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http://purl.uniprot.org/citations/34458755http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34458755http://www.w3.org/2000/01/rdf-schema#comment"Cellulases and related β-1,4-glucanases are essential components of lignocellulose-degrading enzyme mixtures. The detection of β-1,4-glucanase activity typically relies on monitoring the breakdown of purified lignocellulose-derived substrates or synthetic chromogenic substrates, limiting the activities which can be detected and complicating the tracing of activity back to specific components within complex enzyme mixtures. As a tool for the rapid detection and identification of β-1,4-glucanases, a series of glycosylated cyclophellitol inhibitors mimicking β-1,4-glucan oligosaccharides have been synthesised. These compounds are highly efficient inhibitors of HiCel7B, a well-known GH7 endo-β-1,4-glucanase. An elaborated activity-based probe facilitated the direct detection and identification of β-1,4-glucanases within a complex fungal secretome without any detectable cross-reactivity with β-d-glucosidases. These probes and inhibitors add valuable new capacity to the growing toolbox of cyclophellitol-derived probes for the activity-based profiling of biomass-degrading enzymes."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.org/dc/terms/identifier"doi:10.1039/d0cb00045k"xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Davies G.J."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Jiang J."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"van Wezel G.P."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"van der Marel G.A."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Overkleeft H.S."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Ram A.F.J."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Codee J.D.C."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"de Boer C."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Florea B.I."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Schroder S.P."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"McGregor N.G.S."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Reijngoud J."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/author"Peterse E."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/name"RSC Chem Biol"xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/pages"148-155"xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/title"Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases."xsd:string
http://purl.uniprot.org/citations/34458755http://purl.uniprot.org/core/volume"1"xsd:string
http://purl.uniprot.org/citations/34458755http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34458755
http://purl.uniprot.org/citations/34458755http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34458755
http://purl.uniprot.org/uniprot/#_P56680-mappedCitation-34458755http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34458755
http://purl.uniprot.org/uniprot/P56680http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34458755