90004-78-7

Basic information

• Product Name: 1-bromo-5-chloro-2-methoxy-4-methylbenzene
• Synonyms: 1-bromo-5-chloro-2-methoxy-4-methylbenzene
• CAS NO: 90004-78-7
• Molecular Weight: 235.508
• Mol File: 90004-78-7.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: 1-bromo-5-chloro-2-methoxy-4-methylbenzene(CAS DataBase Reference)
• NIST Chemistry Reference: 1-bromo-5-chloro-2-methoxy-4-methylbenzene(90004-78-7)
• EPA Substance Registry System: 1-bromo-5-chloro-2-methoxy-4-methylbenzene(90004-78-7)

Safety Data

• Hazardous Substances Data: 90004-78-7(Hazardous Substances Data)

Upstream product

• 59-50-7 4-Chloro-3-methylphenol 
• 13334-71-9 1-chloro-4-methoxy-2-methylbenzene 

Downstream Products

• 28478-41-3 2-methoxy-4-methyl-5-chlorobenzoic acid 
• 90110-96-6 2-Chlor-4-brom-5-methoxy-benzoesaeure 
• 73147-24-7 dimethyl-2-chloro-5-methoxyterephthalate 
• 35458-35-6 5-chloro-2-hydroxy-4-methyl-benzoic acid 
• 77923-35-4 2-chloro-5-methoxyterephthalic acid 

Relevant articles and documents

Pharmacophore Mapping of Thienopyrimidine-Based Monophosphonate (ThP-MP) Inhibitors of the Human Farnesyl Pyrophosphate Synthase

The human farnesyl pyrophosphate synthase (hFPPS), a key regulatory enzyme in the mevalonate pathway, catalyzes the biosynthesis of the C-15 isoprenoid farnesyl pyrophosphate (FPP). FPP plays a crucial role in the post-translational prenylation of small GTPases that perform a plethora of cellular functions. Although hFPPS is a well-established therapeutic target for lytic bone diseases, the currently available bisphosphonate drugs exhibit poor cellular uptake and distribution into nonskeletal tissues. Recent drug discovery efforts have focused primarily on allosteric inhibition of hFPPS and the discovery of non-bisphosphonate drugs for potentially treating nonskeletal diseases. Hit-to-lead optimization of a new series of thienopyrimidine-based monosphosphonates (ThP-MPs) led to the identification of analogs with nanomolar potency in inhibiting hFPPS. Their interactions with the allosteric pocket of the enzyme were characterized by crystallography, and the results provide further insight into the pharmacophore requirements for allosteric inhibition.