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http://purl.uniprot.org/citations/21144863http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21144863http://www.w3.org/2000/01/rdf-schema#comment"ACBPs are implicated in acyl-CoA trafficking in many eukaryotes and some prokaryotes. Six genes encode proteins designated as AtACBP1-AtACBP6 in the Arabidopsis thaliana ACBP family. These ACBPs are conserved in the acyl-CoA-binding domain, but vary in size from 92 amino acids (10.4 kDa) to 668 amino acids (73.1 kDa), and are subcellularly localised to different compartments in plant cells. Results from in vitro binding assays show that their corresponding recombinant proteins exhibit differential binding affinities to acyl-CoA esters and phospholipids, implying that these ACBPs may have non-redundant biological functions in vivo. By using knockout/downregulated and overexpression lines of Arabidopsis ACBPs, recent investigations have revealed that in addition to their proposed roles in phospholipid metabolism, these ACBPs can influence plant development including early embryogenesis and leaf senescence, as well as plant stress responses including heavy metal resistance, oxidative stress, freezing tolerance and pathogen resistance. In this review, recent progress on the biochemical and functional analyses of Arabidopsis ACBPs, their links to metabolic/signalling pathways, and their potential applications in development of stress tolerance are discussed."xsd:string
http://purl.uniprot.org/citations/21144863http://purl.org/dc/terms/identifier"doi:10.1016/j.plipres.2010.11.002"xsd:string
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/author"Xiao S."xsd:string
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/author"Chye M.L."xsd:string
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/name"Prog Lipid Res"xsd:string
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/pages"141-151"xsd:string
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/title"New roles for acyl-CoA-binding proteins (ACBPs) in plant development, stress responses and lipid metabolism."xsd:string
http://purl.uniprot.org/citations/21144863http://purl.uniprot.org/core/volume"50"xsd:string
http://purl.uniprot.org/citations/21144863http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21144863
http://purl.uniprot.org/citations/21144863http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21144863
http://purl.uniprot.org/uniprot/#_P57752-mappedCitation-21144863http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21144863
http://purl.uniprot.org/uniprot/#_Q9SM23-mappedCitation-21144863http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21144863
http://purl.uniprot.org/uniprot/Q9SM23http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21144863
http://purl.uniprot.org/uniprot/P57752http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21144863