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CALM3 — MET

Text-mined interactions from Literome

Yin et al., Chem Res Toxicol 2000 : Consistent with this interpretation, a CaM mutant in which glutamines were substituted for Met ( 144 ) and Met ( 145 ) fully activates the PM-Ca-ATPase irrespective of the oxidative modification of the other seven methionines to their corresponding methionine sulfoxides
Balog et al., J Biol Chem 2003 : Mutating individual CaM Met residues to Gln demonstrated that Met-109 was required for apo-CaM activation of RyR1 but not for Ca ( 2+ ) -CaM inhibition of the channel
Bartlett et al., Biochemistry 2003 : These results are discussed in terms of a possible functional role for Met ( 144 ) and Met ( 145 ) in CaM as redox sensors that function to modulate calcium homeostasis and energy metabolism in response to conditions of oxidative stress
Balog et al., Am J Physiol Heart Circ Physiol 2006 : Site-specific substitution of individual CaM Met residues with Gln demonstrated that Met124 was required for both high-affinity CaM binding to RyR2 and for maximal CaM inhibition
Xi et al., Plant Sci 2012 : Site directed mutagenesis experiments further revealed that Met ( 506 ) and Leu ( 507 ) in the CaMBD are critical for both CaM- and DNA binding abilities of AtGT2L