Title : Orthology Analysis and In Vivo Complementation Studies to Elucidate the Role of DIR1 during Systemic Acquired Resistance in Arabidopsis thaliana and Cucumis sativus.

Pub. Date : 2016

PMID : 27200039






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 In vitro assays to compare the capacity of recombinant AtDIR1 and targeted AtDIR1-variant proteins to bind the lipophilic probe TNS (6,P-toluidinylnaphthalene-2-sulfonate) provided evidence that conserved leucine 43 and aspartic acid 39 contribute to the size of the DIR1 hydrophobic cavity and possibly hydrophobic ligand binding. 2-(4-toluidino)-6-naphthalenesulfonic acid Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein Arabidopsis thaliana
2 In vitro assays to compare the capacity of recombinant AtDIR1 and targeted AtDIR1-variant proteins to bind the lipophilic probe TNS (6,P-toluidinylnaphthalene-2-sulfonate) provided evidence that conserved leucine 43 and aspartic acid 39 contribute to the size of the DIR1 hydrophobic cavity and possibly hydrophobic ligand binding. 2-(4-toluidino)-6-naphthalenesulfonic acid Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein Arabidopsis thaliana
3 In vitro assays to compare the capacity of recombinant AtDIR1 and targeted AtDIR1-variant proteins to bind the lipophilic probe TNS (6,P-toluidinylnaphthalene-2-sulfonate) provided evidence that conserved leucine 43 and aspartic acid 39 contribute to the size of the DIR1 hydrophobic cavity and possibly hydrophobic ligand binding. 2-(4-toluidino)-6-naphthalenesulfonic acid Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein Arabidopsis thaliana
4 In vitro assays to compare the capacity of recombinant AtDIR1 and targeted AtDIR1-variant proteins to bind the lipophilic probe TNS (6,P-toluidinylnaphthalene-2-sulfonate) provided evidence that conserved leucine 43 and aspartic acid 39 contribute to the size of the DIR1 hydrophobic cavity and possibly hydrophobic ligand binding. 2-(4-toluidino)-6-naphthalenesulfonic acid Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein Arabidopsis thaliana
5 In vitro assays to compare the capacity of recombinant AtDIR1 and targeted AtDIR1-variant proteins to bind the lipophilic probe TNS (6,P-toluidinylnaphthalene-2-sulfonate) provided evidence that conserved leucine 43 and aspartic acid 39 contribute to the size of the DIR1 hydrophobic cavity and possibly hydrophobic ligand binding. 2-(4-toluidino)-6-naphthalenesulfonic acid Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein Arabidopsis thaliana