FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2016800089> ?p ?o ?g. }

• W2016800089 endingPage "2571" @default.
• W2016800089 startingPage "2565" @default.
• W2016800089 abstract "A series of natural epimers of alpha-homonojirimycin and its N-alkylated derivatives have been prepared to investigate the contribution of the different chiral centers and conformation of the specificity and potency of inhibition of glycosidases. These epimers and N-alkylated derivatives are alpha-homonojirimycin (1), beta-homonojirimycin (2), alpha-homomannojirimycin (3), beta-homomannojirimycin (4), alpha-3,4-di-epi-homonojirimycin (5), beta-4,5-di-epi-homonojirimycin (6), N-methyl-alpha-homonojirimycin (7), and N-butyl-alpha-homonojirimycin (8). Compound 1 was a potent inhibitor of a range of alpha-glucosidases with IC50 values of 1 to 0.01 microM. Compounds 2, 3, and 4 were surprisingly inactive as inhibitors of beta-glucosidase and alpha- and beta-mannosidases but were moderately good as inhibitors of rice and some mammalian alpha-glucosidases. Compound 4 was active in the micromolar range toward all alpha-glucosidases tested. Furthermore, compound 4, which superimposes well on beta-l-fucose, was a 10-fold more effective inhibitor of alpha-l-fucosidase than 1-deoxymannojirimycin (12) and 3, with a Ki value of 0.45 microM. Only compounds 5 and 6 showed inhibitory activity toward alpha- and beta-galactosidases (6with an IC50 value of 6.4 microM against alpha-galactosidase). The high-resolution structure of 1 has been determined by X-ray diffraction and showed a chair conformation with the C1 OH (corresponding to the C6 OH in 1-deoxynojirimycin) predominantly equatorial to the piperidine ring in the crystal structure. This preferred (C1 OH equatorial) conformation was also corroborated by 1H NMR coupling constants. The coupling constants for 7 suggest the axial orientation of the C1 OH, while in 8 the C1 OH axial conformation was not observed. The C1 OH axial conformation appears to be responsible for more potent inhibition toward processing alpha-glucosidase I than alpha-glucosidase II. It has been assumed that the anti-HIV activity of alkaloidal glycosidase inhibitors results from the inhibition of processing alpha-glucosidase I, but 1, 7, and 8 were inactive against HIV-1 replication at 500 microg/mL as measured by inhibition of virus-induced cytopathogenicity in MT-4 cells. In contrast, the EC50 value for N-butyl-1-deoxynojirimycin (11), which also inhibits processing alpha-glucosidase I, was 37 microg/mL. Compound 7 has been shown to be a better inhibitor of alpha-glucosidase I than 1 and 8 both in vitro and in the cell culture system. These data imply that inhibition of HIV by glycosidase inhibitors can be due to factors other than simply inhibition of processing alpha-glucosidase I." @default.
• W2016800089 created "2016-06-24" @default.
• W2016800089 creator A5005260393 @default.
• W2016800089 creator A5005616195 @default.
• W2016800089 creator A5005720957 @default.
• W2016800089 creator A5012030130 @default.
• W2016800089 creator A5023792530 @default.
• W2016800089 creator A5042437899 @default.
• W2016800089 creator A5051716463 @default.
• W2016800089 creator A5065145912 @default.
• W2016800089 creator A5078914737 @default.
• W2016800089 creator A5080592581 @default.
• W2016800089 creator A5087333213 @default.
• W2016800089 creator A5090092776 @default.
• W2016800089 creator A5091237671 @default.
• W2016800089 date "1998-06-16" @default.
• W2016800089 modified "2023-09-27" @default.
• W2016800089 title "Homonojirimycin Isomers and N-Alkylated Homonojirimycins: Structural and Conformational Basis of Inhibition of Glycosidases" @default.
• W2016800089 cites W1515555384 @default.
• W2016800089 cites W1516917377 @default.
• W2016800089 cites W1559781420 @default.
• W2016800089 cites W1704481257 @default.
• W2016800089 cites W1966498983 @default.
• W2016800089 cites W1974898808 @default.
• W2016800089 cites W1979083254 @default.
• W2016800089 cites W1983975531 @default.
• W2016800089 cites W1996394361 @default.
• W2016800089 cites W2012097474 @default.
• W2016800089 cites W2020459278 @default.
• W2016800089 cites W2032826794 @default.
• W2016800089 cites W2042280050 @default.
• W2016800089 cites W2063825413 @default.
• W2016800089 cites W2068161396 @default.
• W2016800089 cites W2080299613 @default.
• W2016800089 cites W2080729497 @default.
• W2016800089 cites W2087546739 @default.
• W2016800089 cites W2091142738 @default.
• W2016800089 cites W2128179591 @default.
• W2016800089 cites W2130421146 @default.
• W2016800089 cites W2137535311 @default.
• W2016800089 cites W2152215708 @default.
• W2016800089 cites W2171610348 @default.
• W2016800089 cites W2255764129 @default.
• W2016800089 cites W2410838417 @default.
• W2016800089 doi "https://doi.org/10.1021/jm970836l" @default.
• W2016800089 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9651160" @default.
• W2016800089 hasPublicationYear "1998" @default.
• W2016800089 type Work @default.
• W2016800089 sameAs 2016800089 @default.
• W2016800089 citedByCount "77" @default.
• W2016800089 countsByYear W20168000892012 @default.
• W2016800089 countsByYear W20168000892013 @default.
• W2016800089 countsByYear W20168000892014 @default.
• W2016800089 countsByYear W20168000892015 @default.
• W2016800089 countsByYear W20168000892016 @default.
• W2016800089 countsByYear W20168000892017 @default.
• W2016800089 countsByYear W20168000892018 @default.
• W2016800089 countsByYear W20168000892020 @default.
• W2016800089 countsByYear W20168000892021 @default.
• W2016800089 countsByYear W20168000892022 @default.
• W2016800089 crossrefType "journal-article" @default.
• W2016800089 hasAuthorship W2016800089A5005260393 @default.
• W2016800089 hasAuthorship W2016800089A5005616195 @default.
• W2016800089 hasAuthorship W2016800089A5005720957 @default.
• W2016800089 hasAuthorship W2016800089A5012030130 @default.
• W2016800089 hasAuthorship W2016800089A5023792530 @default.
• W2016800089 hasAuthorship W2016800089A5042437899 @default.
• W2016800089 hasAuthorship W2016800089A5051716463 @default.
• W2016800089 hasAuthorship W2016800089A5065145912 @default.
• W2016800089 hasAuthorship W2016800089A5078914737 @default.
• W2016800089 hasAuthorship W2016800089A5080592581 @default.
• W2016800089 hasAuthorship W2016800089A5087333213 @default.
• W2016800089 hasAuthorship W2016800089A5090092776 @default.
• W2016800089 hasAuthorship W2016800089A5091237671 @default.
• W2016800089 hasConcept C159110408 @default.
• W2016800089 hasConcept C161790260 @default.
• W2016800089 hasConcept C164361826 @default.
• W2016800089 hasConcept C181199279 @default.
• W2016800089 hasConcept C185592680 @default.
• W2016800089 hasConcept C203130289 @default.
• W2016800089 hasConcept C2775944032 @default.
• W2016800089 hasConcept C2776584326 @default.
• W2016800089 hasConcept C2776980637 @default.
• W2016800089 hasConcept C2781462491 @default.
• W2016800089 hasConcept C49453240 @default.
• W2016800089 hasConcept C55493867 @default.
• W2016800089 hasConcept C64943373 @default.
• W2016800089 hasConcept C71240020 @default.
• W2016800089 hasConcept C71924100 @default.
• W2016800089 hasConceptScore W2016800089C159110408 @default.
• W2016800089 hasConceptScore W2016800089C161790260 @default.
• W2016800089 hasConceptScore W2016800089C164361826 @default.
• W2016800089 hasConceptScore W2016800089C181199279 @default.
• W2016800089 hasConceptScore W2016800089C185592680 @default.
• W2016800089 hasConceptScore W2016800089C203130289 @default.
• W2016800089 hasConceptScore W2016800089C2775944032 @default.
• W2016800089 hasConceptScore W2016800089C2776584326 @default.
• W2016800089 hasConceptScore W2016800089C2776980637 @default.

• next