912999-04-3 Usage
Molecular structure
A complex structure derived from isoindole, featuring a hydroxy group, an isopropyl group, and a benzoyl group.
Chemical classification
A chemical compound belonging to the isoindole derivatives group.
Hydroxy group
The presence of a hydroxy group (-OH) may contribute to its potential antioxidant properties.
Isopropyl group
Contains an isopropyl group (-CH(CH3)2) which could influence its therapeutic effects.
Benzoyl group
Features a benzoyl group (-C6H5CO) that may contribute to its potential anti-inflammatory and analgesic effects.
Pharmaceutical applications
Commonly used in the pharmaceutical industry due to its potential therapeutic properties.
Therapeutic effects
Possesses potential antioxidant, anti-inflammatory, and analgesic effects based on its molecular structure.
Research and development
Currently being studied for its potential applications in treating various medical conditions, making it an important target for further research in pharmaceutical chemistry.
Check Digit Verification of cas no
The CAS Registry Mumber 912999-04-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 9,1,2,9,9 and 9 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 912999-04:
(8*9)+(7*1)+(6*2)+(5*9)+(4*9)+(3*9)+(2*0)+(1*4)=203
203 % 10 = 3
So 912999-04-3 is a valid CAS Registry Number.
912999-04-3Relevant articles and documents
Selective Inhibition of the Hsp90α Isoform
Mishra, Sanket J.,Khandelwal, Anuj,Banerjee, Monimoy,Balch, Maurie,Peng, Shuxia,Davis, Rachel E.,Merfeld, Taylor,Munthali, Vitumbiko,Deng, Junpeng,Matts, Robert L.,Blagg, Brian S. J.
, p. 10547 - 10551 (2021)
The 90 kDa heat shock protein (Hsp90) is a molecular chaperone that processes nascent polypeptides into their biologically active conformations. Many of these proteins contribute to the progression of cancer, and consequently, inhibition of the Hsp90 protein folding machinery represents an innovative approach toward cancer chemotherapy. However, clinical trials with Hsp90 N-terminal inhibitors have encountered deleterious side effects and toxicities, which appear to result from the pan-inhibition of all four Hsp90 isoforms. Therefore, the development of isoform-selective Hsp90 inhibitors is sought to delineate the pathological role played by each isoform. Herein, we describe a structure-based approach that was used to design the first Hsp90α-selective inhibitors, which exhibit >50-fold selectivity versus other Hsp90 isoforms.
