[go: up one dir, main page]
More Web Proxy on the site http://driver.im/

Leung et al., 2000 - Google Patents

Protease inhibitors: current status and future prospects

Leung et al., 2000

Document ID
2027004089556075555
Author
Leung D
Abbenante G
Fairlie D
Publication year
Publication venue
Journal of medicinal chemistry

External Links

Snippet

The four major classes of protease enzymes1-4 (aspartic, serine, cysteine, and metallo) selectively catalyze the hydrolysis of polypeptide bonds. Their control over protein synthesis, turnover, and function enables them to regulate physiological processes such as digestion …
Continue reading at pubs.acs.org (other versions)

Classifications

    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6424—Serine endopeptidases (3.4.21)
    • C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6489—Metalloendopeptidases (3.4.24)
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/43—Enzymes; Proenzymes; Derivatives thereof
    • A61K38/46—Hydrolases (3)
    • A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14—Hydrolases (3)
    • C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
    • C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • A61K38/55—Protease inhibitors
    • A61K38/57—Protease inhibitors from animals; from humans
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
    • A61K38/06—Tripeptides
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81—Protease inhibitors
    • C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/81—Protease inhibitors
    • C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
    • C07K14/8146—Metalloprotease (E.C. 3.4.24) inhibitors, e.g. tissue inhibitor of metallo proteinase, TIMP

Similar Documents

Publication Publication Date Title
Leung et al. Protease inhibitors: current status and future prospects
Abbenante et al. Protease inhibitors in the clinic
Otto et al. Cysteine proteases and their inhibitors
Dash et al. Aspartic peptidase inhibitors: implications in drug development
Becker et al. Potent inhibitors of furin and furin-like proprotein convertases containing decarboxylated P1 arginine mimetics
Basak Inhibitors of proprotein convertases
Harish et al. Microbial serine protease inhibitors and their therapeutic applications
Tyndall et al. Proteases universally recognize beta strands in their active sites
Babine et al. Molecular recognition of protein− ligand complexes: Applications to drug design
Kruse et al. Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors
Bouvier et al. Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania
Castro et al. Looking at the proteases from a simple perspective
Lee et al. Extracellular proteases as targets for treatment of cancer metastases
Tyndall et al. Conformational homogeneity in molecular recognition by proteolytic enzymes
Swedberg et al. Design of potent and selective cathepsin G inhibitors based on the sunflower trypsin inhibitor-1 scaffold
Maryanoff et al. Inhibitors of proteases and amide hydrolases that employ an α-ketoheterocycle as a key enabling functionality
Steinmetzer et al. The antiviral potential of host protease inhibitors
Ewing et al. Progress in the design of inhibitors of coagulation factor Xa
Leontovyč et al. SmSP2: A serine protease secreted by the blood fluke pathogen Schistosoma mansoni with anti-hemostatic properties
Swedberg et al. Highly potent and selective plasmin inhibitors based on the sunflower trypsin inhibitor-1 scaffold attenuate fibrinolysis in plasma
Al-Awadhi et al. Targeting eukaryotic proteases for natural products-based drug development
Li et al. Binding loop substitutions in the cyclic peptide SFTI-1 generate potent and selective chymase inhibitors
Mittl et al. Opportunities for structure-based design of protease-directed drugs
Fernández et al. Progress in metallocarboxypeptidases and their small molecular weight inhibitors
Xu et al. Design of specific serine protease inhibitors based on a versatile peptide scaffold: conversion of a urokinase inhibitor to a plasma kallikrein inhibitor