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Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase

The Journal of biological chemistry, 2016-04, Vol.291 (14), p.7742-7753

2016

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Identification of the Tau phosphorylation pattern that drives its aggregation

Proceedings of the National Academy of Sciences - PNAS, 2017-08, Vol.114 (34), p.9080-9085

2017

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Major Differences between the Self-Assembly and Seeding Behavior of Heparin-Induced and in Vitro Phosphorylated Tau and Their Modulation by Potential Inhibitors

ACS chemical biology, 2019-06, Vol.14 (6), p.1363-1379

2019

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Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy

Proceedings of the National Academy of Sciences - PNAS, 2014-03, Vol.111 (12), p.4584-4589

2014

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Bioinspired Hybrid Fluorescent Ligands for the FK1 Domain of FKBP52

Journal of medicinal chemistry, 2020-09, Vol.63 (18), p.10330-10338

2020

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A β‑Turn Motif in the Steroid Hormone Receptor’s Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52

Biochemistry (Easton), 2016-09, Vol.55 (38), p.5366-5376

2016

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The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein

Methods in molecular biology (Clifton, N.J.), 2017, Vol.1523, p.179

2017

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Phosphorylation of the Immunosuppressant FK506-Binding Protein FKBP52 by Casein Kinase II: Regulation of HSP90-Binding Activity of FKBP52

Proceedings of the National Academy of Sciences - PNAS, 1997-12, Vol.94 (26), p.14500-14505

1997

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Concomitant Neuronal Tau Deposition and FKBP52 Decrease Is an Early Feature of Different Human and Experimental Tauopathies

Journal of Alzheimer's disease, 2023-01, Vol.94 (1), p.313-331

2023

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Bio-inspired hybrid fluorescent ligands for the FK1 domain of FKBP52

Journal of medicinal chemistry, 2020

2020

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The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation: FKBP52 and Tubulin Functional interaction

The FASEB journal, 2007-09, Vol.21 (11), p.2787-97

2007

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Several regions of human estrogen receptor are involved in the formation of receptor-heat shock protein 90 complexes

The Journal of biological chemistry, 1990-11, Vol.265 (33), p.20686-20691

1990

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The Ability of the Immunophilin FKBP59-HBI to Interact with the 90-kDa Heat Shock Protein is Encoded by its Tetratricopeptide Repeat Domain

Proceedings of the National Academy of Sciences - PNAS, 1994-11, Vol.91 (23), p.11197-11201

1994

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FAP48, a New Protein That Forms Specific Complexes with Both Immunophilins FKBP59 and FKBP12

The Journal of biological chemistry, 1996-12, Vol.271 (51), p.32923-32929

1996

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Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase

Identification of the Tau phosphorylation pattern that drives its aggregation

Major Differences between the Self-Assembly and Seeding Behavior of Heparin-Induced and in Vitro Phosphorylated Tau and Their Modulation by Potential Inhibitors

Immunophilin FKBP52 induces Tau-P301L filamentous assembly in vitro and modulates its activity in a model of tauopathy

Bioinspired Hybrid Fluorescent Ligands for the FK1 Domain of FKBP52

A β‑Turn Motif in the Steroid Hormone Receptor’s Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52

The Study of Posttranslational Modifications of Tau Protein by Nuclear Magnetic Resonance Spectroscopy: Phosphorylation of Tau Protein by ERK2 Recombinant Kinase and Rat Brain Extract, and Acetylation by Recombinant Creb-Binding Protein

Phosphorylation of the Immunosuppressant FK506-Binding Protein FKBP52 by Casein Kinase II: Regulation of HSP90-Binding Activity of FKBP52

Concomitant Neuronal Tau Deposition and FKBP52 Decrease Is an Early Feature of Different Human and Experimental Tauopathies

Bio-inspired hybrid fluorescent ligands for the FK1 domain of FKBP52

The immunophilin FKBP52 specifically binds to tubulin and prevents microtubule formation: FKBP52 and Tubulin Functional interaction

Several regions of human estrogen receptor are involved in the formation of receptor-heat shock protein 90 complexes

The Ability of the Immunophilin FKBP59-HBI to Interact with the 90-kDa Heat Shock Protein is Encoded by its Tetratricopeptide Repeat Domain

FAP48, a New Protein That Forms Specific Complexes with Both Immunophilins FKBP59 and FKBP12

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