about
Effect of intracellular loop 3 on intrinsic dynamics of human β2-adrenergic receptor.Discovery of high affinity ligands for β2-adrenergic receptor through pharmacophore-based high-throughput virtual screening and docking.Investigation of allosteric coupling in human β2-adrenergic receptor in the presence of intracellular loop 3.How an Inhibitor Bound to Subunit Interface Alters Triosephosphate Isomerase DynamicsA docking study using atomistic conformers generated via elastic network model for cyclosporin A/cyclophilin A complex.Assessing protein-ligand binding modes with computational tools: the case of PDE4B.Molecular Docking Study Based on Pharmacophore Modeling for Novel PhosphodiesteraseIV Inhibitors.Structural analysis of peptide fragments following the hydrolysis of bovine serum albumin by trypsin and chymotrypsin.Transmembrane helix 6 observed at the interface of β2AR homodimers in blind docking studiesLigand-binding affinity of alternative conformers of human β2 -adrenergic receptor in the presence of intracellular loop 3 (ICL3) and their potential use in virtual screening studiesIntrinsic Dynamics and Causality in Correlated Motions Unraveled in Two Distinct Inactive States of Human β2-Adrenergic ReceptorDistinctive Communication Networks in Inactive States of β2 -Adrenergic Receptor: Mutual Information and Entropy Transfer Analysis
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Q35037321-71D247BC-8F74-4B23-AFB9-283C44EC38EFQ35228099-9A4D41C2-80CF-4B07-8AD9-973BD6A67F92Q36066206-D70EC40E-2EB6-4AB9-BF96-37A82291C65EQ42083172-785B3C6D-A8EF-4583-B100-4C949791BB12Q45984545-210B79BA-EA01-41D7-82CE-35792FD07A6EQ48113134-D7CD8D68-C6A0-4BAA-A606-587779861648Q51603501-F0D8F205-1EAC-4E5B-A330-1074AD98A4B1Q53184326-3D8373A2-3D88-45D9-93C8-8786DD6EE577Q85644700-2AD237B4-4AFC-48F3-8065-CEE6BC0531ACQ91023706-DBA07C44-43F9-42AF-94D4-834AA04A9A6FQ92847065-8D75FD40-6FA3-4A9C-B343-65E45F9D7FB6Q96339144-6710B79F-5131-4AF8-9FF9-7AEB74E48340
P50
description
investigador
@es
researcher
@en
name
E Demet Akten
@en
type
label
E Demet Akten
@en
prefLabel
E Demet Akten
@en
P31
P496
0000-0002-0358-3171