http://purl.uniprot.org/citations/31925978 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/31925978 | http://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/31925978 | http://purl.org/dc/terms/identifier | "doi:10.1111/tpj.14688"xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Becker S."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Wawra S."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Hehemann J.H."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Rovenich H."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Zuccaro A."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Wanke A."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Schwanke F."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/author | "Velte S."xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/name | "Plant J"xsd:string |
http://purl.uniprot.org/citations/31925978 | http://purl.uniprot.org/core/pages | "1142-1156"xsd:string |
http://purl.uniprot.org/citations/31925978 | http://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/31925978 | http://purl.uniprot.org/core/volume | "102"xsd:string |
http://purl.uniprot.org/citations/31925978 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/31925978 |
http://purl.uniprot.org/citations/31925978 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/31925978 |
http://purl.uniprot.org/uniprot/#_A8R7E6-mappedCitation-31925978 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/31925978 |
http://purl.uniprot.org/uniprot/A8R7E6 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/31925978 |