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methyl (E)‐4‐(3‐chloro‐3‐oxoprop‐1‐en‐1‐yl)benzoate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

145241-74-3

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145241-74-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 145241-74-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,5,2,4 and 1 respectively; the second part has 2 digits, 7 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 145241-74:
(8*1)+(7*4)+(6*5)+(5*2)+(4*4)+(3*1)+(2*7)+(1*4)=113
113 % 10 = 3
So 145241-74-3 is a valid CAS Registry Number.

145241-74-3Relevant academic research and scientific papers

Modular Cyclopentenone Synthesis through the Catalytic Molecular Shuffling of Unsaturated Acid Chlorides and Alkynes

Lee, Yong Ho,Denton, Elliott H.,Morandi, Bill

supporting information, p. 20948 - 20955 (2020/12/21)

We describe a general strategy for the intermolecular synthesis of polysubstituted cyclopentenones using palladium catalysis. Overall, this reaction is achieved via a molecular shuffling process involving an alkyne, an α,β-unsaturated acid chloride, which serves as both the alkene and carbon monoxide source, and a hydrosilane to create three new C-C bonds. This new carbon monoxide-free pathway delivers the products with excellent yields. Furthermore, the regioselectivity is complementary to conventional methods for cyclopentenone synthesis. In addition, a set of regio- and chemodivergent reactions are presented to emphasize the synthetic potential of this novel strategy.

Design, synthesis and cytotoxic evaluation of novel imatinib amide derivatives that target Abl kinase

Yao, Ri-Sheng,Guan, Qiu-Xiang,Lu, Xiao-Qin,Ruan, Ban-Feng

, p. 20 - 28 (2015/03/31)

Novel imatinib amide derivatives (a1-28, b1-9) were synthesized and evaluated for their biological activities. All compounds were characterized by 1H NMR, MS and elemental analysis. Among all the derivatives, compounds a4, a10, a21, b1 and b2 displayed the most significant ability of inhibiting K562 cell proliferation with the IC50 values of 0.67, 0.66, 0.65, 0.59 and 0.62 μM, respectively, indicating that these compounds were potent inhibitors of Bcr-Abl in leukemic K562 cells, comparable to the reference compound imatinib. Molecular docking study was performed to position compounds a21 and b1 into the active site of Abl to determine the probable binding modes

Synthesis of cinnamic acid-derived 4,5-dihydrooxazoles

Kronek, Juraj,Nedelcev, Tomas,Mikulec, Marcel,Kleinova, Angela,Luston, Jozef

, p. 1424 - 1432 (2013/07/26)

A range of cinnamic units containing 4,5-dihydrooxazoles was prepared using two different synthetic routes. The first method was based on the transformation of substituted cinnamic or benzoic acids to 2-styryl-4,5- dihydrooxazoles. Several derivatives con

Paracyclophanes: Extending the bridges. Synthesis

Pechlivanidis, Zissis,Hopf, Henning,Ernst, Ludger

experimental part, p. 223 - 237 (2009/06/21)

Preparatively satisfactory routes to [3.2]paracyclophane (10), [4.2]paracyclophane (14), [4.3]paracyclophane (19) as well as several derivatives of these compounds - among others the bromides 25, the ester 31, the diesters 40-43 - are described using well-established methods of cyclophane chemistry (ring-closure reactions leading to thiacyclophanes, ring contraction by sulfone pyrolysis). The parent systems and their derivatives are now available in gram quantities allowing a study of their chemical properties. Wiley-VCH Verlag GmbH & Co. KGaA, 2009.

Non-thiol farnesyltransferase inhibitors: Utilization of the far aryl binding site by 5-cinnamoylaminobenzophenones

Mitsch, Andreas,Wissner, Pia,Boehm, Markus,Silber, Katrin,Klebe, Gerhard,Sattler, Isabel,Schlitzer, Martin

, p. 493 - 501 (2007/10/03)

We recently described two novel aryl binding sites of farnesyltransferase. In this study, the cinnamoyl residue was designed as an appropriate substituent for our benzophenone-based AAX-peptidomimetic compound capable of occupying the far aryl binding site.

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