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http://purl.uniprot.org/citations/18210371http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18210371http://www.w3.org/2000/01/rdf-schema#comment"The plant extracellular matrix contains typical polysaccharides such as cellulose, hemicelluloses, and pectins that interact to form dense interwoven networks. Plant cell walls play crucial roles during development and constitute the first barrier of defense against invading pathogens. Cell wall proteomics has greatly contributed to the description of the protein content of a compartment specific to plants. Around 400 cell wall proteins (CWPs) of Arabidopsis, representing about one fourth of its estimated cell wall proteome, have been described. The main points to note are that: (i) the diversity of enzymes acting on polysaccharides suggests a great plasticity of cell walls; (ii) CWPs such as proteases, polysaccharide hydrolytic enzymes, and lipases may contribute to the generation of signals; (iii) proteins of unknown functions were identified, suggesting new roles for cell walls. Recently, the characterization of PTMs such as N- and O-glycosylations improved our knowledge of CWP structure. The presence of many glycoside hydrolases and proteases suggests a complex regulation of CWPs involving various types of post-translational events. The first 3-D structures to be resolved gave clues about the interactions between CWPs, or between CWPs and polysaccharides. Future work should include: extracting and identifying CWPs still recalcitrant to proteomics, describing the cell wall interactome, improving quantification, and unraveling the roles of each of the CWPs."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.org/dc/terms/identifier"doi:10.1002/pmic.200700938"xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/author"Albenne C."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/author"Canut H."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/author"Pont-Lezica R."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/author"Jamet E."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/author"Irshad M."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/author"Boudart G."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/name"Proteomics"xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/pages"893-908"xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/title"Recent advances in plant cell wall proteomics."xsd:string
http://purl.uniprot.org/citations/18210371http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/18210371http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18210371
http://purl.uniprot.org/citations/18210371http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18210371
http://purl.uniprot.org/uniprot/#_P0C7R4-mappedCitation-18210371http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18210371
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http://purl.uniprot.org/uniprot/#_A0A1P8B1N1-mappedCitation-18210371http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18210371
http://purl.uniprot.org/uniprot/#_A0A1P8BEK8-mappedCitation-18210371http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18210371
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