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Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chainMicrosecond molecular dynamics simulations of Mg²⁺- and K⁺-bound E1 intermediate states of the calcium pumpAtomic-level mechanisms for phospholamban regulation of the calcium pump.Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin.Reconciling binding mechanisms of intrinsically disordered proteins.The Ca2+-ATPase pump facilitates bidirectional proton transport across the sarco/endoplasmic reticulum.Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin.Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain.Tyr74 is essential for the formation, stability and function of Plasmodium falciparum triosephosphate isomerase dimer.Synthesis, anticholinesterase activity and structure-activity relationships of m-Aminobenzoic acid derivatives.Molecular docking of four beta-amyloid1-42 fragments on the alpha7 nicotinic receptor: delineating the binding site of the Abeta peptides.Structural considerations for the rational design of selective anti-trypanosomal agents: the role of the aromatic clusters at the interface of triosephosphate isomerase dimer.Leucine-rich hydrophobic clusters promote folding of the N-terminus of the intrinsically disordered transactivation domain of p53.p-Aminobenzoic acid derivatives as acetylcholinesterase inhibitors.Identification of multiple allosteric sites on the M1 muscarinic acetylcholine receptor.Backbone conformational preferences of an intrinsically disordered protein in solution.Effect of a M1 allosteric modulator on scopolamine-induced amnesia.Knowledgebase for addiction-related genes: is it possible an extrapolation to rational multi-target drug design?Exploring the possible binding sites at the interface of triosephosphate isomerase dimer as a potential target for anti-tripanosomal drug design.Preexisting domain motions underlie protonation-dependent structural transitions of the P-type Ca2+-ATPase.Docking and quantum mechanic studies on cholinesterases and their inhibitorsToward a rational design of selective multi-trypanosomatid inhibitors: a computational docking studyAromatic-aromatic interactions in the formation of the MDM2-p53 complexThe benefits of the multi-target approach in drug design and discoveryTransient stability of the helical pattern of region F19-L22 of the N-terminal domain of p53: a molecular dynamics simulation studyFully flexible docking models of the complex between alpha7 nicotinic receptor and a potent heptapeptide inhibitor of the beta-amyloid peptide bindingStructural basis for relief of phospholamban-mediated inhibition of the sarcoplasmic reticulum Ca2+-ATPase at saturating Ca2+ conditions
P50
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P50
description
researcher
@en
wetenschapper
@nl
name
Michel Espinoza-Fonseca
@en
Michel Espinoza-Fonseca
@nl
type
label
Michel Espinoza-Fonseca
@en
Michel Espinoza-Fonseca
@nl
prefLabel
Michel Espinoza-Fonseca
@en
Michel Espinoza-Fonseca
@nl
P106
P31
P496
0000-0002-7356-5681