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http://purl.uniprot.org/citations/31925978http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31925978http://www.w3.org/2000/01/rdf-schema#comment"Plants survey their environment for the presence of potentially harmful or beneficial microbes. During colonization, cell surface receptors perceive microbe-derived or modified-self ligands and initiate appropriate responses. The recognition of fungal chitin oligomers and the subsequent activation of plant immunity are well described. In contrast, the mechanisms underlying β-glucan recognition and signaling activation remain largely unexplored. Here, we systematically tested immune responses towards different β-glucan structures and show that responses vary between plant species. While leaves of the monocots Hordeum vulgare and Brachypodium distachyon can recognize longer (laminarin) and shorter (laminarihexaose) β-1,3-glucans with responses of varying intensity, duration and timing, leaves of the dicot Nicotiana benthamiana activate immunity in response to long β-1,3-glucans, whereas Arabidopsis thaliana and Capsella rubella perceive short β-1,3-glucans. Hydrolysis of the β-1,6 side-branches of laminarin demonstrated that not the glycosidic decoration but rather the degree of polymerization plays a pivotal role in the recognition of long-chain β-glucans. Moreover, in contrast to the recognition of short β-1,3-glucans in A. thaliana, perception of long β-1,3-glucans in N. benthamiana and rice is independent of CERK1, indicating that β-glucan recognition may be mediated by multiple β-glucan receptor systems."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.org/dc/terms/identifier"doi:10.1111/tpj.14688"xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Becker S."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Wawra S."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Hehemann J.H."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Rovenich H."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Zuccaro A."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Wanke A."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Schwanke F."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/author"Velte S."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/name"Plant J"xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/pages"1142-1156"xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/title"Plant species-specific recognition of long and short beta-1,3-linked glucans is mediated by different receptor systems."xsd:string
http://purl.uniprot.org/citations/31925978http://purl.uniprot.org/core/volume"102"xsd:string
http://purl.uniprot.org/citations/31925978http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31925978
http://purl.uniprot.org/citations/31925978http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31925978
http://purl.uniprot.org/uniprot/#_A8R7E6-mappedCitation-31925978http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31925978
http://purl.uniprot.org/uniprot/A8R7E6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/31925978