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Food chain transport of nanoparticles affects behaviour and fat metabolism in fish

PloS one, 2012-02, Vol.7 (2), p.e32254

2012

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The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils

Proceedings of the National Academy of Sciences - PNAS, 2020-10, Vol.117 (41), p.25272-25283

2020

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Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

Proceedings of the National Academy of Sciences - PNAS, 2014-07, Vol.111 (26), p.9384-9389

2014

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A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

Nature structural & molecular biology, 2015-03, Vol.22 (3), p.207-213

2015

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High Resolution Structural Characterization of Aβ42 Amyloid Fibrils by Magic Angle Spinning NMR

Journal of the American Chemical Society, 2015-06, Vol.137 (23), p.7509-7518

2015

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Quantification of the Concentration of Aβ42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay

Journal of the American Chemical Society, 2014-01, Vol.136 (1), p.219-225

2014

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Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid

Communications biology, 2019-10, Vol.2 (1), p.365-365, Article 365

2019

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Correlation between sperm motility and sperm chromatin structure assay parameters

Fertility and sterility, 2003-12, Vol.80 (6), p.1404-1412

2003

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In vivo protein stabilization based on fragment complementation and a split GFP system

Proceedings of the National Academy of Sciences - PNAS, 2010-11, Vol.107 (46), p.19826-19831

2010

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The Major Bactericidal Activity of Human Seminal Plasma Is Zinc-Dependent and Derived from Fragmentation of the Semenogelins

The Journal of immunology (1950), 2008-09, Vol.181 (5), p.3413-3421

2008

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On the role of sidechain size and charge in the aggregation of A β 42 with familial mutations

Proceedings of the National Academy of Sciences - PNAS, 2018-06, Vol.115 (26), p.E5849

2018

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On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations

Proceedings of the National Academy of Sciences - PNAS, 2018-06, Vol.115 (26), p.E5849-E5858

2018

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Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide

Scientific reports, 2016-01, Vol.6 (1), p.18728, Article 18728

2016

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The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation

Chemical science (Cambridge), 2015-07, Vol.6 (7), p.4215-4233

2015

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Using NProAutoprotease Fusion Technology to Express a Semenogelin I Peptide

Biophysical journal, 2019-02, Vol.116 (3), p.63

2019

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Serine phosphorylation mimics of Aβ form distinct, non-cross-seeding fibril morphs

Chemical science (Cambridge), 2024

2024

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BRICHOS Domains Efficiently Delay Fibrillation of Amyloid β-Peptide

The Journal of biological chemistry, 2012-09, Vol.287 (37), p.31608-31617

2012

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pH‐Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide

Small (Weinheim an der Bergstrasse, Germany), 2021-07, Vol.17 (26), p.e2007188-n/a

2021

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Role of Aromatic Side Chains in Amyloid β‑Protein Aggregation

ACS chemical neuroscience, 2012-12, Vol.3 (12), p.1008-1016

2012

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On the role of sidechain size and charge in the aggregation of Aß42 with familial mutations

Proceedings of the National Academy of Sciences - PNAS, 2018-06, Vol.115 (26), p.E5849

2018

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N‑Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42

Journal of the American Chemical Society, 2015-11, Vol.137 (46), p.14673-14685

2015

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A peptide from human semenogelin I self-assembles into a pH-responsive hydrogel

Soft matter, 2015-01, Vol.11 (2), p.414-421

2015

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pentraxin serum amyloid P component is found in the male genital tract and attached to spermatozoa

International journal of andrology, 2008-10, Vol.31 (5), p.508-517

2008

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High Resolution Structural Characterization of A beta(42) Amyloid Fibrils by Magic Angle Spinning NMR

Journal of the American Chemical Society, 2015, Vol.137 (23), p.7509

2015

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A Study in Semenogelin I Hydrogel Aggregation Kinetics

Biophysical journal, 2015-01, Vol.108 (2), p.484a-484a

2015

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Food chain transport of nanoparticles affects behaviour and fat metabolism in fish

The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils

Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides

A molecular chaperone breaks the catalytic cycle that generates toxic Aβ oligomers

High Resolution Structural Characterization of Aβ42 Amyloid Fibrils by Magic Angle Spinning NMR

Quantification of the Concentration of Aβ42 Propagons during the Lag Phase by an Amyloid Chain Reaction Assay

Autocatalytic amplification of Alzheimer-associated Aβ42 peptide aggregation in human cerebrospinal fluid

Correlation between sperm motility and sperm chromatin structure assay parameters

In vivo protein stabilization based on fragment complementation and a split GFP system

The Major Bactericidal Activity of Human Seminal Plasma Is Zinc-Dependent and Derived from Fragmentation of the Semenogelins

On the role of sidechain size and charge in the aggregation of A β 42 with familial mutations

On the role of sidechain size and charge in the aggregation of Aβ42 with familial mutations

Quantitative analysis of intrinsic and extrinsic factors in the aggregation mechanism of Alzheimer-associated Aβ-peptide

The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation

Using NProAutoprotease Fusion Technology to Express a Semenogelin I Peptide

Serine phosphorylation mimics of Aβ form distinct, non-cross-seeding fibril morphs

BRICHOS Domains Efficiently Delay Fibrillation of Amyloid β-Peptide

pH‐Responsive Capsules with a Fibril Scaffold Shell Assembled from an Amyloidogenic Peptide

Role of Aromatic Side Chains in Amyloid β‑Protein Aggregation

On the role of sidechain size and charge in the aggregation of Aß42 with familial mutations

N‑Terminal Extensions Retard Aβ42 Fibril Formation but Allow Cross-Seeding and Coaggregation with Aβ42

A peptide from human semenogelin I self-assembles into a pH-responsive hydrogel

pentraxin serum amyloid P component is found in the male genital tract and attached to spermatozoa

High Resolution Structural Characterization of A beta(42) Amyloid Fibrils by Magic Angle Spinning NMR

A Study in Semenogelin I Hydrogel Aggregation Kinetics

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