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Cell signaling, post-translational protein modifications and NMR spectroscopy

Journal of biomolecular NMR, 2012-11, Vol.54 (3), p.217-236

2012

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Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B

The Journal of biological chemistry, 2009-05, Vol.284 (20), p.13589-13601

2009

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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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Characterization of the AT180 epitope of phosphorylated Tau protein by a combined nuclear magnetic resonance and fluorescence spectroscopy approach

Biochemical and biophysical research communications, 2011-09, Vol.412 (4), p.743-746

2011

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Systematic Identification of Tubulin-interacting Fragments of the Microtubule-associated Protein Tau Leads to a Highly Efficient Promoter of Microtubule Assembly

The Journal of biological chemistry, 2011-09, Vol.286 (38), p.33358-33368

2011

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Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A

Biochemistry (Easton), 2017-06, Vol.56 (24), p.3029-3048

2017

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Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy

Biochemistry (Easton), 2006-10, Vol.45 (41), p.12560-12572

2006

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A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication

The Journal of biological chemistry, 2015-07, Vol.290 (31), p.19104-19120

2015

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Hepatitis C Virus NS5B and Host Cyclophilin A Share a Common Binding Site on NS5A

The Journal of biological chemistry, 2012-12, Vol.287 (53), p.44249-44260

2012

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Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded

Biochemical and biophysical research communications, 2009-04, Vol.381 (4), p.634-638

2009

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Proline-Rich Region II (PRR2) Plays an Important Role in Tau-Glycan Interaction: An NMR Study

Biomolecules (Basel, Switzerland), 2022-10, Vol.12 (11), p.1573

2022

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Elucidating Tau function and dysfunction in the era of cryo-EM

The Journal of biological chemistry, 2019-06, Vol.294 (24), p.9316-9325

2019

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NMR Investigation of the Interaction between the Neuronal Protein Tau and the Microtubules

Biochemistry (Easton), 2007-03, Vol.46 (11), p.3055-3064

2007

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A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge

Biochemical and biophysical research communications, 2014-03, Vol.445 (2), p.299-303

2014

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Comparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho‐form distributions

Molecular systems biology, 2011-04, Vol.7 (1), p.482-n/a

2011

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The domain 2 of the HCV NS5A protein is intrinsically unstructured

Protein and peptide letters, 2010-08, Vol.17 (8), p.1012-1018

2010

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NMR Meets Tau: Insights into Its Function and Pathology

Biomolecules (Basel, Switzerland), 2016-06, Vol.6 (2), p.28

2016

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Molecular Basis for an Ancient Partnership between Prolyl Isomerase Pin1 and Phosphatase Inhibitor-2

Biochemistry (Easton), 2011-08, Vol.50 (30), p.6567-6578

2011

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Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein

FEBS letters, 2005-08, Vol.579 (19), p.4159-4164

2005

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NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease

Biochemical Society transactions, 2010-08, Vol.38 (4), p.1006-1011

2010

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The Peptidyl Prolyl cis/trans-Isomerase Pin1 Recognizes the Phospho-Thr212-Pro213 Site on Tau

Biochemistry (Easton), 2004-02, Vol.43 (7), p.2032-2040

2004

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Structural and Functional Characterization of the Interaction between Cyclophilin B and a Heparin-derived Oligosaccharide

The Journal of biological chemistry, 2007-11, Vol.282 (47), p.34148-34158

2007

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Oleuropein and derivatives from olives as Tau aggregation inhibitors

Neurochemistry international, 2011-05, Vol.58 (6), p.700-707

2011

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Tau Aggregation in Alzheimer's Disease: What Role for Phosphorylation?

Prion, 2007-01, Vol.1 (1), p.21-25

2007

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Futile Encounter Engineering of the DSR‑M Dextransucrase Modifies the Resulting Polymer Length

Biochemistry (Easton), 2019-06, Vol.58 (25), p.2853-2859

2019

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Cell signaling, post-translational protein modifications and NMR spectroscopy

Hepatitis C Virus NS5A Protein Is a Substrate for the Peptidyl-prolyl cis/trans Isomerase Activity of Cyclophilins A and B

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

Characterization of the AT180 epitope of phosphorylated Tau protein by a combined nuclear magnetic resonance and fluorescence spectroscopy approach

Systematic Identification of Tubulin-interacting Fragments of the Microtubule-associated Protein Tau Leads to a Highly Efficient Promoter of Microtubule Assembly

Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A

Structural Impact of Heparin Binding to Full-Length Tau As Studied by NMR Spectroscopy

A Proline-Tryptophan Turn in the Intrinsically Disordered Domain 2 of NS5A Protein Is Essential for Hepatitis C Virus RNA Replication

Hepatitis C Virus NS5B and Host Cyclophilin A Share a Common Binding Site on NS5A

Domain 3 of non-structural protein 5A from hepatitis C virus is natively unfolded

Proline-Rich Region II (PRR2) Plays an Important Role in Tau-Glycan Interaction: An NMR Study

Elucidating Tau function and dysfunction in the era of cryo-EM

NMR Investigation of the Interaction between the Neuronal Protein Tau and the Microtubules

A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge

Comparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho‐form distributions

The domain 2 of the HCV NS5A protein is intrinsically unstructured

NMR Meets Tau: Insights into Its Function and Pathology

Molecular Basis for an Ancient Partnership between Prolyl Isomerase Pin1 and Phosphatase Inhibitor-2

Regulation of Pin1 peptidyl-prolyl cis/trans isomerase activity by its WW binding module on a multi-phosphorylated peptide of Tau protein

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease

The Peptidyl Prolyl cis/trans-Isomerase Pin1 Recognizes the Phospho-Thr212-Pro213 Site on Tau

Structural and Functional Characterization of the Interaction between Cyclophilin B and a Heparin-derived Oligosaccharide

Oleuropein and derivatives from olives as Tau aggregation inhibitors

Tau Aggregation in Alzheimer's Disease: What Role for Phosphorylation?

Futile Encounter Engineering of the DSR‑M Dextransucrase Modifies the Resulting Polymer Length

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