- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
1 Online-Ressource.
- Sprache
-
Englisch
- Erschienen in
-
Mechanism-based traps enable protease and hydrolase substrate discovery ; volume:602 ; number:7898 ; day:16 ; month:2 ; year:2022 ; pages:701-707 ; date:2.2022
Nature; 602, Heft 7898 (16.2.2022), 701-707, 2.2022
- Urheber
-
Tang, Shan
Beattie, Adam T.
Kafkova, Lucie
Petris, Gianluca
Huguenin-Dezot, Nicolas
Fiedler, Marc
Freeman, Matthew
Chin, Jason W.
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1038/s41586-022-04414-9
- URN
-
urn:nbn:de:101:1-2408182107599.959931476760
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:56 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Tang, Shan
- Beattie, Adam T.
- Kafkova, Lucie
- Petris, Gianluca
- Huguenin-Dezot, Nicolas
- Fiedler, Marc
- Freeman, Matthew
- Chin, Jason W.
- SpringerLink (Online service)
Ähnliche Objekte (12)
Viscometric Measurement of Protease Activities on Gelatine Substrate
Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots
Sumo-dependent substrate targeting of the SUMO protease Ulp1
Engineering of TEV protease variants with redesigned substrate specificity
Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures
Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation
Substrate recognition and cleavage by the mitochondrial rhomboid protease PARL
Block-based characterization of protease specificity from substrate sequence profile
Substrate-specificity of the DNA-protein crosslink repair protease SPRTN
Reduced sphingolipid hydrolase activities, substrate accumulation and ganglioside decline in Parkinson’s disease
Phylogenetic analyses suggest multiple changes of substrate specificity within the Glycosyl hydrolase 20 family
Viscometric Measurement of Protease Activities on Gelatine Substrate
Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots
Sumo-dependent substrate targeting of the SUMO protease Ulp1
Engineering of TEV protease variants with redesigned substrate specificity
Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures
Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation
Substrate recognition and cleavage by the mitochondrial rhomboid protease PARL
Block-based characterization of protease specificity from substrate sequence profile
Substrate-specificity of the DNA-protein crosslink repair protease SPRTN
Reduced sphingolipid hydrolase activities, substrate accumulation and ganglioside decline in Parkinson’s disease
Phylogenetic analyses suggest multiple changes of substrate specificity within the Glycosyl hydrolase 20 family
Viscometric Measurement of Protease Activities on Gelatine Substrate
Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
Oligogalacturonate hydrolase with unique substrate preference from the pulp of parsley roots
Sumo-dependent substrate targeting of the SUMO protease Ulp1
Engineering of TEV protease variants with redesigned substrate specificity
Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate–peptide complex structures
Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation
Substrate recognition and cleavage by the mitochondrial rhomboid protease PARL
Block-based characterization of protease specificity from substrate sequence profile
Substrate-specificity of the DNA-protein crosslink repair protease SPRTN
Reduced sphingolipid hydrolase activities, substrate accumulation and ganglioside decline in Parkinson’s disease