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21950-36-7

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  • Adenosine, 5'-aMino-5'-deoxy-2',3'-O-(1-Methylethylidene)-

    Cas No: 21950-36-7

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  • 10 Gram

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  • Senova Pharma
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21950-36-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 21950-36-7 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 2,1,9,5 and 0 respectively; the second part has 2 digits, 3 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 21950-36:
(7*2)+(6*1)+(5*9)+(4*5)+(3*0)+(2*3)+(1*6)=97
97 % 10 = 7
So 21950-36-7 is a valid CAS Registry Number.

21950-36-7Relevant articles and documents

Methionyl adenylate analogues as inhibitors of methionyl-tRNA synthetase

Lee, Jeewoo,Sang, Uk Kang,Mee, Kyoung Kang,Moon, Woo Chun,Yeong, Joon Jo,Jin, Hwan Kwak,Kim, Sunghoon

, p. 1365 - 1370 (1999)

Four stable analogues of methionyl adenylate (3-6) were designed as inhibitors of methionyl-tRNA synthetase and synthesized from 2',3'- isopropylideneadenosine. They strongly inhibited aminoacylation activity of methionyl-tRNA synthetases isolated from Escherichi coli, Mycobacterium tuberculosis, Saccharomyces cerevisiae and human. Among the microorganisms tested, however, these chemicals showed the growth inhibition effect only on E. coli.

Synthesis and evaluation of adenosine containing 3-arylfuran-2(5H)-ones as tyrosyl-tRNA synthetase inhibitors

Wei, Wei,Liu, Qi,Li, Zhen-Zhen,Shi, Wei-Kang,Fu, Xing,Liu, Jia,Zhu, Xuan,Wang, Xiao-Cong,Xu, Ning,Li, Teng-Fei,Jiang, Fu-Rui,Xiao, Zhu-Ping,Zhu, Hai-Liang

, p. 62 - 68 (2017)

Tyrosyl-tRNA synthetase (TyrRS) is an aminoacyl-tRNA synthetase family protein that possesses an essential role in bacterial protein synthesis. The synthesis, structure-activity relationship, and evolution of a novel series of adenosine-containing 3-arylfuran-2(5H)-ones as TyrRS inhibitors are described. Advanced compound d3 from this series exhibited excellent affinity for TyrRS with IC50 of 0.61?±?0.04?μM. Bacterial growth inhibition assays demonstrated that d3 showed submicromolar antibacterial potency against Escherichia coli and Pseudomonas aeruginosa, and compared to the marketed antibiotics ciprofloxacin.

Potent SARS-CoV-2 mRNA Cap Methyltransferase Inhibitors by Bioisosteric Replacement of Methionine in SAM Cosubstrate

Bobi?eva, Olga,Bobrovs, Raitis,Ka?epe, Iveta,Patetko, Liene,Kalni??, Gints,?i?ovs, Mihails,Bula, Anna L.,Grī Nberga, Solveiga,Borodu??is, Mā Rti??,Ramata-Stunda, Anna,Rostoks, Nils,Jirgensons, Aigars,Tā Rs, Kaspars,Jaudzems, Kristaps

supporting information, p. 1102 - 1107 (2021/06/30)

Viral mRNA cap methyltransferases (MTases) are emerging targets for the development of broad-spectrum antiviral agents. In this work, we designed potential SARS-CoV-2 MTase Nsp14 and Nsp16 inhibitors by using bioisosteric substitution of the sulfonium and amino acid substructures of the cosubstrate S-adenosylmethionine (SAM), which serves as the methyl donor in the enzymatic reaction. The synthetically accessible target structures were prioritized using molecular docking. Testing of the inhibitory activity of the synthesized compounds showed nanomolar to submicromolar IC50 values for five compounds. To evaluate selectivity, enzymatic inhibition of the human glycine N-methyltransferase involved in cellular SAM/SAH ratio regulation was also determined, which indicated that the discovered compounds are nonselective inhibitors of the studied MTases with slight selectivity for Nsp16. No cytotoxic effects were observed; however, this is most likely a result of the poor cell permeability of all evaluated compounds.

Purine derivative and preparation method and application thereof

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Paragraph 0166; 0211; 0216-0217, (2021/06/26)

The invention discloses a purine derivative and a preparation method and application thereof, belongs to the technical field of medicines, and designs and synthesizes a series of purine derivatives and optical isomers, pharmaceutically acceptable salts, solvates or prodrugs of the purine derivatives. Experiments show that the compound has outstanding anti-cell proliferation activity and DOT1L enzyme inhibition effect, shows good tumor growth inhibition activity in a tumor transplantation tumor model, and has a good application prospect.

Biosynthesis, Mechanism of Action, and Inhibition of the Enterotoxin Tilimycin Produced by the Opportunistic Pathogen Klebsiella oxytoca

Aldrich, Courtney C.,Alexander, Evan M.,Balbo, Silvia,Drake, Eric,Guidolin, Valeria,Gulick, Andrew M.,Hurben, Alexander K.,Kreitler, Dale F.,Villalta, Peter W.

, p. 1976 - 1997 (2020/10/06)

Tilimycin is an enterotoxin produced by the opportunistic pathogen Klebsiella oxytoca that causes antibiotic-associated hemorrhagic colitis (AAHC). This pyrrolobenzodiazepine (PBD) natural product is synthesized by a bimodular nonribosomal peptide synthetase (NRPS) pathway composed of three proteins: NpsA, ThdA, and NpsB. We describe the functional and structural characterization of the fully reconstituted NRPS system and report the steady-state kinetic analysis of all natural substrates and cofactors as well as the structural characterization of both NpsA and ThdA. The mechanism of action of tilimycin was confirmed using DNA adductomics techniques through the detection of putative N-2 guanine alkylation after tilimycin exposure to eukaryotic cells, providing the first structural characterization of a PBD-DNA adduct formed in cells. Finally, we report the rational design of small-molecule inhibitors that block tilimycin biosynthesis in whole cell K. oxytoca (IC50 = 29 ± 4 μM) through the inhibition of NpsA (KD = 29 ± 4 nM).

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