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N-(4-chlorobenzyl)-N'-cyclohexylthiourea is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

345302-92-3

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345302-92-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 345302-92-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 3,4,5,3,0 and 2 respectively; the second part has 2 digits, 9 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 345302-92:
(8*3)+(7*4)+(6*5)+(5*3)+(4*0)+(3*2)+(2*9)+(1*2)=123
123 % 10 = 3
So 345302-92-3 is a valid CAS Registry Number.

345302-92-3Downstream Products

345302-92-3Relevant academic research and scientific papers

Molecular determinants of ligand binding modes in the histamine H 4 receptor: Linking ligand-based three-dimensional quantitative structure-activity relationship (3D-QSAR) models to in silico guided receptor mutagenesis studies

Istyastono, Enade P.,Nijmeijer, Saskia,Lim, Herman D.,Van De Stolpe, Andrea,Roumen, Luc,Kooistra, Albert J.,Vischer, Henry F.,De Esch, Iwan J. P.,Leurs, Rob,De Graaf, Chris

experimental part, p. 8136 - 8147 (2012/01/05)

The histamine H4 receptor (H4R) is a G protein-coupled receptor (GPCR) that plays an important role in inflammation. Similar to the homologous histamine H3 receptor (H3R), two acidic residues in the H4/sub

Development of a pharmacophore model for histamine H3 receptor antagonists, using the newly developed molecular modeling program SLATE

De Esch,Mills,Perkins,Romeo,Hoffmann,Wieland,Leurs,Menge,Nederkoorn,Dean,Timmerman

, p. 1666 - 1674 (2007/10/03)

New molecular modeling tools were developed to construct a qualitative pharmacophore model for histamine H3 receptor antagonists. The program SLATE superposes ligands assuming optimum hydrogen bond geometry. One or two ligands are allowed to flex in the procedure, thereby enabling the determination of the bioactive conformation of flexible H3 antagonists. In the derived model, four hydrogen-bonding site points and two hydrophobic pockets available for binding antagonists are revealed. The model results in a better understanding of the structure-activity relationships of H3 antagonists. To validate the model, a series of new antagonists was synthesized. The compounds were designed to interact with all four hydrogen-bonding site points and the two hydrophobic pockets simultaneously. These ligands have high H3 receptor affinity, thereby illustrating how the model can be used in the design of new classes of H3 antagonists.

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