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PubMed:20634289 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-124 Sentence denotes Requirement of calcium binding, myristoylation, and protein-protein interaction for the Copine BON1 function in Arabidopsis.
T2 125-232 Sentence denotes Copines are highly conserved proteins with lipid-binding activities found in animals, plants, and protists.
T3 233-364 Sentence denotes They contain two calcium-dependent phospholipid binding C2 domains at the amino terminus and a VWA domain at the carboxyl terminus.
T4 365-501 Sentence denotes The biological roles of most copines are not understood and the biochemical properties required for their functions are largely unknown.
T5 502-600 Sentence denotes The Arabidopsis copine gene BON1/CPN1 is a negative regulator of cell death and defense responses.
T6 601-687 Sentence denotes Here we probed the potential biochemical activities of BON1 through mutagenic studies.
T7 688-817 Sentence denotes We found that mutations of aspartates in the C2 domains did not alter plasma membrane localization but compromised BON1 activity.
T8 818-944 Sentence denotes Mutation at putative myristoylation residue glycine 2 altered plasma membrane localization of BON1 and rendered BON1 inactive.
T9 945-1036 Sentence denotes Mass spectrometry analysis of BON1 further suggests that the N-peptide of BON1 is modified.
T10 1037-1157 Sentence denotes Furthermore, mutations that affect the interaction between BON1 and its functional partner BAP1 abolished BON1 function.
T11 1158-1378 Sentence denotes This analysis reveals an unanticipated regulation of copine protein localization and function by calcium and lipid modification and suggests an important role in protein-protein interaction for the VWA domain of copines.