Varnavas D. Mouchlis
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View article: The mechanism of allosteric regulation of calcium-independent phospholipase A <sub>2</sub> by ATP and calmodulin binding to the ankyrin domain
The mechanism of allosteric regulation of calcium-independent phospholipase A <sub>2</sub> by ATP and calmodulin binding to the ankyrin domain Open
Group VIA calcium-independent phospholipase A 2 (iPLA 2 ) is a member of the PLA 2 superfamily that exhibits calcium-independent activity in contrast to the other two major types, secreted phospholipase A 2 (sPLA 2 ) and cytosolic phosphol…
View article: Identification of two novel chemical classes of Autotaxin (ATX) inhibitors using Enalos Asclepios KNIME nodes
Identification of two novel chemical classes of Autotaxin (ATX) inhibitors using Enalos Asclepios KNIME nodes Open
View article: Identification of Two Novel Chemical Classes of Autotaxin (ATX) Inhibitors Using Enalos Asclepios KNIME Nodes
Identification of Two Novel Chemical Classes of Autotaxin (ATX) Inhibitors Using Enalos Asclepios KNIME Nodes Open
View article: Correction to “Highly Potent 2-Oxoester Inhibitors of Cytosolic Phospholipase A<sub>2</sub> (GIVA cPLA<sub>2</sub>)”
Correction to “Highly Potent 2-Oxoester Inhibitors of Cytosolic Phospholipase A<sub>2</sub> (GIVA cPLA<sub>2</sub>)” Open
[This corrects the article DOI: 10.1021/acsomega.8b01214.].
View article: Membrane Allostery Recruits Unique Hydrophobic Binding Sites Promoting Substrate Specificity of Lipolytic Enzymes
Membrane Allostery Recruits Unique Hydrophobic Binding Sites Promoting Substrate Specificity of Lipolytic Enzymes Open
View article: Allosteric Regulation by Membranes Controls Specificity of Lipolytic Enzymes through Recruitment of Unique Hydrophobic Binding Pockets
Allosteric Regulation by Membranes Controls Specificity of Lipolytic Enzymes through Recruitment of Unique Hydrophobic Binding Pockets Open
View article: 2-Oxoesters: A Novel Class of Potent and Selective Inhibitors of Cytosolic Group IVA Phospholipase A2
2-Oxoesters: A Novel Class of Potent and Selective Inhibitors of Cytosolic Group IVA Phospholipase A2 Open
Cytosolic phospholipase A 2 (GIVA cPLA 2 ) is the only PLA 2 that exhibits a marked preference for hydrolysis of arachidonic acid containing phospholipid substrates releasing free arachidonic acid and lysophospholipids and giving rise to t…
View article: 2-Oxoamides based on dipeptides as selective calcium-independent phospholipase A2 inhibitors
2-Oxoamides based on dipeptides as selective calcium-independent phospholipase A2 inhibitors Open