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Ethanol, 2-[[(4-methoxyphenyl)methyl]thio]- is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

35378-93-9

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35378-93-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 35378-93-9 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,5,3,7 and 8 respectively; the second part has 2 digits, 9 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 35378-93:
(7*3)+(6*5)+(5*3)+(4*7)+(3*8)+(2*9)+(1*3)=139
139 % 10 = 9
So 35378-93-9 is a valid CAS Registry Number.

35378-93-9Relevant academic research and scientific papers

Bioresponsive small molecule polyamines as noncytotoxic alternative to polyethylenimine

Drake, Christopher R.,Aissaoui, Abderrahim,Argyros, Orestis,Serginson, James M.,Monnery, Bryn D.,Thanou, Maya,Steinke, Joachim H. G.,Miller, Andrew D.

, p. 2040 - 2055 (2010)

Nonviral gene therapy continues to require novel synthetic vectors to deliver therapeutic nucleic acids effectively and safely. The majority of synthetic nonviral vectors employed in clinical trials to date have been cationic liposomes; however, cationic

Organosulfur compounds as potential fungicides: The preparation and properties of some substituted benzyl 2-hydroxyethyl oligosulfides

Ayodele, Ezekiel T.,Hudson, Harry R.,Ojo, Isaac A. O.,Pianka, Max

, p. 123 - 142 (2007/10/03)

Compounds of the general type ArCH2SnCH2CH2OH (n = 1 - 4, Ar = Ph, 2-MeC6H4. 4-MeC6H4, 4-ClC6H4, 4-MeOC6H4; n = 1 - 3, Ar = 2-ClC6H4; n = 2, Ar = 4-FC6H4; n = 3 or 4, Ar = 2-furyl) have been prepared as analogues of the trisulfide PhCH2SSSCH2CH2OH (an antimicrobial compound which occurs in the plant Petiveria alliacea) and their potential for application as agricultural fungicides has been examined. In vitro tests against Fusarium culmorum, Fusarium oxysporum and Gauennmyceles graminis showed that all compounds gave > 80% control of these organisms at 1000 ppm. Tests at 100 and 10 ppm showed varying levels of control but the activity did not depend significantly on the number of sulfur atoms present. Selected compounds were also shown to be active in vivo against Erysiphe graminis on barley seedlings, Botrytis fabae and Uromyces viciae-fabae on bean seedlings, Podosphaera leucotricha on apple seedlings, and Phytophthora infestans on potato leaf. The compounds were phytotoxic at concentrations greater than 0.33%.

Thiol ligands and complexes for X-ray imaging

-

, (2008/06/13)

The present invention provides new and structurally diverse compositions comprising compounds of the general formula: STR1 Wherein R1, R2, R3, R4, and R5 are the same or different and are --CO--(CHsu

Design of novel inhibitors of aminopeptidases. Synthesis of peptide-derived diamino thiols and sulfur replacement analogues of bestatin

Gordon,Godfrey,Delaney,Asaad,Von Langen,Cushman

, p. 2199 - 2211 (2007/10/02)

Investigations were directed toward inhibition of an aminopeptidase, isolated from rat brain, which has been implicated in the metabolic inactivation of enkephalins. The design rationale and synthesis of novel peptidyl diamino thiol inhibitors of rat brain aminopeptidase are presented, along with accompanying structure-activity analysis. Some of the reported compounds are highly active aminopeptidase inhibitors and possess enzyme inhibitory potency in the nanomolar range (62; I50 = 1 nM). Analysis of the data permits speculations on possible modes of binding of diamino thiols to aminopeptidase. Other investigations were directed toward understanding the mode of enzyme binding of the naturally occurring aminopeptidase inhibitor bestatin. On the basis of published models of enzyme binding, replacement of the C-2 hydroxyl group of bestatin by a sulfhydryl group was anticipated to lead to enhanced inhibition due to a strengthened interaction of this group with enzymic zinc. Contrary to expectations, 'thiobestatin' inhibited rat brain aminopeptidase with only the same degree of effectiveness as the corresponding alcohol. Speculations on the possible mode of enzyme-inhibitor binding of bestatin are offered.

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