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Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth

Angewandte Chemie International Edition, 2012-05, Vol.51 (21), p.5247-5251

International ed. in English, 2012

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Structure of a low-population intermediate state in the release of an enzyme product

eLife, 2015-01, Vol.4

2015

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The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

Journal of molecular biology, 2010-10, Vol.402 (5), p.783-796

2010

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Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain

PloS one, 2013-06, Vol.8 (6), p.e67961-e67961

2013

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Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

Proceedings of the National Academy of Sciences - PNAS, 2011-12, Vol.108 (52), p.21057-21062

2011

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Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Journal of the American Chemical Society, 2010-11, Vol.132 (44), p.15580-15588

2010

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Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation

Journal of the American Chemical Society, 2011-05, Vol.133 (20), p.7737-7743

2011

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Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

Angewandte Chemie International Edition, 2011-07, Vol.50 (31), p.7048-7051

International ed. in English, 2011

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Mapping of Two Networks of Residues That Exhibit Structural and Dynamical Changes upon Binding in a PDZ Domain Protein

Journal of the American Chemical Society, 2008-07, Vol.130 (28), p.8931-8939

2008

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Inhibition of α‑Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α‑Synuclein Species

Biochemistry (Easton), 2017-03, Vol.56 (9), p.1177-1180

2017

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The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme

Biophysical journal, 2016-12, Vol.111 (11), p.2358-2367

2016

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Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation

Scientific reports, 2017-11, Vol.7 (1), p.15018-12, Article 15018

2017

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Predicting conformational entropy of bond vectors in proteins by networks of coupled rotators

The Journal of chemical physics, 2008-09, Vol.129 (9), p.095107-095107

2008

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Networks of Coupled Rotators: Relationship between Structures and Internal Dynamics in Metal-Binding Proteins. Applications to apo- and holo-Calbindin

Journal of the American Chemical Society, 2007-04, Vol.129 (16), p.4998-5006

2007

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Predicting conformational entropy of bond vectors in proteinsby networks of coupled rotators

The Journal of chemical physics, 2008-09, Vol.129 (9), p.095107-095107-5

2008

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Networks of coupled rotators: Relationship between structures and internal dynamics in metal-binding proteins

Journal of the American Chemical Society, 2008-04, Vol.129 (16)

2008

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Population of non-native states of lysozyme variants drives amyloid fibril formation

Journal of the American Chemical Society, 2011-04, Vol.133 (20), p.7737-7743

2011

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A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis

Protein engineering, design and selection, 2010-07, Vol.23 (7), p.499-506

2010

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Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen

Angewandte Chemie, 2012-05, Vol.124 (21), p.5339-5344

2012

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Journal of Molecular Biology

Journal of molecular biology, 2010, p.783-96

2010

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Exploring the energy landscape of human lysozyme

Dhulesia, Anne

2010

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Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

Angewandte Chemie, 2011-07, Vol.123 (31), p.7186-7189

2011

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Journal of the American Chemical Society

Journal of the American Chemical Society, 2011, p.7737-43

2011

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Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen

Angewandte Chemie, 2012-05, Vol.124 (21), p.5339-5344

2012

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Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

Angewandte Chemie, 2011-07, Vol.123 (31), p.7186-7189

2011

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Detailed Analysis of the Energy Barriers for Amyloid Fibril Growth

Structure of a low-population intermediate state in the release of an enzyme product

The Non-Core Regions of Human Lysozyme Amyloid Fibrils Influence Cytotoxicity

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

Local Cooperativity in an Amyloidogenic State of Human Lysozyme Observed at Atomic Resolution

Population of Nonnative States of Lysozyme Variants Drives Amyloid Fibril Formation

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

Mapping of Two Networks of Residues That Exhibit Structural and Dynamical Changes upon Binding in a PDZ Domain Protein

Inhibition of α‑Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α‑Synuclein Species

The Significance of the Location of Mutations for the Native-State Dynamics of Human Lysozyme

Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation

Predicting conformational entropy of bond vectors in proteins by networks of coupled rotators

Networks of Coupled Rotators: Relationship between Structures and Internal Dynamics in Metal-Binding Proteins. Applications to apo- and holo-Calbindin

Predicting conformational entropy of bond vectors in proteinsby networks of coupled rotators

Networks of coupled rotators: Relationship between structures and internal dynamics in metal-binding proteins

Population of non-native states of lysozyme variants drives amyloid fibril formation

A non-natural variant of human lysozyme (I59T) mimics the in vitro behaviour of the I56T variant that is responsible for a form of familial amyloidosis

Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen

Journal of Molecular Biology

Exploring the energy landscape of human lysozyme

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

Journal of the American Chemical Society

Analyse der Energiebarrieren für das Wachstum von Amyloidfibrillen

Disulfide Bonds Reduce the Toxicity of the Amyloid Fibrils Formed by an Extracellular Protein

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