
Diamidine compounds
Dox
PRMT1
shRNA
Medulloblastoma
Dox, Doxycycline
shRNA, short hairpin RNA
PRMT1, protein arginine methyltransferase 1
Language English
License This is an open access article under the CC BY-NC-ND license.
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References Chandrashekar, Bashel, Balasubramanya, Creighton, Rodriguez, Chakravarthi, Varambally (bib6) 2017 Aug; 19
Hansen, Li, Zheng, Lotta, Dedhe, Schor (bib13) 2017; 8
Ivanov, Coyle, Walker, Grabowska (bib10) 2016 Oct 20; 236
Gao, Zhang, Villarreal, He, Su, Bedford, Moh, Shen, Shi, Bedford, Xu (bib14) 2019 Jun 4; 47
Li, An, Xu, Lin, Su, Liu (bib18) 2019; 38
Ceccarelli, D'Andrea, Micheli, Tirone (bib5) 2020 Mar 13; 10
Northcott, Robinson, Kratz, Mabbott, Pomeroy, Clifford, Rutkowski, Ellison, Malkin, Taylor, Gajjar, Pfister (bib2) 2019 Feb 14; 5
Wang, Tan, Yang, Yin, Yuan, Qiang, Peng (bib9) 2012; 45
Chaturvedi, Mahapatra, Kesherwani, Kling, Shukla, Ray, Kanchan, Perumal, McGuire, Sharp, Joshi, Coulter (bib3) 2019 Nov 6; 19
Tewary, Zheng, Ho (bib8) 2019; 76
Favia, Salvatori, Nanni, Iwamoto-Stohl, Valente, Mai, Scagnoli, Fontanella, Totta, Nasi, Illi (bib17) 2019 Nov 4; 9
Ryu, Kim, Son, Min, Kim, Han (bib19) 2019; 41
Fedoriw, Rajapurkar, O'Brien, Gerhart, Mitchell, Adams, Rioux, Lingaraj, Ribich, Pappalardi, Shah, Laraio, Liu, Butticello, Carpenter, Creasy, Korenchuk, McCabe, McHugh, Nagarajan, Wagner, Zappacosta, Annan, Concha, Thomas, Hart, Smith, Copeland, Moyer, Campbell, Stickland, Mills, Jacques-O'Hagan, Allain, Johnston, Raimondi, Porter Scott, Waters, Swinger, Boriack-Sjodin, Riera, Shapiro, Chesworth, Prinjha, Kruger, Barbash, Mohammad (bib16) 2019 Jul 8; 36
Hua, Hansen, He, Dai, Choi, Fulton, Lloyd, Szemes, Sen, Ding, Angelastro, Fei, Li, Wu, Yang, Malik, Bao, George Zheng, Liu, Schor, Li, Li (bib4) 2020 May 15; 9
Guccione, Richard (bib11) 2019 Oct; 20
Zhang, Qian, Yan, He, Jassim, Ivanov, Zheng (bib12) 2017; 8
Fong, Pignata, Goy, Kawabata, Lee, Koh, Musiani, Massignani, Kotini, Penson, Wun, Shen, Schwarz, Low, Rialdi, Ki, Wollmann, Mzoughi, Gay, Thompson, Hart, Barbash, Luciani, Szewczyk, Wouters, Delwel, Papapetrou, Barsyte-Lovejoy, Arrowsmith, Minden, Jin, Melnick, Bonaldi, Abdel-Wahab, Guccione (bib15) 2019 Aug 12; 36
Bryant, Heiss, Banasavadi-Siddegowda (bib1) 2021 Jan 11; 10
Bartha, Győrffy (bib7) 2021 Mar 5; 22
Northcott (10.1016/j.bbrep.2022.101364_bib2) 2019; 5
Chaturvedi (10.1016/j.bbrep.2022.101364_bib3) 2019; 19
Zhang (10.1016/j.bbrep.2022.101364_bib12) 2017; 8
Ceccarelli (10.1016/j.bbrep.2022.101364_bib5) 2020; 10
Tewary (10.1016/j.bbrep.2022.101364_bib8) 2019; 76
Gao (10.1016/j.bbrep.2022.101364_bib14) 2019; 47
Guccione (10.1016/j.bbrep.2022.101364_bib11) 2019; 20
Favia (10.1016/j.bbrep.2022.101364_bib17) 2019; 9
Hua (10.1016/j.bbrep.2022.101364_bib4) 2020; 9
Fedoriw (10.1016/j.bbrep.2022.101364_bib16) 2019; 36
Wang (10.1016/j.bbrep.2022.101364_bib9) 2012; 45
Li (10.1016/j.bbrep.2022.101364_bib18) 2019; 38
Bartha (10.1016/j.bbrep.2022.101364_bib7) 2021; 22
Ivanov (10.1016/j.bbrep.2022.101364_bib10) 2016; 236
Hansen (10.1016/j.bbrep.2022.101364_bib13) 2017; 8
Fong (10.1016/j.bbrep.2022.101364_bib15) 2019; 36
Chandrashekar (10.1016/j.bbrep.2022.101364_bib6) 2017; 19
Ryu (10.1016/j.bbrep.2022.101364_bib19) 2019; 41
Bryant (10.1016/j.bbrep.2022.101364_bib1) 2021; 10
References_xml – volume: 9
  start-page: 50
  year: 2020 May 15
  ident: bib4
  article-title: PRMT1 promotes neuroblastoma cell survival through ATF5
  publication-title: Oncogenesis
– volume: 5
  start-page: 11
  year: 2019 Feb 14
  ident: bib2
  publication-title: Medulloblastoma. Nat Rev Dis Primers.
– volume: 45
  start-page: 470
  year: 2012
  end-page: 475
  ident: bib9
  article-title: The role of protein arginine-methyltransferase 1 in gliomagenesis
  publication-title: BMB Rep.
– volume: 36
  start-page: 100
  year: 2019 Jul 8
  end-page: 114.e25
  ident: bib16
  article-title: Anti-tumor activity of the type I PRMT inhibitor, GSK3368715, synergizes with PRMT5 inhibition through MTAP loss
  publication-title: Cancer Cell
– volume: 10
  start-page: 226
  year: 2020 Mar 13
  ident: bib5
  article-title: Deletion of Btg1 induces prmt1-dependent apoptosis and increased stemness in shh-type medulloblastoma cells without affecting tumor frequency
  publication-title: Front. Oncol.
– volume: 47
  start-page: 5038
  year: 2019 Jun 4
  end-page: 5048
  ident: bib14
  article-title: PRMT1 loss sensitizes cells to PRMT5 inhibition
  publication-title: Nucleic Acids Res.
– volume: 10
  start-page: 124
  year: 2021 Jan 11
  ident: bib1
  article-title: Arginine methylation in brain tumors: tumor biology and therapeutic strategies
  publication-title: Cells
– volume: 236
  start-page: 10
  year: 2016 Oct 20
  end-page: 25
  ident: bib10
  article-title: In vitro models of medulloblastoma: choosing the right tool for the job
  publication-title: J. Biotechnol.
– volume: 36
  start-page: 194
  year: 2019 Aug 12
  end-page: 209
  ident: bib15
  article-title: Therapeutic targeting of RNA splicing catalysis through inhibition of protein arginine methylation
  publication-title: Cancer Cell
– volume: 19
  start-page: 1056
  year: 2019 Nov 6
  ident: bib3
  article-title: Role of protein arginine methyltransferase 5 in group 3 (MYC-driven) Medulloblastoma
  publication-title: BMC Cancer
– volume: 8
  start-page: 2118
  year: 2017
  end-page: 2123
  ident: bib13
  article-title: Using chemistry to target neuroblastoma
  publication-title: ACS Chem. Neurosci.
– volume: 20
  start-page: 642
  year: 2019 Oct
  end-page: 657
  ident: bib11
  article-title: The regulation, functions and clinical relevance of arginine methylation
  publication-title: Nat. Rev. Mol. Cell Biol.
– volume: 38
  start-page: 64
  year: 2019
  ident: bib18
  article-title: The arginine methyltransferase PRMT5 and PRMT1 distinctly regulate the degradation of anti-apoptotic protein CFLAR(L) in human lung cancer cells
  publication-title: J. Exp. Clin. Cancer Res.
– volume: 8
  start-page: 440
  year: 2017
  end-page: 444
  ident: bib12
  article-title: Discovery of decamidine as a new and potent PRMT1 inhibitor
  publication-title: Medchemcomm
– volume: 19
  start-page: 649
  year: 2017 Aug
  end-page: 658
  ident: bib6
  article-title: UALCAN: a portal for facilitating tumor subgroup gene expression and survival analyses
  publication-title: Neoplasia
– volume: 76
  start-page: 2917
  year: 2019
  end-page: 2932
  ident: bib8
  article-title: Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level
  publication-title: Cell. Mol. Life Sci.
– volume: 22
  start-page: 2622
  year: 2021 Mar 5
  ident: bib7
  article-title: TNMplot.com: a web tool for the comparison of gene expression in normal, tumor and metastatic tissues
  publication-title: Int. J. Mol. Sci.
– volume: 9
  year: 2019 Nov 4
  ident: bib17
  article-title: The Protein Arginine Methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells
  publication-title: Sci. Rep.
– volume: 41
  start-page: 1691
  year: 2019
  end-page: 1699
  ident: bib19
  article-title: Downregulation of PRMT1, a histone arginine methyltransferase, by sodium propionate induces cell apoptosis in colon cancer
  publication-title: Oncol. Rep.
– volume: 5
  start-page: 11
  issue: 1
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib2
  publication-title: Medulloblastoma. Nat Rev Dis Primers.
  doi: 10.1038/s41572-019-0063-6
– volume: 19
  start-page: 649
  issue: 8
  year: 2017
  ident: 10.1016/j.bbrep.2022.101364_bib6
  article-title: UALCAN: a portal for facilitating tumor subgroup gene expression and survival analyses
  publication-title: Neoplasia
  doi: 10.1016/j.neo.2017.05.002
– volume: 41
  start-page: 1691
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib19
  article-title: Downregulation of PRMT1, a histone arginine methyltransferase, by sodium propionate induces cell apoptosis in colon cancer
  publication-title: Oncol. Rep.
– volume: 76
  start-page: 2917
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib8
  article-title: Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-019-03145-x
– volume: 38
  start-page: 64
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib18
  article-title: The arginine methyltransferase PRMT5 and PRMT1 distinctly regulate the degradation of anti-apoptotic protein CFLAR(L) in human lung cancer cells
  publication-title: J. Exp. Clin. Cancer Res.
  doi: 10.1186/s13046-019-1064-8
– volume: 10
  start-page: 124
  issue: 1
  year: 2021
  ident: 10.1016/j.bbrep.2022.101364_bib1
  article-title: Arginine methylation in brain tumors: tumor biology and therapeutic strategies
  publication-title: Cells
  doi: 10.3390/cells10010124
– volume: 47
  start-page: 5038
  issue: 10
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib14
  article-title: PRMT1 loss sensitizes cells to PRMT5 inhibition
  publication-title: Nucleic Acids Res.
  doi: 10.1093/nar/gkz200
– volume: 9
  start-page: 50
  issue: 5
  year: 2020
  ident: 10.1016/j.bbrep.2022.101364_bib4
  article-title: PRMT1 promotes neuroblastoma cell survival through ATF5
  publication-title: Oncogenesis
  doi: 10.1038/s41389-020-0237-9
– volume: 9
  issue: 1
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib17
  article-title: The Protein Arginine Methyltransferases 1 and 5 affect Myc properties in glioblastoma stem cells
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-019-52291-6
– volume: 36
  start-page: 100
  issue: 1
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib16
  article-title: Anti-tumor activity of the type I PRMT inhibitor, GSK3368715, synergizes with PRMT5 inhibition through MTAP loss
  publication-title: Cancer Cell
  doi: 10.1016/j.ccell.2019.05.014
– volume: 45
  start-page: 470
  year: 2012
  ident: 10.1016/j.bbrep.2022.101364_bib9
  article-title: The role of protein arginine-methyltransferase 1 in gliomagenesis
  publication-title: BMB Rep.
  doi: 10.5483/BMBRep.2012.45.8.022
– volume: 8
  start-page: 2118
  issue: 10
  year: 2017
  ident: 10.1016/j.bbrep.2022.101364_bib13
  article-title: Using chemistry to target neuroblastoma
  publication-title: ACS Chem. Neurosci.
  doi: 10.1021/acschemneuro.7b00258
– volume: 236
  start-page: 10
  year: 2016
  ident: 10.1016/j.bbrep.2022.101364_bib10
  article-title: In vitro models of medulloblastoma: choosing the right tool for the job
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2016.07.028
– volume: 22
  start-page: 2622
  issue: 5
  year: 2021
  ident: 10.1016/j.bbrep.2022.101364_bib7
  article-title: TNMplot.com: a web tool for the comparison of gene expression in normal, tumor and metastatic tissues
  publication-title: Int. J. Mol. Sci.
  doi: 10.3390/ijms22052622
– volume: 19
  start-page: 1056
  issue: 1
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib3
  article-title: Role of protein arginine methyltransferase 5 in group 3 (MYC-driven) Medulloblastoma
  publication-title: BMC Cancer
  doi: 10.1186/s12885-019-6291-z
– volume: 10
  start-page: 226
  year: 2020
  ident: 10.1016/j.bbrep.2022.101364_bib5
  article-title: Deletion of Btg1 induces prmt1-dependent apoptosis and increased stemness in shh-type medulloblastoma cells without affecting tumor frequency
  publication-title: Front. Oncol.
  doi: 10.3389/fonc.2020.00226
– volume: 8
  start-page: 440
  issue: 2
  year: 2017
  ident: 10.1016/j.bbrep.2022.101364_bib12
  article-title: Discovery of decamidine as a new and potent PRMT1 inhibitor
  publication-title: Medchemcomm
  doi: 10.1039/C6MD00573J
– volume: 36
  start-page: 194
  issue: 2
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib15
  article-title: Therapeutic targeting of RNA splicing catalysis through inhibition of protein arginine methylation
  publication-title: Cancer Cell
  doi: 10.1016/j.ccell.2019.07.003
– volume: 20
  start-page: 642
  issue: 10
  year: 2019
  ident: 10.1016/j.bbrep.2022.101364_bib11
  article-title: The regulation, functions and clinical relevance of arginine methylation
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-019-0155-x
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Snippet Aberrant expression of protein arginine methyltransferases (PRMTs) has been implicated in a number of brain tumors, but the role of PRMT1 in medulloblastoma,...
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SubjectTerms Diamidine compounds
Medulloblastoma
PRMT1
PRMT1 inhibitors
Title PRMT1 is an important factor for medulloblastoma cell proliferation and survival
URI https://dx.doi.org/10.1016/j.bbrep.2022.101364
https://www.ncbi.nlm.nih.gov/pubmed/36237442
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