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141041-86-3

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141041-86-3 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 141041-86-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,4,1,0,4 and 1 respectively; the second part has 2 digits, 8 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 141041-86:
(8*1)+(7*4)+(6*1)+(5*0)+(4*4)+(3*1)+(2*8)+(1*6)=83
83 % 10 = 3
So 141041-86-3 is a valid CAS Registry Number.

141041-86-3Relevant articles and documents

RITA Mimics: Synthesis and Mechanistic Evaluation of Asymmetric Linked Trithiazoles

Pietkiewicz, Adrian L.,Zhang, Yuqi,Rahimi, Marwa N.,Stramandinoli, Michael,Teusner, Matthew,McAlpine, Shelli R.

supporting information, p. 401 - 406 (2017/04/21)

The established cytotoxic agent RITA contains a thiophene-furan-thiophene backbone and two terminal alcohol groups. Herein we investigate the effect of using thiazoles as the backbone in RITA-like molecules and modifying the terminal groups of these trithiazoles, thereby generating 41 unique structures. Incorporating side chains with varied steric bulk allowed us to investigate how size and a stereocenter impacted biological activity. Subjecting compounds to growth inhibition assays on HCT-116 cells showed that the most potent compounds 7d, 7e, and 7h had GI50 values of 4.4, 4.4, and 3.4 μM, respectively, versus RITA (GI50 of 800 nM). Analysis of these compounds in apoptosis assays proved that 7d, 7e, and 7h were as effective as RITA at inducing apoptosis. Evaluating the impact of 7h on proteins targeted by RITA (p53, c-Myc, and Mcl-1) indicated that it acts via a different mechanism of action to that of RITA. RITA suppressed Mcl-1 protein via p53, whereas compound 7h suppressed Mcl-1 expression via an alternative mechanism independent of p53.

Chemoenzymatic Synthesis of Thiazolyl Peptide Natural Products Featuring an Enzyme-Catalyzed Formal [4 + 2] Cycloaddition

Wever, Walter J.,Bogart, Jonathan W.,Baccile, Joshua A.,Chan, Andrew N.,Schroeder, Frank C.,Bowers, Albert A.

supporting information, p. 3494 - 3497 (2015/03/30)

Thiocillins from Bacillus cereus ATCC 14579 are members of the well-known thiazolyl peptide class of natural product antibiotics, the biosynthesis of which has recently been shown to proceed via post-translational modification of ribosomally encoded precursor peptides. It has long been hypothesized that the final step of thiazolyl peptide biosynthesis involves a formal [4 + 2] cycloaddition between two dehydroalanines, a unique transformation that had eluded enzymatic characterization. Here we demonstrate that TclM, a single enzyme from the thiocillin biosynthetic pathway, catalyzes this transformation. To facilitate characterization of this new class of enzyme, we have developed a combined chemical and biological route to the complex peptide substrate, relying on chemical synthesis of a modified C-terminal fragment and coupling to a 38-residue leader peptide by means of native chemical ligation (NCL). This strategy, combined with active enzyme, provides a new chemoenzymatic route to this promising class of antibiotics.

Synthesis of o -me ulongamide b and o -me ulongamide c, natural modified cyclodepsipeptides

Alvarado, Cuauhtémoc,Hernández, Gerardo,Díaz, Eduardo,Soano, José D.,Vilchis-Reyes, Miguel A.,Martínez-Urbina, Miguel A.,Guzmán, Angel

, p. 993 - 1006 (2013/03/13)

Synthesis of O-Me ulongamide B and O-Me ulongamide C, modified natural cyclodepsipeptides, was achieved by a convergent route. The respective dipeptides and tridepsipeptides were coupled, obtaining linear depsipentapeptides, which were then deprotected and cyclized. These compounds were tested against three different types of human carcinoma cells and showed only moderate activity.

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