IMPRiND Project

Publishable summaries

IMPRiND produces annual publishable reports which describe the project achievements. They are public and and the latest can be downloaded by clicking on the links below.

IMPRiND Public Events

Below you will find information regarding public events organised by IMPRiND.

Scientific publications

Publications in peer-reviewed journals, conference proceedings, book chapters and books.
1.
Seeding Propensity and Characteristics of Pathogenic αSyn Assemblies in Formalin-Fixed Human Tissue from the Enteric Nervous System, Olfactory Bulb, and Brainstem in Cases Staged for Parkinson’s Disease.
Cells 10, 139 (2021). doi:10.3390/cells10010139
2.
The differential solvent exposure of N-terminal residues provides ‘fingerprints’ of alpha-synuclein fibrillar polymorphs.
Journal of Biological Chemistry 100737 (2021). doi:10.1016/j.jbc.2021.100737
3.
Tau assemblies do not behave like independently acting prion-like particles in mouse neural tissue.
Acta Neuropathologica Communications 9, 41 (2021). doi:10.1186/s40478-021-01141-6
4.
TNF-α and α-synuclein fibrils differently regulate human astrocyte immune reactivity and impair mitochondrial respiration.
Cell Reports 34, 108895 (2021). doi:10.1016/j.celrep.2021.108895
5.
Overexpression of α-Synuclein by Oligodendrocytes in Transgenic Mice Does Not Recapitulate the Fibrillar Aggregation Seen in Multiple System Atrophy.
Cells 9, 2371 (2020). doi:10.3390/cells9112371
6.
Distinct alpha‐Synuclein species induced by seeding are selectively cleared by the Lysosome or the Proteasome in neuronally differentiated SH‐SY5Y cells.
Journal of Neurochemistry jnc.15174 (2020). doi:10.1111/jnc.15174. Archive: https://zenodo.org/record/4570369#.YD0kCV1KiWh
7.
Structures of α-synuclein filaments from multiple system atrophy.
Nature 585, 464–469 (2020). doi:10.1038/s41586-020-2317-6
8.
Prominent microglial inclusions in transgenic mouse models of α-synucleinopathy that are distinct from neuronal lesions.
Acta Neuropathologica Communications 8, 133 (2020). doi:10.1186/s40478-020-00993-8
9.
The structural differences between patient-derived α-synuclein strains dictate characteristics of Parkinson’s disease, multiple system atrophy and dementia with Lewy bodies.
Acta Neuropathologica 139, 977–1000 (2020). doi:10.1007/s00401-020-02157-3
10.
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs.
Biophysical Journal (2020). doi:10.1016/j.bpj.2020.01.022
11.
Interaction of the chaperones alpha B-crystallin and CHIP with fibrillar alpha-synuclein: Effects on internalization by cells and identification of interacting interfaces.
Biochemical and Biophysical Research Communications 527, 760–769 (2020). doi:10.1016/j.bbrc.2020.04.091
12.
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding.
Scientific Reports 10, 4895 (2020). doi:10.1038/s41598-020-61757-x
13.
Novel self-replicating α-synuclein polymorphs that escape ThT monitoring can spontaneously emerge and acutely spread in neurons.
Science Advances 6, eabc4364 (2020). doi:10.1126/sciadv.abc4364
14.
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
Scientific Reports 10, 12827 (2020). doi:10.1038/s41598-020-69744-y
15.
Les protéinopathies infectieuses de Parkinson et d’Alzheimer.
Bulletin de l’Académie Nationale de Médecine 204, 224–231 (2020). doi:10.1016/j.banm.2019.12.019. Archive: https://hal-cea.archives-ouvertes.fr/cea-02859853
16.
Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species.
Journal of Biological Chemistry 295, 9676–9690 (2020). doi:10.1074/jbc.RA120.013478
17.
Acute targeting of pre-amyloid seeds in transgenic mice reduces Alzheimer-like pathology later in life.
Nature Neuroscience 23, 1580–1588 (2020). doi:10.1038/s41593-020-00737-w. Archive: https://zenodo.org/record/4562254#.YDfVlF1KgdW
18.
α-Synuclein conformational strains spread, seed and target neuronal cells differentially after injection into the olfactory bulb.
Acta Neuropathologica Communications 7, 221 (2019). doi:10.1186/s40478-019-0859-3
19.
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy.
eLife 8, e48907 (2019). doi:10.7554/eLife.48907
20.
Detection of alpha-synuclein aggregates in gastrointestinal biopsies by protein misfolding cyclic amplification.
Neurobiology of Disease 129, 38–43 (2019). doi:10.1016/j.nbd.2019.05.002
21.
The Role of Antibodies and Their Receptors in Protection Against Ordered Protein Assembly in Neurodegeneration.
Frontiers in Immunology 10, 1139 (2019). doi:10.3389/fimmu.2019.01139
22.
Pharmacological Transdifferentiation of Human Nasal Olfactory Stem Cells into Dopaminergic Neurons.
Stem Cells International 2019, 1–15 (2019). doi:10.1155/2019/2945435
23.
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.
Frontiers in Molecular Neuroscience 12, 107 (2019). doi:10.3389/fnmol.2019.00107
24.
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.
Nature 568, 420–423 (2019). doi:10.1038/s41586-019-1026-5
25.
Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.
Stem Cell Reports (2019). doi:10.1016/j.stemcr.2018.12.007
26.
Clustering of Tau fibrils impairs the synaptic composition of α3‐Na+/K+‐ATPase and AMPA receptors.
The EMBO Journal e99871 (2019). doi:10.15252/embj.201899871
27.
α‐synuclein oligomers and fibrils: a spectrum of species, a spectrum of toxicities.
Journal of Neurochemistry 150, 522–534 (2019). doi:10.1111/jnc.14808
28.
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons.
Acta Neuropathologica 137, 961–980 (2019). doi:10.1007/s00401-019-01995-0
29.
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models.
Acta Neuropathologica 138, 415–441 (2019). doi:10.1007/s00401-019-02014-y
30.
How is alpha‐synuclein cleared from the cell?.
Journal of Neurochemistry 150, 577–590 (2019). doi:10.1111/jnc.14704
31.
Reduced serum immunoglobulin G concentrations in multiple sclerosis: prevalence and association with disease-modifying therapy and disease course.
Therapeutic Advances in Neurological Disorders 12, 175628641987834 (2019). doi:10.1177/1756286419878340
32.
Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer’s and Pick’s disease.
bioRxiv 468892 (2018). doi:10.1101/468892
33.
Assessment of the efficacy of different procedures that remove and disassemble alpha-synuclein, tau and A-beta fibrils from laboratory material and surfaces.
Scientific Reports 8, 10788 (2018). doi:10.1038/s41598-018-28856-2
34.
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
ACS Chemical Neuroscience 9, 1276–1282 (2018). doi:10.1021/acschemneuro.8b00094
35.
Tau Filaments and the Development of Positron Emission Tomography Tracers.
Frontiers in Neurology 9, (2018). doi:10.3389/fneur.2018.00070
36.
Structures of filaments from Pick’s disease reveal a novel tau protein fold.
Nature 561, 137–140 (2018). doi:10.1038/s41586-018-0454-y
37.
Tau filaments from multiple cases of sporadic and inherited Alzheimer’s disease adopt a common fold.
Acta Neuropathologica 136, 699–708 (2018). doi:10.1007/s00401-018-1914-z
38.
Neurodegeneration and the ordered assembly of α-synuclein.
Cell and Tissue Research 373, 137–148 (2018). doi:10.1007/s00441-017-2706-9
39.
A Critical Assessment of Exosomes in the Pathogenesis and Stratification of Parkinson’s Disease.
Journal of Parkinson’s Disease 7, 569–576 (2017). doi:10.3233/JPD-171176
40.
Cryo-EM structures of tau filaments from Alzheimer’s disease.
Nature 547, 185–190 (2017). doi:10.1038/nature23002

Project Flyer

The IMPRiND project flyer describes the project at a glance. It is mainly intended as a printed product but its electronic version is available for download.

This project receives funding from the Innovative Medicines Initiative 2 Joint Undertaking (www.imi.europa.eu) under grant agreement No 116060. This Joint Undertaking receives support from the European Union’s Horizon 2020 research and innovation programme and EFPIA.

This work is supported by the Swiss State Secretariat for Education‚ Research and Innovation (SERI) under contract number 17.00038.

The opinions expressed and arguments employed herein do not necessarily reflect the official views of these funding bodies.

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