IMPRiND Project

Latest news

Publication in Nature by IMPRiND partner Michel Goedert.

New insights into the cryo-EM structures of alpha-synuclein filaments isolated from MSA and DLB brain by IMPRiND partner Michel Goedert. ...

Draft future IMI Call topics published online

The draft texts of the topics that are slated for inclusion in IMI’s next Calls for proposals are published: IMI2 – Call 22 is a ...

The socio-economic impact of IMI projects

12 years and 150 projects later, what kind of socio-economic impact has IMI-funded research had? Read more on the imi.europa website. ...

Blocking aggregate propagation in neurodegenerative diseases


Blocking aggregate propagation in neurodegenerative diseases IMPRiND – Inhibiting Misfolded protein Propagation In Neurodegenerative Diseases – is an international consortium that aims to map and target critical steps in the propagation of misfolded tau and α-synuclein, considered the main culprits of neurodegeneration in Alzheimer's and Parkinson's disease respectively. Our plans are built upon:
  • Identify disease-relevant misfolded assemblies, imprint their biological properties in vitro and/or in cellulo and generate homogeneous populations in order to assay and interfere with their pathogenic effects.
  • Develop and miniaturise assays to monitor up-take, secretion, clearance and oligomerisation using bimolecular fluorescence complementation of oligomeric species or transfer of untagged assemblies to fluorescently labelled fibril-naïve cells and measure markers of early proteotoxicity that are suitable for high throughput or high content screens.
  • Perform genetic screens based on disease-relevant gene/protein networks and assess druggability of identified targets.
  • Deliver robust validation assays for these molecular events in complex cellular systems with greater functional resemblance to the native milieu of the brain such as iPSC-based models and organotypic cultures or simple model organisms such as Drosophila or zebrafish.
  • Improve existing animal models in order to standardise pathological readouts for in vivo validation of modifiers, correlate them with novel peripheral or in situ markers using microdialysis to accelerate the assessment of therapeutic interventions and relevance to humans, e.g. by transplantation of human iPSC neurons in animals.
In the IMPRiND consortium, we will construct this entire pipeline to examine the propagation of α-synuclein and tau and test their tractability against disease progression.
IMPRIND started in March 2017 and will run until February 2021.

Most recent publications

1.
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
2.
Structures of α-synuclein filaments from multiple system atrophy.
Nature 1-6 (2020). doi:10.1038/s41586-020-2317-6
3.
Emergence of stealth polymorphs that escape α-synuclein amyloid monitoring, take over and acutely spread in neurons.
(Neuroscience, 2020). http://biorxiv.org/lookup/doi/10.1101/2020.02.11.943670.
4.
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
bioRxiv 2020.01.27.921643 (2020). doi:10.1101/2020.01.27.921643
5.
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs.
Biophysical Journal (2020). doi:10.1016/j.bpj.2020.01.022
6.
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
7.
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
8.
Novel tau filament fold in corticobasal degeneration, a four-repeat tauopathy.
bioRxiv 811703 (2019). doi:10.1101/811703
9.
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
10.
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-02014-y
11.
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.
Nature 568, 420-423 (2019). doi:10.1038/s41586-019-1026-5
12.
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-01995-0
13.
Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.
Stem Cell Reports (2019). doi:10.1016/j.stemcr.2018.12.007
14.
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
15.
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
16.
Pharmacological Transdifferentiation of Human Nasal Olfactory Stem Cells into Dopaminergic Neurons.
Stem Cells International (2019). https://www.hindawi.com/journals/sci/2019/2945435/.
17.
The Role of Antibodies and Their Receptors in Protection Against Ordered Protein Assembly in Neurodegeneration.
Frontiers in Immunology 10, (2019). doi:10.3389/fimmu.2019.01139
18.
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.
Frontiers in Molecular Neuroscience 12, (2019). doi:10.3389/fnmol.2019.00107
19.
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
ACS Chemical Neuroscience 9, 1276-1282 (2018). doi:10.1021/acschemneuro.8b00094
20.
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
21.
123I-FP-CIT SPECT [(123) I-2β-carbomethoxy-3β-(4-iodophenyl)-N-(3-fluoropropyl) nortropane single photon emission computed tomography] Imaging in a p.A53T α-synuclein Parkinson’s disease cohort versus Parkinson’s disease: 123I-FP-CIT IMAGING IN A P.A53T PD COHORT.
Movement Disorders 33, 1734-1739 (2018). doi:10.1002/mds.27451
22.
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
23.
Cryo-EM structures of tau filaments from Alzheimer’s disease.
Nature 547, 185-190 (2017). doi:10.1038/nature23002
24.
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding | Scientific Reports.
https://www.nature.com/articles/s41598-020-61757-x.
25.
How is alpha-synuclein cleared from the cell?.
Journal of Neurochemistry doi:10.1111/jnc.14704

1.
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
2.
Structures of α-synuclein filaments from multiple system atrophy.
Nature 1-6 (2020). doi:10.1038/s41586-020-2317-6
3.
Emergence of stealth polymorphs that escape α-synuclein amyloid monitoring, take over and acutely spread in neurons.
(Neuroscience, 2020). http://biorxiv.org/lookup/doi/10.1101/2020.02.11.943670.
4.
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
bioRxiv 2020.01.27.921643 (2020). doi:10.1101/2020.01.27.921643
5.
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs.
Biophysical Journal (2020). doi:10.1016/j.bpj.2020.01.022
6.
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
7.
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
8.
Novel tau filament fold in corticobasal degeneration, a four-repeat tauopathy.
bioRxiv 811703 (2019). doi:10.1101/811703
9.
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
10.
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-02014-y
11.
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.
Nature 568, 420-423 (2019). doi:10.1038/s41586-019-1026-5
12.
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-01995-0
13.
Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.
Stem Cell Reports (2019). doi:10.1016/j.stemcr.2018.12.007
14.
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
15.
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
16.
Pharmacological Transdifferentiation of Human Nasal Olfactory Stem Cells into Dopaminergic Neurons.
Stem Cells International (2019). https://www.hindawi.com/journals/sci/2019/2945435/.
17.
The Role of Antibodies and Their Receptors in Protection Against Ordered Protein Assembly in Neurodegeneration.
Frontiers in Immunology 10, (2019). doi:10.3389/fimmu.2019.01139
18.
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.
Frontiers in Molecular Neuroscience 12, (2019). doi:10.3389/fnmol.2019.00107
19.
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
ACS Chemical Neuroscience 9, 1276-1282 (2018). doi:10.1021/acschemneuro.8b00094
20.
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
21.
123I-FP-CIT SPECT [(123) I-2β-carbomethoxy-3β-(4-iodophenyl)-N-(3-fluoropropyl) nortropane single photon emission computed tomography] Imaging in a p.A53T α-synuclein Parkinson’s disease cohort versus Parkinson’s disease: 123I-FP-CIT IMAGING IN A P.A53T PD COHORT.
Movement Disorders 33, 1734-1739 (2018). doi:10.1002/mds.27451
22.
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
23.
Cryo-EM structures of tau filaments from Alzheimer’s disease.
Nature 547, 185-190 (2017). doi:10.1038/nature23002
24.
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding | Scientific Reports.
https://www.nature.com/articles/s41598-020-61757-x.
25.
How is alpha-synuclein cleared from the cell?.
Journal of Neurochemistry doi:10.1111/jnc.14704

1.
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
2.
Structures of α-synuclein filaments from multiple system atrophy.
Nature 1-6 (2020). doi:10.1038/s41586-020-2317-6
3.
Emergence of stealth polymorphs that escape α-synuclein amyloid monitoring, take over and acutely spread in neurons.
(Neuroscience, 2020). http://biorxiv.org/lookup/doi/10.1101/2020.02.11.943670.
4.
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
bioRxiv 2020.01.27.921643 (2020). doi:10.1101/2020.01.27.921643
5.
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs.
Biophysical Journal (2020). doi:10.1016/j.bpj.2020.01.022
6.
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
7.
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
8.
Novel tau filament fold in corticobasal degeneration, a four-repeat tauopathy.
bioRxiv 811703 (2019). doi:10.1101/811703
9.
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
10.
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-02014-y
11.
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.
Nature 568, 420-423 (2019). doi:10.1038/s41586-019-1026-5
12.
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-01995-0
13.
Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.
Stem Cell Reports (2019). doi:10.1016/j.stemcr.2018.12.007
14.
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
15.
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
16.
Pharmacological Transdifferentiation of Human Nasal Olfactory Stem Cells into Dopaminergic Neurons.
Stem Cells International (2019). https://www.hindawi.com/journals/sci/2019/2945435/.
17.
The Role of Antibodies and Their Receptors in Protection Against Ordered Protein Assembly in Neurodegeneration.
Frontiers in Immunology 10, (2019). doi:10.3389/fimmu.2019.01139
18.
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.
Frontiers in Molecular Neuroscience 12, (2019). doi:10.3389/fnmol.2019.00107
19.
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
ACS Chemical Neuroscience 9, 1276-1282 (2018). doi:10.1021/acschemneuro.8b00094
20.
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
21.
123I-FP-CIT SPECT [(123) I-2β-carbomethoxy-3β-(4-iodophenyl)-N-(3-fluoropropyl) nortropane single photon emission computed tomography] Imaging in a p.A53T α-synuclein Parkinson’s disease cohort versus Parkinson’s disease: 123I-FP-CIT IMAGING IN A P.A53T PD COHORT.
Movement Disorders 33, 1734-1739 (2018). doi:10.1002/mds.27451
22.
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
23.
Cryo-EM structures of tau filaments from Alzheimer’s disease.
Nature 547, 185-190 (2017). doi:10.1038/nature23002
24.
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding | Scientific Reports.
https://www.nature.com/articles/s41598-020-61757-x.
25.
How is alpha-synuclein cleared from the cell?.
Journal of Neurochemistry doi:10.1111/jnc.14704

1.
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
2.
Structures of α-synuclein filaments from multiple system atrophy.
Nature 1-6 (2020). doi:10.1038/s41586-020-2317-6
3.
Emergence of stealth polymorphs that escape α-synuclein amyloid monitoring, take over and acutely spread in neurons.
(Neuroscience, 2020). http://biorxiv.org/lookup/doi/10.1101/2020.02.11.943670.
4.
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
bioRxiv 2020.01.27.921643 (2020). doi:10.1101/2020.01.27.921643
5.
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs.
Biophysical Journal (2020). doi:10.1016/j.bpj.2020.01.022
6.
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
7.
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
8.
Novel tau filament fold in corticobasal degeneration, a four-repeat tauopathy.
bioRxiv 811703 (2019). doi:10.1101/811703
9.
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
10.
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-02014-y
11.
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.
Nature 568, 420-423 (2019). doi:10.1038/s41586-019-1026-5
12.
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-01995-0
13.
Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.
Stem Cell Reports (2019). doi:10.1016/j.stemcr.2018.12.007
14.
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
15.
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
16.
Pharmacological Transdifferentiation of Human Nasal Olfactory Stem Cells into Dopaminergic Neurons.
Stem Cells International (2019). https://www.hindawi.com/journals/sci/2019/2945435/.
17.
The Role of Antibodies and Their Receptors in Protection Against Ordered Protein Assembly in Neurodegeneration.
Frontiers in Immunology 10, (2019). doi:10.3389/fimmu.2019.01139
18.
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.
Frontiers in Molecular Neuroscience 12, (2019). doi:10.3389/fnmol.2019.00107
19.
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
ACS Chemical Neuroscience 9, 1276-1282 (2018). doi:10.1021/acschemneuro.8b00094
20.
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
21.
123I-FP-CIT SPECT [(123) I-2β-carbomethoxy-3β-(4-iodophenyl)-N-(3-fluoropropyl) nortropane single photon emission computed tomography] Imaging in a p.A53T α-synuclein Parkinson’s disease cohort versus Parkinson’s disease: 123I-FP-CIT IMAGING IN A P.A53T PD COHORT.
Movement Disorders 33, 1734-1739 (2018). doi:10.1002/mds.27451
22.
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
23.
Cryo-EM structures of tau filaments from Alzheimer’s disease.
Nature 547, 185-190 (2017). doi:10.1038/nature23002
24.
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding | Scientific Reports.
https://www.nature.com/articles/s41598-020-61757-x.
25.
How is alpha-synuclein cleared from the cell?.
Journal of Neurochemistry doi:10.1111/jnc.14704

1.
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
2.
Structures of α-synuclein filaments from multiple system atrophy.
Nature 1-6 (2020). doi:10.1038/s41586-020-2317-6
3.
Emergence of stealth polymorphs that escape α-synuclein amyloid monitoring, take over and acutely spread in neurons.
(Neuroscience, 2020). http://biorxiv.org/lookup/doi/10.1101/2020.02.11.943670.
4.
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
bioRxiv 2020.01.27.921643 (2020). doi:10.1101/2020.01.27.921643
5.
Differential Membrane Binding and Seeding of Distinct α-Synuclein Fibrillar Polymorphs.
Biophysical Journal (2020). doi:10.1016/j.bpj.2020.01.022
6.
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
7.
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
8.
Novel tau filament fold in corticobasal degeneration, a four-repeat tauopathy.
bioRxiv 811703 (2019). doi:10.1101/811703
9.
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
10.
Endogenous oligodendroglial alpha-synuclein and TPPP/p25α orchestrate alpha-synuclein pathology in experimental multiple system atrophy models.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-02014-y
11.
Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules.
Nature 568, 420-423 (2019). doi:10.1038/s41586-019-1026-5
12.
LRRK2 modifies α-syn pathology and spread in mouse models and human neurons.
Acta Neuropathologica (2019). doi:10.1007/s00401-019-01995-0
13.
Propagation of α-Synuclein Strains within Human Reconstructed Neuronal Network.
Stem Cell Reports (2019). doi:10.1016/j.stemcr.2018.12.007
14.
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
15.
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
16.
Pharmacological Transdifferentiation of Human Nasal Olfactory Stem Cells into Dopaminergic Neurons.
Stem Cells International (2019). https://www.hindawi.com/journals/sci/2019/2945435/.
17.
The Role of Antibodies and Their Receptors in Protection Against Ordered Protein Assembly in Neurodegeneration.
Frontiers in Immunology 10, (2019). doi:10.3389/fimmu.2019.01139
18.
Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.
Frontiers in Molecular Neuroscience 12, (2019). doi:10.3389/fnmol.2019.00107
19.
Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.
ACS Chemical Neuroscience 9, 1276-1282 (2018). doi:10.1021/acschemneuro.8b00094
20.
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
21.
123I-FP-CIT SPECT [(123) I-2β-carbomethoxy-3β-(4-iodophenyl)-N-(3-fluoropropyl) nortropane single photon emission computed tomography] Imaging in a p.A53T α-synuclein Parkinson’s disease cohort versus Parkinson’s disease: 123I-FP-CIT IMAGING IN A P.A53T PD COHORT.
Movement Disorders 33, 1734-1739 (2018). doi:10.1002/mds.27451
22.
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
23.
Cryo-EM structures of tau filaments from Alzheimer’s disease.
Nature 547, 185-190 (2017). doi:10.1038/nature23002
24.
The expression level of alpha-synuclein in different neuronal populations is the primary determinant of its prion-like seeding | Scientific Reports.
https://www.nature.com/articles/s41598-020-61757-x.
25.
How is alpha-synuclein cleared from the cell?.
Journal of Neurochemistry doi:10.1111/jnc.14704

Latest news

Publication in Nature by IMPRiND partner Michel Goedert.

New insights into the cryo-EM structures of alpha-synuclein filaments isolated from MSA and DLB brain by IMPRiND partner Michel Goedert. ...

Draft future IMI Call topics published online

The draft texts of the topics that are slated for inclusion in IMI’s next Calls for proposals are published: IMI2 – Call 22 is a ...

The socio-economic impact of IMI projects

12 years and 150 projects later, what kind of socio-economic impact has IMI-funded research had? Read more on the imi.europa website. ...

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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