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N-(2-phenylethyl)-3-nitrobenzenesulfonamide is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

35763-22-5

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35763-22-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 35763-22-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,5,7,6 and 3 respectively; the second part has 2 digits, 2 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 35763-22:
(7*3)+(6*5)+(5*7)+(4*6)+(3*3)+(2*2)+(1*2)=125
125 % 10 = 5
So 35763-22-5 is a valid CAS Registry Number.

35763-22-5Relevant academic research and scientific papers

Synthesis and molecular docking of 1,2,3-triazole-based sulfonamides as aromatase inhibitors

Pingaew, Ratchanok,Prachayasittikul, Veda,Mandi, Prasit,Nantasenamat, Chanin,Prachayasittikul, Supaluk,Ruchirawat, Somsak,Prachayasittikul, Virapong

, p. 3472 - 3480 (2015/08/03)

Abstract A series of 1,4-disubstituted-1,2,3-triazoles (13-35) containing sulfonamide moiety were synthesized and evaluated for their aromatase inhibitory effects. Most triazoles with open-chain sulfonamide showed significant aromatase inhibitory activity

Novel 1,4-naphthoquinone-based sulfonamides: Synthesis, QSAR, anticancer and antimalarial studies

Pingaew, Ratchanok,Prachayasittikul, Veda,Worachartcheewan, Apilak,Nantasenamat, Chanin,Prachayasittikul, Supaluk,Ruchirawat, Somsak,Prachayasittikul, Virapong

, p. 446 - 459 (2015/10/05)

A novel series of 1,4-naphthoquinones (33-44) tethered by open and closed chain sulfonamide moieties were designed, synthesized and evaluated for their cytotoxic and antimalarial activities. All quinone-sulfonamide derivatives displayed a broad spectrum o

Synthesis and cytotoxicity of novel N-sulfonyl-1,2,3,4- tetrahydroisoquinoline thiosemicarbazone derivatives

Pingaew, Ratchanok,Prachayasittikul, Supaluk,Ruchirawat, Somsak,Prachayasittikul, Virapong

, p. 267 - 277 (2013/03/13)

The modified Pictet-Spengler reaction of phenylethylbenzene sulfonamide with a commercially available glyoxal to construct 1-benzoyl- and 1-acetyl-1,2,3,4-tetrahydroisoquinolines 9a-n has been reported. The reaction could be accomplished, regardless of th

Progresses in the pursuit of aldose reductase inhibitors: The structure-based lead optimization step

Ramunno, Anna,Cosconati, Sandro,Sartini, Stefania,Maglio, Vita,Angiuoli, Sara,La Pietra, Valeria,Di Maro, Salvatore,Giustiniano, Mariateresa,La Motta, Concettina,Da Settimo, Federico,Marinelli, Luciana,Novellino, Ettore

experimental part, p. 216 - 226 (2012/07/16)

Aldose reductase (ALR2) is a crucial enzyme in the development of the major complications of diabetes mellitus. Very recently it has been demonstrated that the ARL2 inhibitor, fidarestat, significantly prevents inflammatory signals (TNF-α, LPS) that cause cancer (colon, breast, prostate and lung), metastasis, asthma, and other inflammatory diseases. Currently, fidarestat is in phase III clinical trial for diabetic neuropathy and was found to be safe. Thus the finding of novel, potent ARL2 inhibitors is today more than in the past in great demand as they can pave the way for a novel therapeutic approach for a number of diseases besides the diabetes. Herein, starting from the virtual screening-derived ALR2 inhibitor S12728 (1), a rational receptor-based lead optimization has been undertaken. The design and synthetic efforts here reported led to the discovery of several new compounds endowed with low micromolar/submicromolar activities.

Design, synthesis and early structure-activity relationship of farnesyltransferase inhibitors which mimic both the peptidic and the prenylic substrate

Schlitzer, Martin,Boehm, Markus,Sattler, Isabel,Dahse, Hans-Martin

, p. 1991 - 2006 (2007/10/03)

Inhibition of the farnesylation of ras proteins has been identified as a promising target in tumor therapy. Only a few farnesyltransferase inhibitors are bisubstrate analogues displaying features of both substrates, the farnesylpyrophosphate and the C-terminal CAAX-tetrapeptide sequence of the ras protein. These known bisubstrate analogues consist of an AAX-tripeptide and a farnesyl residue connected through various linkers. We have developed a class of novel compounds that mimic a bisubstrate inhibitor structure and that differ from the known ones by lacking peptidic or farnesylic substructures. Long chain fatty acids and aryl-substituted carboxylic acids were used as farnesyl surrogates. These structures were linked to isoleucine amide, benzoic acid amide, N-substituted aminobenzenesulfonamides and N(α)-aryl-substituted methionine derivatives, respectively, which function as AA- or AAX-mimetics. Copyright (C) 2000 Elsevier Science Ltd.

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