In Situ Extension as an Approach for Identifying Novel α-Amylase Inhibitors-Reference-Cited by-同舟云学术

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In Situ Extension as an Approach for Identifying Novel α-Amylase Inhibitors

Published:2004-11 Issue:46 Volume:279 Page:48282-48291
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Numao Shin,Damager Iben,Li Chunmin,Wrodnigg Tanja M.,Begum Anjuman,Overall Christopher M.,Brayer Gary D.,Withers Stephen G.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference39 articles.

1. A classification of glycosyl hydrolases based on amino acid sequence similarities

2. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities

3. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.

4. Crystal structures of the psychrophilic α‐amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor

5. The structure of human pancreaticα-amylase at 1.8 Å resolution and comparisons with related enzymes

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1. Glycosidase-targeting small molecules for biological and therapeutic applications;Chemical Society Reviews;2023

2. Unexpected One‐Pot Formation of Lactam Oximes from Amino‐Hydroxamic Esters;European Journal of Organic Chemistry;2022-05-31

3. Development of an active site titration reagent for α-amylases;Chemical Science;2021

4. Eriobotrya japonica leaf triterpenoid acids ameliorate metabolic syndrome in C57BL/6J mice fed with high-fat diet;Biomedicine & Pharmacotherapy;2020-12

5. Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase;Chemical Science;2019

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