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1359132-64-1

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1359132-64-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1359132-64-1 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,3,5,9,1,3 and 2 respectively; the second part has 2 digits, 6 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 1359132-64:
(9*1)+(8*3)+(7*5)+(6*9)+(5*1)+(4*3)+(3*2)+(2*6)+(1*4)=161
161 % 10 = 1
So 1359132-64-1 is a valid CAS Registry Number.

1359132-64-1Downstream Products

1359132-64-1Relevant articles and documents

Diversified thiazole substituted coumarins and chromones as non-cytotoxic ros and no inhibitors

Faheem, Aisha,Hussain, Shafquat,Jabeen, Almas,Khan, Khalid Mohammed,Naqvi, Farwa,Perveen, Shahnaz,Salar, Uzma

, p. 545 - 553 (2020/04/30)

Background: Non-steroidal anti-inflammatory drugs (NSAIDs) such as ibuprofen, aspirin, indomethacin, flufenamic acid and phenylbutazone are used to treat most of the inflammatory disorders. These NSAIDs are also associated with serious side effects includ

Synthesis of a novel series of thiazole-based histone acetyltransferase inhibitors

Secci, Daniela,Carradori, Simone,Bizzarri, Bruna,Bolasco, Adriana,Ballario, Paola,Patramani, Zoi,Fragapane, Paola,Vernarecci, Stefano,Canzonetta, Claudia,Filetici, Patrizia

, p. 1680 - 1689 (2014/03/21)

Acetylation, which targets a broad range of histone and non-histone proteins, is a reversible mechanism and plays a critical role in eukaryotic genes activation/deactivation. Acetyltransferases are very well conserved through evolution. This allows the use of a simple model organism, such as budding yeast, for the study of their related processes and to discover specific inhibitors. Following a simple yeast-based chemogenetic approach, we have identified a novel HAT (histone acetyltransferase) inhibitor active both in vitro and in vivo. This new synthetic compound, 1-(4-(4-chlorophenyl)thiazol-2- yl)-2-(propan-2-ylidene)hydrazine, named BF1, showed substrate selectivity for histone H3 acetylation and inhibitory activity in vitro on recombinant HAT Gcn5 and p300. Finally, we tested BF1 on human cells, HeLa as control and two aggressive cancer cell lines: a neuroblastoma from neuronal tissue and glioblastoma from brain tumour. Both global acetylation of histone H3 and specific acetylation at lysine 18 (H3AcK18) were lowered by BF1 treatment. Collectively, our results show the efficacy of this novel HAT inhibitor and propose the utilization of BF1 as a new, promising tool for future pharmacological studies.

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