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848133-04-0

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848133-04-0 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 848133-04-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 8,4,8,1,3 and 3 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 848133-04:
(8*8)+(7*4)+(6*8)+(5*1)+(4*3)+(3*3)+(2*0)+(1*4)=170
170 % 10 = 0
So 848133-04-0 is a valid CAS Registry Number.

848133-04-0Relevant articles and documents

AGENTS FOR USE IN THE TREATMENT OF AMYLOIDOSIS

-

, (2022/04/03)

The present invention relates to compounds for stabilising the native tetrameric form of transthyretin and protecting it from proteolytic cleavage; compounds for use in the prevention and treatment of transthyretin amyloidosis; and agents and medicaments comprising such compounds. The compounds are based on a general structure A-L-B, wherein A is a group of formula (II) or of formula (III): or of formula (IV) or of formula (V) B is a group of formula (III), (IV), or (V), or a group of formula (VI) or a group of formula –R10Z, wherein: Z is selected from -CO2R', -CONR'R'', -SO2R' wherein R' and R'' are independently H or C1-C4 alkyl; and R10 is a C1-C4 alkylene or alkenylene group; and L represents a linker group which is a saturated or unsaturated chain of 5 to 13 carbon atoms.

Kinetic stabilization of an oligomeric protein by a single ligand binding event

Wiseman, R. Luke,Johnson, Steven M.,Kelker, Matthew S.,Foss, Ted,Wilson, Ian A.,Kelly, Jeffery W.

, p. 5540 - 5551 (2007/10/03)

Protein native state stabilization imposed by small molecule binding is an attractive strategy to prevent the misfolding and misassembly processes associated with amyloid diseases. Transthyretin (TTR) amyloidogenesis requires rate-limiting tetramer dissociation before misassembly of a partially denatured monomer ensues. Selective stabilization of the native TTR tetramer over the dissociative transition state by small molecule binding to both thyroxine binding sites raises the kinetic barrier of tetramer dissociation, preventing amyloidogenesis. Assessing the amyloidogenicity of a TTR tetramer having only one amyloidogenesis inhibitor (I) bound is challenging because the two small molecule binding constants are generally not distinct enough to allow for the exclusive formation of TTR·I in solution to the exclusion of TTR·I2 and unliganded TTR. Herein, we report a method to tether one fibril formation inhibitor to TTR by disulfide bond formation. Occupancy of only one of the two thyroxine binding sites is sufficient to inhibit tetramer dissociation in 6.0 M urea and amyloidogenesis under acidic conditions by imposing kinetic stabilization on the entire tetramer. The sufficiency of single occupancy for stabilizing the native state of TTR provides the incentive to search for compounds displaying striking negative binding cooperativity (e.g., Kd1 in nanomolar range and Kd2 in the micromolar to millimolar range), enabling lower doses of inhibitor to be employed in the clinic, mitigating potential side effects.

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