Mechanism-based traps enable protease and hydrolase substrate discovery

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: 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

Creator: Tang, Shan
Beattie, Adam T.
Kafkova, Lucie
Petris, Gianluca
Huguenin-Dezot, Nicolas
Fiedler, Marc
Freeman, Matthew
Chin, Jason W.

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41586-022-04414-9

URN: urn:nbn:de:101:1-2408182107599.959931476760

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:56 AM CEST

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Tang, Shan
Beattie, Adam T.
Kafkova, Lucie
Petris, Gianluca
Huguenin-Dezot, Nicolas
Fiedler, Marc
Freeman, Matthew
Chin, Jason W.
SpringerLink (Online service)

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Mechanism-based traps enable protease and hydrolase substrate discovery

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Other Objects (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

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Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation

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Substrate-specificity of the DNA-protein crosslink repair protease SPRTN

Substrate recognition and cleavage by the mitochondrial rhomboid protease PARL

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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)

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Clostridioides difficile bile salt hydrolase activity has substrate specificity and affects biofilm formation

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Substrate recognition and cleavage by the mitochondrial rhomboid protease PARL

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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

Block-based characterization of protease specificity from substrate sequence profile

Substrate-specificity of the DNA-protein crosslink repair protease SPRTN

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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

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