Matches in UGent Biblio for { <https://biblio.ugent.be/publication/1266393#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B337650.
- aggregation creator B337651.
- aggregation creator B337652.
- aggregation creator B337653.
- aggregation creator B337654.
- aggregation creator B337655.
- aggregation creator B337656.
- aggregation creator B337657.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2011".
- aggregation format "application/pdf".
- aggregation hasFormat 1266393.bibtex.
- aggregation hasFormat 1266393.csv.
- aggregation hasFormat 1266393.dc.
- aggregation hasFormat 1266393.didl.
- aggregation hasFormat 1266393.doc.
- aggregation hasFormat 1266393.json.
- aggregation hasFormat 1266393.mets.
- aggregation hasFormat 1266393.mods.
- aggregation hasFormat 1266393.rdf.
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- aggregation hasFormat 1266393.txt.
- aggregation hasFormat 1266393.xls.
- aggregation hasFormat 1266393.yaml.
- aggregation isPartOf urn:issn:0028-0836.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "A novel protein family mediates Casparian strip formation in the endodermis".
- aggregation abstract "Polarized epithelia are fundamental to multicellular life. In animal epithelia, conserved junctional complexes establish membrane diffusion barriers, cellular adherence and sealing of the extracellular space(1). Plant cellular barriers are of independent evolutionary origin. The root endodermis strongly resembles a polarized epithelium and functions in nutrient uptake and stress resistance(2). Its defining features are the Casparian strips, belts of specialized cell wall material that generate an extracellular diffusion barrier(2). The mechanisms localizing Casparian strips are unknown. Here we identify and characterize a family of transmembrane proteins of previously unknown function. These 'CASPs' (Casparian strip membrane domain proteins) specifically mark a membrane domain that predicts the formation of Casparian strips. CASP1 displays numerous features required for a constituent of a plant junctional complex: it forms complexes with other CASPs; it becomes immobile upon localization; and it sediments like a large polymer. CASP double mutants display disorganized Casparian strips, demonstrating a role for CASPs in structuring and localizing this cell wall modification. To our knowledge, CASPs are the first molecular factors that are shown to establish a plasma membrane and extracellular diffusion barrier in plants, and represent a novel way of epithelial barrier formation in eukaryotes.".
- aggregation authorList BK634450.
- aggregation endPage "U564".
- aggregation issue "7347".
- aggregation startPage "380".
- aggregation volume "473".
- aggregation aggregates 1266545.
- aggregation isDescribedBy 1266393.
- aggregation similarTo nature10070.
- aggregation similarTo LU-1266393.