Journal: Molecules

Article Title: Towards Imaging Tau Hyperphosphorylation: Is DYRK1A a Potential Target for Imaging Hyperphosphorylation of Tau? Molecular Modeling Assessment and Synthesis of [ 125 I]Radioiodinated DYRK1A Inhibitor

doi: 10.3390/molecules30050990

Figure Lengend Snippet: Phosphokinases and Tau phosphosites.

Article Snippet: Using Chimera-Autodock (version 1.17.3; 2023) as previously described for our experiments with Tau ligands [ ], DYRK1A (PDB 4YLL [ ]) was used to model the various molecules for DYRK1A binding energy calculations.

Techniques: Clinical Proteomics

Journal: Molecules

Article Title: Towards Imaging Tau Hyperphosphorylation: Is DYRK1A a Potential Target for Imaging Hyperphosphorylation of Tau? Molecular Modeling Assessment and Synthesis of [ 125 I]Radioiodinated DYRK1A Inhibitor

doi: 10.3390/molecules30050990

Figure Lengend Snippet: Schematic showing chromosome 21 with the Down’s syndrome critical region (DSCR) highlighted. Expression of DYRK1A is regulated by DSCR and is upregulated in Down’s syndrome (#1 blue dotted line). Membrane-bound DYRK1A may play a role in the hyperphosphorylation of Tau (#2 blue dotted line), resulting in the formation of neurofibrillary tangles (#3 blue dotted line). (Orange star: DYRK1A kinase; Green circles: normal Tau; Orange circles: phosphorylated Tau; Orange lines: Tau tangles).

Article Snippet: Using Chimera-Autodock (version 1.17.3; 2023) as previously described for our experiments with Tau ligands [ ], DYRK1A (PDB 4YLL [ ]) was used to model the various molecules for DYRK1A binding energy calculations.

Techniques: Expressing, Membrane

Journal: Molecules

Article Title: Towards Imaging Tau Hyperphosphorylation: Is DYRK1A a Potential Target for Imaging Hyperphosphorylation of Tau? Molecular Modeling Assessment and Synthesis of [ 125 I]Radioiodinated DYRK1A Inhibitor

doi: 10.3390/molecules30050990

Figure Lengend Snippet: Chemical structures of compounds with reported binding profiles. 1 . Harmine, binds to DYRK1A and MAO-A; 2 . 10-bromo-2-iodo-11 H -indolo[3,2-c]quinoline-6-carboxylic acid (4E3) binds to DYRK1A; 3 . 10-iodo-11 H -indolo[3,2-c]quinoline-6-carboxylic acid (KuFal184) binds to DYRK1A.

Article Snippet: Using Chimera-Autodock (version 1.17.3; 2023) as previously described for our experiments with Tau ligands [ ], DYRK1A (PDB 4YLL [ ]) was used to model the various molecules for DYRK1A binding energy calculations.

Techniques: Binding Assay

Journal: Molecules

Article Title: Towards Imaging Tau Hyperphosphorylation: Is DYRK1A a Potential Target for Imaging Hyperphosphorylation of Tau? Molecular Modeling Assessment and Synthesis of [ 125 I]Radioiodinated DYRK1A Inhibitor

doi: 10.3390/molecules30050990

Figure Lengend Snippet: DYRK1A and Tau binding energies of agents.

Article Snippet: Using Chimera-Autodock (version 1.17.3; 2023) as previously described for our experiments with Tau ligands [ ], DYRK1A (PDB 4YLL [ ]) was used to model the various molecules for DYRK1A binding energy calculations.

Techniques: Binding Assay

Journal: Molecules

Article Title: Towards Imaging Tau Hyperphosphorylation: Is DYRK1A a Potential Target for Imaging Hyperphosphorylation of Tau? Molecular Modeling Assessment and Synthesis of [ 125 I]Radioiodinated DYRK1A Inhibitor

doi: 10.3390/molecules30050990

Figure Lengend Snippet: ( A ). DYRK1A (PDB 4YLL protein structure used for binding energy measurements of various molecules; ( B ). Interaction of KuFAL184 at the binding site of DYRK1A. Three residues of DYRK1A binding site have been highlighted in red, including Leu241, Asp307, and Lys188. The high affinity of KuFal184 is driven by the “salt bridge” interaction between the carboxylate group in KuFal184 and Lys188.

Article Snippet: Using Chimera-Autodock (version 1.17.3; 2023) as previously described for our experiments with Tau ligands [ ], DYRK1A (PDB 4YLL [ ]) was used to model the various molecules for DYRK1A binding energy calculations.

Techniques: Binding Assay

Journal: Molecules

Article Title: Towards Imaging Tau Hyperphosphorylation: Is DYRK1A a Potential Target for Imaging Hyperphosphorylation of Tau? Molecular Modeling Assessment and Synthesis of [ 125 I]Radioiodinated DYRK1A Inhibitor

doi: 10.3390/molecules30050990

Figure Lengend Snippet: DYRK1A (PDB 4YLL ) Chimera-Autodock molecular models: energy-minimized comparative chemical structures in the binding site. ( A ). Energy-minimized comparison of KuFal184 and IPPI at the DYRK1A binding site; ( B ). Energy-minimized comparison of KuFal184 and MK-6240 at the DYRK1A binding site; ( C ). Energy-minimized comparison of harmine and IPPI at the DYRK1A binding site; ( D ). Energy-minimized comparison of harmine and MK-6240 at the DYRK1A binding site.

Article Snippet: Using Chimera-Autodock (version 1.17.3; 2023) as previously described for our experiments with Tau ligands [ ], DYRK1A (PDB 4YLL [ ]) was used to model the various molecules for DYRK1A binding energy calculations.

Techniques: Binding Assay, Comparison