IndraLab

Statements

MLO binds CALM1. 14 / 14
| 14
sparser
"This may indicate that CAM binding to MLO proteins is a fine-tuned and balanced process, highlighting its putative physiological relevance in the context of MLO function."
37767715
sparser
"Site-directed mutagenesis has revealed key amino acid residues in the barley Mlo calcium-binding domain (CAMBD) that, when mutated, affect the MLO-CAM association."
36747653
sparser
"Our data shed further light on the interaction of MLO and CAM proteins and provide a comprehensive comparative assessment of different types of protein-protein interaction assays with wild-type and mutant versions of an integral membrane protein."
36747653
sparser
"Site-directed mutagenesis has revealed the importance of key hydrophobic amino acid residues within the CAMBD for the establishment of the MLO-CAM interaction."
36747653
sparser
"Amino acid substitutions of these essential residues with positively charged arginines largely prevented the calcium-dependent binding of CAM to the CAMBDs of barley and rice MLO proteins ( xref ; xref )."
36747653
sparser
"This mutation is analogous to the one previously found to abolish CAM binding to barley and rice MLO proteins ( xref ; xref )."
36747653
sparser
"This may indicate that CAM binding to MLO proteins is a fine-tuned and balanced process, highlighting its putative physiological relevance in the context of MLO function."
36747653
sparser
"This binding is prohibited by mutation of two amino acid residues (L 18 R and W 21 R, corresponding to L 456 R and W 459 R in full-length MLO2) that are in analogous positions within the CAMBD to those that were previously identified as being essential for the binding of CAM to barley and rice MLO proteins ( xref ; xref )."
36747653
sparser
"Site-directed mutagenesis has revealed key amino acid residues in the barley Mlo calmodulin-binding domain (CAMBD) that, when mutated, affect the MLO–CAM association."
37767715
sparser
"Our data shed further light on the interaction of MLO and CAM proteins and provide a comprehensive comparative assessment of different types of protein–protein interaction assays with wild-type and mutant versions of an integral membrane protein."
37767715
sparser
"Site-directed mutagenesis has revealed the importance of key hydrophobic amino acid residues within the CAMBD for the establishment of the MLO–CAM interaction."
37767715
sparser
"This binding is prohibited by mutation of two amino acid residues (L 18 R and W 21 R, corresponding to L 456 R and W 459 R in full-length MLO2) that are in analogous positions within the CAMBD to those that were previously identified as being essential for the binding of CAM to MLO proteins in monocotyledonous plants (barley and rice; [ xref , xref ])."
37767715
sparser
"As reported previously, the barley MLO C-terminus interacted with soy bean CaM1."
34073116
sparser
"This mutation is analogous to the one previously found to abolish CAM binding to barley and rice MLO proteins [ xref , xref ]."
37767715