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Calcium Dyshomeostasis in Alzheimer’s Disease Pathogenesis

International journal of molecular sciences, 2021-05, Vol.22 (9), p.4914

2021

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Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases

BioEssays, 2022-11, Vol.44 (11), p.n/a

2022

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The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity

Biophysical chemistry, 2013-12, Vol.182, p.30-43

2013

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The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

Nature communications, 2021-03, Vol.12 (1), p.1814-16, Article 1814

2021

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The Toxicity of Protein Aggregates: New Insights into the Mechanisms

International journal of molecular sciences, 2023-04, Vol.24 (9), p.7974

2023

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Editorial: Promising therapeutic strategies for Alzheimer's disease: a focus on amyloid-β targeting

Frontiers in neuroscience, 2024-04, Vol.18, p.1415641-1415641

2024

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Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases

Scientific reports, 2016-09, Vol.6 (1), p.32721-32721, Article 32721

2016

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Toxicity of Protein Oligomers Is Rationalized by a Function Combining Size and Surface Hydrophobicity

ACS chemical biology, 2014-10, Vol.9 (10), p.2309-2317

2014

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Targeting Pathological Amyloid Aggregates with Conformation-Sensitive Antibodies

Current Alzheimer research, 2020-01, Vol.17 (8), p.722-734

2020

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Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases

International journal of molecular sciences, 2019-07, Vol.20 (15), p.3685

2019

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Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies

The Journal of biological chemistry, 2016-09, Vol.291 (37), p.19437-19448

2016

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SIRT1 modulates MAPK pathways in ischemic–reperfused cardiomyocytes

Cellular and molecular life sciences : CMLS, 2012-07, Vol.69 (13), p.2245-2260

2012

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α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies

Neural regeneration research, 2023-11, Vol.18 (11), p.2332-2342

2023

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An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature

Annals of medicine (Helsinki), 2023-12, Vol.55 (1), p.72-88

2023

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Quantitative assessment of the degradation of aggregated TDP‐43 mediated by the ubiquitin proteasome system and macroautophagy

The FASEB journal, 2017-12, Vol.31 (12), p.5609-5624

2017

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Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers

Proceedings of the National Academy of Sciences - PNAS, 2012-07, Vol.109 (31), p.12479-12484

2012

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Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation

International journal of molecular sciences, 2019-11, Vol.20 (22), p.5558

2019

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Soluble Prion Peptide 107-120 Protects Neuroblastoma SH-SY5Y Cells against Oligomers Associated with Alzheimer's Disease

International journal of molecular sciences, 2020-10, Vol.21 (19), p.7273

2020

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Exploring the Release of Toxic Oligomers from α-Synuclein Fibrils with Antibodies and STED Microscopy

Life (Basel, Switzerland), 2021-05, Vol.11 (5), p.431

2021

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Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers

Journal of cell science, 2012-05, Vol.125 (Pt 10), p.2416-2427

2012

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A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF

Alzheimer's research & therapy, 2024-01, Vol.16 (1), p.1-13, Article 13

2024

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Single molecule experiments emphasize GM1 as a key player of the different cytotoxicity of structurally distinct Aβ1–42 oligomers

Biochimica et biophysica acta, 2016-02, Vol.1858 (2), p.386-392

2016

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TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells

PloS one, 2014-01, Vol.9 (1), p.e86720

2014

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Putative novel CSF biomarkers of Alzheimer's disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort

Translational neurodegeneration, 2024-03, Vol.13 (1), p.14-14, Article 14

2024

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A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells

Biochimica et biophysica acta, 2009-10, Vol.1788 (10), p.2204-2216

2009

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Calcium Dyshomeostasis in Alzheimer’s Disease Pathogenesis

Amyloid fibrils act as a reservoir of soluble oligomers, the main culprits in protein deposition diseases

The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity

The release of toxic oligomers from α-synuclein fibrils induces dysfunction in neuronal cells

The Toxicity of Protein Aggregates: New Insights into the Mechanisms

Editorial: Promising therapeutic strategies for Alzheimer's disease: a focus on amyloid-β targeting

Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases

Toxicity of Protein Oligomers Is Rationalized by a Function Combining Size and Surface Hydrophobicity

Targeting Pathological Amyloid Aggregates with Conformation-Sensitive Antibodies

Partial Failure of Proteostasis Systems Counteracting TDP-43 Aggregates in Neurodegenerative Diseases

Quantification of the Relative Contributions of Loss-of-function and Gain-of-function Mechanisms in TAR DNA-binding Protein 43 (TDP-43) Proteinopathies

SIRT1 modulates MAPK pathways in ischemic–reperfused cardiomyocytes

α-Synuclein oligomers and fibrils: partners in crime in synucleinopathies

An in situ and in vitro investigation of cytoplasmic TDP-43 inclusions reveals the absence of a clear amyloid signature

Quantitative assessment of the degradation of aggregated TDP‐43 mediated by the ubiquitin proteasome system and macroautophagy

Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers

Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation

Soluble Prion Peptide 107-120 Protects Neuroblastoma SH-SY5Y Cells against Oligomers Associated with Alzheimer's Disease

Exploring the Release of Toxic Oligomers from α-Synuclein Fibrils with Antibodies and STED Microscopy

Membrane lipid composition and its physicochemical properties define cell vulnerability to aberrant protein oligomers

A single-domain antibody detects and neutralises toxic Aβ42 oligomers in the Alzheimer’s disease CSF

Single molecule experiments emphasize GM1 as a key player of the different cytotoxicity of structurally distinct Aβ1–42 oligomers

TDP-43 inclusion bodies formed in bacteria are structurally amorphous, non-amyloid and inherently toxic to neuroblastoma cells

Putative novel CSF biomarkers of Alzheimer's disease based on the novel concept of generic protein misfolding and proteotoxicity: the PRAMA cohort

A protective role for lipid raft cholesterol against amyloid-induced membrane damage in human neuroblastoma cells

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