681465-85-0

Usage

Uses

Used in Pharmaceutical Industry:
Benzoic acid, 4-amino-3-(1-methylethoxy)-, methyl ester (9CI) is used as an intermediate in the synthesis of pharmaceuticals. Its unique chemical structure allows it to be a key component in the development of new medications.
Used in Agrochemical Industry:
In the agrochemical industry, Benzoic acid, 4-amino-3-(1-methylethoxy)-, methyl ester (9CI) is also utilized as an intermediate in the synthesis of various agrochemicals. Its potential applications in this field contribute to the development of new products for agriculture.
It is important to handle Benzoic acid, 4-amino-3-(1-methylethoxy)-, methyl ester (9CI) with care, as it may have harmful effects if not used properly. However, its potential uses in medicine and agriculture highlight its importance as a versatile compound in these industries.

Upstream product

• 159783-41-2 methyl 3-isopropyloxy-4-nitrobenzoate 
• 63435-16-5 3-hydroxy-4-aminobenzoic acid methyl ester 
• 75-26-3 isopropyl bromide 
• 619-14-7 3-hydroxy-4-nitro-benzoic acid 
• 713-52-0 methyl 3-hydroxy-4-nitrobenzoate 
• 75-30-9 2-iodo-propane 

Downstream Products

• 1006030-90-5 methyl 3-isopropoxy-4-(3-(2-naphthylmethoxy)-4-nitro-benzoylamino)-benzoate 
• 1006030-86-9 methyl 3-isopropoxy-4-(3-benzyloxy-4-nitro-benzoylamino)-benzoate 
• 1006030-84-7 methyl 3-isopropoxy-4-(3-propoxy-4-nitro-benzoylamino)-benzoate 
• 1006030-83-6 methyl 3-isopropoxy-4-(3-isopropoxy-4-nitro-benzoylamino)-benzoate 
• 1318208-92-2 isopropyl 3-isopropoxy-4-(3-isopropoxy-4-nitrobenzamido)benzoate 

Relevant academic research and scientific papers

ANTIVIRAL HETEROCYCLIC COMPOUNDS

The present invention discloses compounds of Formula (I), or pharmaceutically acceptable salts, esters, or prodrugs thereof: which inhibit Human Respiratory Syncytial Virus (HRSV) or Human Metapneumovirus (HMPV) inhibitors. The present invention further relates to pharmaceutical compositions comprising the aforementioned compounds for administration to a subject suffering from HRSV or HMPV infection. The invention also relates to methods of treating an HRSV or HMPV infection in a subject by administering a pharmaceutical composition comprising the compounds of the present invention.

CYSTOBACTAMIDES

The present invention provides cystobactamides of formula (I) and the use thereof for the treatment or prophylaxis of bacterial infections:

The Albicidin Resistance Factor AlbD Is a Serine Endopeptidase That Hydrolyzes Unusual Oligoaromatic-Type Peptides

The para-aminobenzoic acid-containing peptide albicidin is a pathogenicity factor synthesized by Xanthomonas albilineans in infections of sugar cane. Albicidin is a nanomolar inhibitor of the bacterial DNA gyrase with a strong activity against various Gram-negative bacteria. The bacterium Pantoea dispersa expresses the hydrolase AlbD, conferring natural resistance against albicidin. We show that AlbD is a novel type of endopeptidase that catalyzes the cleavage of albicidin at a peptide backbone amide bond, thus abolishing its antimicrobial activity. Additionally, we determined the minimal cleavage motif of AlbD with substrates derived by chemical synthesis. Our results clearly identify AlbD as a unique endopeptidase that is the first member of a new subfamily of peptidases. Our findings provide the molecular basis for a natural detoxification mechanism, potentially rendering a new tool in biological chemistry approaches.

COMPOUNDS USEFUL FOR THE TREATMENT OF METABOLIC DISORDERS AND SYNTHESIS OF THE SAME

The present invention provides compounds of Formula (I): wherein variables X, Y, Z and R1 are as described herein. Some of the compounds described herein are glutamate dehydrogenase activators. The invention is also directed to pharmaceutical compositions comprising these compounds, uses of these compounds and compositions in the treatment of metabolic disorders as well as synthesis of the compounds.

Relaxation of the rigid backbone of an oligoamide-foldamer-based α-helix mimetic: Identification of potent Bcl-xL inhibitors

By conducting a structure-activity relationship study of the backbone of a series of oligoamide-foldamer-based α-helix mimetics of the Bak BH3 helix, we have identified especially potent inhibitors of Bcl-xL. The most potent compound has a Ki value of 94 nM in vitro, and single-digit micromolar IC50 values against the proliferation of several Bcl-xL-overexpressing cancer cell lines. The Royal Society of Chemistry 2012.

Hydrophobic side-chain interactions in a family of dimeric amide foldamers-potential alpha-helix mimetics

A series of new alpha-helix mimetics based on a benzamide scaffold and potentially able to disrupt protein-protein interactions have been synthesized and characterized by X-ray analysis. Inspection of the solid state structures of aromatic amide dimers co

Synthesis of functionalised aromatic oligamide rods

A current goal in synthetic chemistry is the design and synthesis of molecules that adopt well defined conformations - so called foldamers. In this manuscript we describe a modular approach for construction of rod shaped para-oligobenzamide molecules. Our approach permits regiospecific incorporation of side chains through a phenolic ether linkage on the scaffold; a feature that partly restricts the conformation of the rod through intramolecular hydrogen-bonding. The Royal Society of Chemistry 2008.

NOVEL COMPOUNDS

There is provided a compound of formula (I): processes for the manufacture thereof, pharmaceutical compositions thereof and uses in therapy.

Terephthalamide peptidomimetic compounds and methods

The present invention relates to compounds and pharmaceutical compositions based upon terephthalamide which are proteomimetic and to methods for inhibiting the interaction of an alpha-helical protein with another protein or binding site. Methods for treat

Terephthalamide derivatives as mimetics of helical peptides: Disruption of the Bcl-xL/Bak interaction

A series of Bcl-xL/Bak antagonists, based on a terephthalamide scaffold, was designed to mimic the α-helical region of the Bak peptide. These molecules showed favorable in vitro activities in disrupting the Bcl-xL/Bak BH3 domain comp