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The Correct Use of "Average" Fluorescence Parameters

Photochemistry and photobiology, 1998-05, Vol.67 (5), p.475-486

1998

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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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The Correct Use of “Average” Fluorescence Parameters

Photochemistry and photobiology, 1998, Vol.67 (5), p.475

1998

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

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

2007

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Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy

Protein and peptide letters, 2006-03, Vol.13 (3), p.235

2006

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Fluorescence Lifetime Standards for Time and Frequency Domain Fluorescence Spectroscopy

Analytical chemistry (Washington), 2007-03, Vol.79 (5), p.2137-2149

2007

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Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules

The FASEB journal, 2009-04, Vol.23 (4), p.1146-1152

2009

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Mechanism of Fluorescence and Conformational Changes of the Sarcoplasmic Calcium Binding Protein of the Sand Worm Nereis diversicolor upon Ca2+ or Mg2+ Binding

Biophysical journal, 2003-09, Vol.85 (3), p.1882-1893

2003

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Towards understanding the phosphorylation code of tau

Biochemical Society transactions, 2012-08, Vol.40 (4), p.698

2012

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NMR Analysis of a Tau Phosphorylation Pattern

Journal of the American Chemical Society, 2006-03, Vol.128 (11), p.3575-3583

2006

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Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and saturating concentrations of Calcofluor White. A fluorescence study

Carbohydrate research, 2000-07, Vol.327 (3), p.333-340

2000

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Accepting its Random Coil Nature Allows a Partial NMR Assignment of the Neuronal Tau Protein

Chembiochem : a European journal of chemical biology, 2004-12, Vol.5 (12), p.1639-1646

2004

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Equilibrium and Kinetic Study of the Conformational Transition toward the Active State of p21Ha-, Induced by the Binding of BeF3− to the GDP-bound State, in the Absence of GTPase-activating Proteins

The Journal of biological chemistry, 1997-09, Vol.272 (37), p.23138-23143

1997

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Regions of Tau Implicated in the Paired Helical Fragment Core as Defined by NMR

Chembiochem : a European journal of chemical biology, 2005-10, Vol.6 (10), p.1849-1856

2005

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Equilibrium and Kinetic Study of the Conformational Transition toward the Active State of p21Ha-ras, Induced by the Binding of BeF3− to the GDP-bound State, in the Absence of GTPase-activating Proteins

The Journal of biological chemistry, 1997-09, Vol.272 (37), p.23138-23143

1997

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Proline-Directed Random-Coil Chemical Shift Values as a Tool for the NMR Assignment of the Tau Phosphorylation Sites

Chembiochem : a European journal of chemical biology, 2004-01, Vol.5 (1), p.73-78

2004

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High-Resolution Magic Angle Spinning NMR of the Neuronal Tau Protein Integrated in Alzheimer's-Like Paired Helical Fragments

Journal of the American Chemical Society, 2005-07, Vol.127 (29), p.10138-10139

2005

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A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data

Protein science, 2000-01, Vol.9 (1), p.158-169

2000

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Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm nereis diversicolor upon Ca(2+) or Mg(2+) binding

Biophysical journal, 2003-09, Vol.85 (3), p.1882

2003

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Tryptophan Properties in Fluorescence and Functional Stability of Plasminogen Activator Inhibitor 1

Biophysical journal, 2003-07, Vol.85 (1), p.501-510

2003

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Fluorescence quenching in the DsbA protein from Escherichia coli: Complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan

Proteins, structure, function, and bioinformatics, 1999-11, Vol.37 (2), p.253-263

1999

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The Correct Use of "Average" Fluorescence Parameters

Photochemistry and photobiology, 1998-05, Vol.67 (5), p.475-486

1998

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Quenching of Tryptophan Fluorescence by the Active-Site Disulfide Bridge in the DsbA Protein from Escherichia coli

Biochemistry (Easton), 1997-05, Vol.36 (21), p.6391-6400

1997

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Proline-Directed Random-Coil Chemical Shift Values as a Tool for the NMR Assignment of the Tau Phosphorylation Sites

Chembiochem : a European journal of chemical biology, 2004-03, Vol.5 (3), p.256-256

2004

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The Correct Use of "Average" Fluorescence Parameters

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

The Correct Use of “Average” Fluorescence Parameters

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

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

Studying the natively unfolded neuronal Tau protein by solution NMR spectroscopy

Fluorescence Lifetime Standards for Time and Frequency Domain Fluorescence Spectroscopy

Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules

Mechanism of Fluorescence and Conformational Changes of the Sarcoplasmic Calcium Binding Protein of the Sand Worm Nereis diversicolor upon Ca2+ or Mg2+ Binding

Towards understanding the phosphorylation code of tau

NMR Analysis of a Tau Phosphorylation Pattern

Interaction between carbohydrate residues of α1-acid glycoprotein (orosomucoid) and saturating concentrations of Calcofluor White. A fluorescence study

Accepting its Random Coil Nature Allows a Partial NMR Assignment of the Neuronal Tau Protein

Equilibrium and Kinetic Study of the Conformational Transition toward the Active State of p21Ha-, Induced by the Binding of BeF3− to the GDP-bound State, in the Absence of GTPase-activating Proteins

Regions of Tau Implicated in the Paired Helical Fragment Core as Defined by NMR

Equilibrium and Kinetic Study of the Conformational Transition toward the Active State of p21Ha-ras, Induced by the Binding of BeF3− to the GDP-bound State, in the Absence of GTPase-activating Proteins

Proline-Directed Random-Coil Chemical Shift Values as a Tool for the NMR Assignment of the Tau Phosphorylation Sites

High-Resolution Magic Angle Spinning NMR of the Neuronal Tau Protein Integrated in Alzheimer's-Like Paired Helical Fragments

A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data

Mechanism of fluorescence and conformational changes of the sarcoplasmic calcium binding protein of the sand worm nereis diversicolor upon Ca(2+) or Mg(2+) binding

Tryptophan Properties in Fluorescence and Functional Stability of Plasminogen Activator Inhibitor 1

Fluorescence quenching in the DsbA protein from Escherichia coli: Complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan

The Correct Use of "Average" Fluorescence Parameters

Quenching of Tryptophan Fluorescence by the Active-Site Disulfide Bridge in the DsbA Protein from Escherichia coli

Proline-Directed Random-Coil Chemical Shift Values as a Tool for the NMR Assignment of the Tau Phosphorylation Sites

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