scholarly journals Extensive and Varied Modifications in Histone H2B of Wild-Type and Histone Deacetylase 1 MutantNeurospora crassa

Biochemistry ◽  
2010 ◽  
Vol 49 (25) ◽  
pp. 5244-5257 ◽  
Author(s):  
D. C. Anderson ◽  
George R. Green ◽  
Kristina Smith ◽  
Eric U. Selker
Keyword(s):  
Histone Deacetylase ◽  
Wild Type ◽  
Histone H2b ◽  
Histone Deacetylase 1

scholarly journals Transcriptional repression ofAurora-Agene by wild-type p53 through directly binding to its promoter with histone deacetylase 1 and mSin3a

2017 ◽  
Vol 142 (1) ◽  
pp. 92-108
Author(s):  
Tsung-Ying Yang ◽  
Chieh-Lin Jerry Teng ◽  
Tsung-Chieh Chester Lin ◽  
Kun-Chieh Chen ◽  
Shih-Lan Hsu ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Transcriptional Repression ◽  
Wild Type ◽  
Histone Deacetylase 1 ◽  
Wild Type P53

scholarly journals 8a, a New Acridine Antiproliferative and Pro-Apoptotic Agent Targeting HDAC1/DNMT1

2021 ◽  
Vol 22 (11) ◽  
pp. 5516
Author(s):  
Qiting Zhang ◽  
Ziyan Wang ◽  
Xinyuan Chen ◽  
Haoxiang Qiu ◽  
Yifan Gu ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Dna Methyltransferase ◽  
Hdac Inhibitors ◽  
Mitochondrial Pathway ◽  
Epigenetic Therapy ◽  
Protein Interaction Data ◽  
Dependent Manner ◽  
Histone Deacetylase 1 ◽  
Histiocytic Lymphoma ◽  
Dose Dependent

Epigenetic therapy using histone deacetylase (HDAC) inhibitors has become an attractive project in new drug development. However, DNA methylation and histone acetylation are important epigenetic ways to regulate the occurrence and development of leukemia. Given previous studies, N-(2-aminophenyl)benzamide acridine (8a), as a histone deacetylase 1 (HDAC1) inhibitor, induces apoptosis and shows significant anti-proliferative activity against histiocytic lymphoma U937 cells. HDAC1 plays a role in the nucleus, which we confirmed by finding that 8a entered the nucleus. Subsequently, we verified that 8a mainly passes through the endogenous (mitochondrial) pathway to induce cell apoptosis. From the protein interaction data, we found that 8a also affected the expression of DNA methyltransferase 1 (DNMT1). Therefore, an experiment was performed to assess the binding of 8a to DNMT1 at the molecular and cellular levels. We found that the binding strength of 8a to DNMT1 enhanced in a dose-dependent manner. Additionally, 8a inhibits the expression of DNMT1 mRNA and its protein. These findings suggested that the anti-proliferative and pro-apoptotic activities of 8a against leukemia cells were achieved by targeting HDAC1 and DNMT1.

scholarly journals Crucial function of histone deacetylase 1 for differentiation of teratomas in mice and humans

2010 ◽  
Vol 29 (23) ◽  
pp. 3992-4007 ◽  
Author(s):  
Sabine Lagger ◽  
Dominique Meunier ◽  
Mario Mikula ◽  
Reinhard Brunmeir ◽  
Michaela Schlederer ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Histone Deacetylase 1

scholarly journals OP0194 HISTONE DEACETYLASE 1 (HDAC1): A KEY MEDIATOR OF T CELLS FOR THE PATHOGENESIS OF RHEUMATOID ARTHRITIS

2019 ◽  
Author(s):  
Lisa Göschl ◽  
Victoria Saferding ◽  
Nicole Boucheron ◽  
Johan Backlund ◽  
Alexander Platzer ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
T Cells ◽  
Histone Deacetylase ◽  
Histone Deacetylase 1

scholarly journals PAICS contributes to gastric carcinogenesis and participates in DNA damage response by interacting with histone deacetylase 1/2

2020 ◽  
Vol 11 (7) ◽  
Author(s):  
Nan Huang ◽  
Chang Xu ◽  
Liang Deng ◽  
Xue Li ◽  
Zhixuan Bian ◽  
...  
Keyword(s):  
Dna Damage ◽  
Histone Deacetylase ◽  
Dna Damage Response ◽  
De Novo ◽  
Dna Damage Repair ◽  
Histone Deacetylase 1 ◽  
Damage Repair ◽  
Damage Response

AbstractPhosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS), an essential enzyme involved in de novo purine biosynthesis, is connected with formation of various tumors. However, the specific biological roles and related mechanisms of PAICS in gastric cancer (GC) remain unclear. In the present study, we identified for the first time that PAICS was significantly upregulated in GC and high expression of PAICS was correlated with poor prognosis of patients with GC. In addition, knockdown of PAICS significantly induced cell apoptosis, and inhibited GC cell growth both in vitro and in vivo. Mechanistic studies first found that PAICS was engaged in DNA damage response, and knockdown of PAICS in GC cell lines induced DNA damage and impaired DNA damage repair efficiency. Further explorations revealed that PAICS interacted with histone deacetylase HDAC1 and HDAC2, and PAICS deficiency decreased the expression of DAD51 and inhibited its recruitment to DNA damage sites by impairing HDAC1/2 deacetylase activity, eventually preventing DNA damage repair. Consistently, PAICS deficiency enhanced the sensitivity of GC cells to DNA damage agent, cisplatin (CDDP), both in vitro and in vivo. Altogether, our findings demonstrate that PAICS plays an oncogenic role in GC, which act as a novel diagnosis and prognostic biomarker for patients with GC.

scholarly journals Double PHD Fingers Protein DPF2 Recognizes Acetylated Histones and Suppresses the Function of Estrogen-related Receptor α through Histone Deacetylase 1

2010 ◽  
Vol 285 (24) ◽  
pp. 18166-18176 ◽  
Author(s):  
Reiko Matsuyama ◽  
Ichiro Takada ◽  
Atsushi Yokoyama ◽  
Sally Fujiyma-Nakamura ◽  
Naoya Tsuji ◽  
...  
Keyword(s):  
Histone Deacetylase ◽  
Histone Deacetylase 1 ◽  
Estrogen Related Receptor
Sign in / Sign up

Export Citation Format

Share Document