Matches in SemOpenAlex for { <https://semopenalex.org/work/W4247577108> ?p ?o ?g. }
Showing items 1 to 89 of
89
with 100 items per page.
- W4247577108 endingPage "10555" @default.
- W4247577108 startingPage "10552" @default.
- W4247577108 abstract "Abstract Gaucher disease is caused by mutations in human acid β‐glucosidase or glucocerebrosidase (GCase), the enzyme responsible for hydrolysis of glucosyl ceramide in the lysosomes. Imino‐ and azasugars such as 1‐deoxynojirimycin and isofagomine are strong inhibitors of the enzyme and are of interest in pharmacological chaperone therapy of the disease. Despite several crystal structures of the enzyme with the imino‐ and azasugars bound in the active site having been resolved, the actual acid–base chemistry of the binding is not known. In this study we show, using photoinduced electron transfer (PET), that 1‐deoxynojirimycin and isofagomine derivatives are protonated by human acid β‐glucosidase when bound, even if they are completely unprotonated outside the enzyme. While isofagomine derivative protonation to some degree was foreshadowed by earlier crystal structures, 1‐deoxynojirimycin derivatives were not believed to act as basic amines in the enzyme." @default.
- W4247577108 created "2022-05-12" @default.
- W4247577108 creator A5010759964 @default.
- W4247577108 creator A5020570291 @default.
- W4247577108 creator A5027669843 @default.
- W4247577108 creator A5039610045 @default.
- W4247577108 creator A5056168495 @default.
- W4247577108 creator A5077968940 @default.
- W4247577108 creator A5078094969 @default.
- W4247577108 date "2020-04-22" @default.
- W4247577108 modified "2023-09-25" @default.
- W4247577108 title "Imino‐ and Azasugar Protonation Inside Human Acid β‐Glucosidase, the Enzyme that is Defective in Gaucher Disease" @default.
- W4247577108 cites W1833787853 @default.
- W4247577108 cites W1975596553 @default.
- W4247577108 cites W1976082900 @default.
- W4247577108 cites W1992491472 @default.
- W4247577108 cites W2024942671 @default.
- W4247577108 cites W2054690534 @default.
- W4247577108 cites W2066022058 @default.
- W4247577108 cites W2077381233 @default.
- W4247577108 cites W2080264145 @default.
- W4247577108 cites W2108929776 @default.
- W4247577108 cites W2123460986 @default.
- W4247577108 cites W2125478478 @default.
- W4247577108 cites W2142115754 @default.
- W4247577108 cites W2162325730 @default.
- W4247577108 cites W2163072183 @default.
- W4247577108 cites W2183090606 @default.
- W4247577108 cites W2252918399 @default.
- W4247577108 cites W2410855987 @default.
- W4247577108 cites W2588291989 @default.
- W4247577108 cites W2753942012 @default.
- W4247577108 cites W4237461948 @default.
- W4247577108 doi "https://doi.org/10.1002/ange.202002850" @default.
- W4247577108 hasPublicationYear "2020" @default.
- W4247577108 type Work @default.
- W4247577108 citedByCount "6" @default.
- W4247577108 countsByYear W42475771082021 @default.
- W4247577108 countsByYear W42475771082022 @default.
- W4247577108 crossrefType "journal-article" @default.
- W4247577108 hasAuthorship W4247577108A5010759964 @default.
- W4247577108 hasAuthorship W4247577108A5020570291 @default.
- W4247577108 hasAuthorship W4247577108A5027669843 @default.
- W4247577108 hasAuthorship W4247577108A5039610045 @default.
- W4247577108 hasAuthorship W4247577108A5056168495 @default.
- W4247577108 hasAuthorship W4247577108A5077968940 @default.
- W4247577108 hasAuthorship W4247577108A5078094969 @default.
- W4247577108 hasConcept C145148216 @default.
- W4247577108 hasConcept C178790620 @default.
- W4247577108 hasConcept C181199279 @default.
- W4247577108 hasConcept C185592680 @default.
- W4247577108 hasConcept C2780120296 @default.
- W4247577108 hasConcept C2780674200 @default.
- W4247577108 hasConcept C30095370 @default.
- W4247577108 hasConcept C55493867 @default.
- W4247577108 hasConcept C71240020 @default.
- W4247577108 hasConcept C94412978 @default.
- W4247577108 hasConceptScore W4247577108C145148216 @default.
- W4247577108 hasConceptScore W4247577108C178790620 @default.
- W4247577108 hasConceptScore W4247577108C181199279 @default.
- W4247577108 hasConceptScore W4247577108C185592680 @default.
- W4247577108 hasConceptScore W4247577108C2780120296 @default.
- W4247577108 hasConceptScore W4247577108C2780674200 @default.
- W4247577108 hasConceptScore W4247577108C30095370 @default.
- W4247577108 hasConceptScore W4247577108C55493867 @default.
- W4247577108 hasConceptScore W4247577108C71240020 @default.
- W4247577108 hasConceptScore W4247577108C94412978 @default.
- W4247577108 hasFunder F4320310459 @default.
- W4247577108 hasFunder F4320321873 @default.
- W4247577108 hasIssue "26" @default.
- W4247577108 hasLocation W42475771081 @default.
- W4247577108 hasOpenAccess W4247577108 @default.
- W4247577108 hasPrimaryLocation W42475771081 @default.
- W4247577108 hasRelatedWork W107855623 @default.
- W4247577108 hasRelatedWork W117444414 @default.
- W4247577108 hasRelatedWork W2076235415 @default.
- W4247577108 hasRelatedWork W2116806337 @default.
- W4247577108 hasRelatedWork W2342443897 @default.
- W4247577108 hasRelatedWork W2381802603 @default.
- W4247577108 hasRelatedWork W2950639335 @default.
- W4247577108 hasRelatedWork W3005352396 @default.
- W4247577108 hasRelatedWork W3011412256 @default.
- W4247577108 hasRelatedWork W4247577108 @default.
- W4247577108 hasVolume "132" @default.
- W4247577108 isParatext "false" @default.
- W4247577108 isRetracted "false" @default.
- W4247577108 workType "article" @default.