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Structural insights into a yeast prion illuminate nucleation and strain diversity

Nature, 2005-06, Vol.435 (7043), p.765-772

2005

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natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures

Proceedings of the National Academy of Sciences - PNAS, 2007-02, Vol.104 (8), p.2649-2654

2007

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Conserved features of intermediates in amyloid assembly determine their benign or toxic states

Proceedings of the National Academy of Sciences - PNAS, 2012-07, Vol.109 (28), p.11172-11177

2012

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Conformation as the Therapeutic Target for Neurodegenerative Diseases

Current Alzheimer research, 2017-01, Vol.14 (4), p.393

2017

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Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI⁺] prion in yeast and aggregation of Sup35 in vitro

Proceedings of the National Academy of Sciences - PNAS, 2004-08, Vol.101 (35), p.12934-12939

2004

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477 Deep learning to drive COVID-19 rapid drug repurposing

Journal for immunotherapy of cancer, 2020-11, Vol.8 (Suppl 3), p.A509-A509

2020

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Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs

Proceedings of the National Academy of Sciences - PNAS, 2008-05, Vol.105 (20), p.7159-7164

2008

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Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif

Journal of molecular biology, 2019-05, Vol.431 (10), p.1920-1939

2019

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The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication

The EMBO journal, 2011-05, Vol.30 (10), p.2057-2070

2011

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Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins

Molecular cell, 2011-07, Vol.43 (1), p.72-84

2011

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A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies

Journal of molecular biology, 2014-06, Vol.426 (13), p.2500-2519

2014

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GAIM fusions are therapeutic candidates for peripheral amyloidosis

Amyloid, 2019-03, Vol.26 (sup1), p.85-86

2019

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MUTAGENESIS OF THE GENERAL AMYLOID INTERACTION MOTIF (GAIM) REVEALS A STRUCTURE-ACTIVITY RELATIONSHIP FOR MISFOLDED BETA-AMYLOID AND TAU AGGREGATES

Alzheimer's & dementia, 2017-07, Vol.13 (7), p.P1006-P1007

2017

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NPT088 reduces both amyloid-β and tau pathologies in transgenic mice

Alzheimer's & dementia : translational research & clinical interventions, 2016-09, Vol.2 (3), p.141-155

2016

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P4‐213: REDUCTION OF β‐AMYLOID AND PHOSPHO‐TAU IN TRANSGENIC MICE BY A NOVEL FUSION PROTEIN BIVALENT FOR A GENERAL AMYLOID INTERACTION MOTIF (GAIM)

Alzheimer's & dementia, 2014-07, Vol.10 (4S_Part_23), p.P866-P866

2014

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REDUCTION OF β-AMYLOID AND PHOSPHO-TAU IN TRANSGENIC MICE BY A NOVEL FUSION PROTEIN BIVALENT FOR A GENERAL AMYLOID INTERACTION MOTIF (GAIM)

Alzheimer's & dementia, 2014-07, Vol.10 (4), p.P866-P866

2014

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P2–050: A novel mechanism that targets misfolded protein assemblies

Alzheimer's & dementia, 2013-07, Vol.9 (4S_Part_9), p.P361-P362

2013

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P4–290: Novel fusion protein bivalent for a general amyloid interaction motif reduces beta‐amyloid aggregates in transgenic mice

Alzheimer's & dementia, 2013-07, Vol.9 (4S_Part_20), p.P810-P810

2013

Volltextzugriff (PDF)

Novel fusion protein bivalent for a general amyloid interaction motif reduces beta-amyloid aggregates in transgenic mice

Alzheimer's & dementia, 2013-07, Vol.9 (4), p.P810-P810

2013

Volltextzugriff (PDF)

O1‐05‐01: Discovery, preclinical development, and clinical trial approach for npt088, a general amyloid interaction motif (GAIM)‐immunoglobulin fusion

Alzheimer's & dementia, 2015-07, Vol.11 (7S_Part_3), p.P135-P135

2015

Volltextzugriff (PDF)

Discovery, preclinical development, and clinical trial approach for npt088, a general amyloid interaction motif (GAIM)-immunoglobulin fusion

Alzheimer's & dementia, 2015-07, Vol.11 (7), p.P135-P135

2015

Volltextzugriff (PDF)

IMMUNOGLOBULIN-GENERAL AMYLOID INTERACTION MOTIF (IG-GAIM) MOLECULES TARGET BETA AMYLOID AND NEUROFIBRILLARY TANGLES IN VITRO AND IN VIVO

Alzheimer's & dementia, 2014-07, Vol.10 (4), p.P494-P494

2014

Volltextzugriff (PDF)

P2‐067: IMMUNOGLOBULIN‐GENERAL AMYLOID INTERACTION MOTIF (IG‐GAIM) MOLECULES TARGET BETA AMYLOID AND NEUROFIBRILLARY TANGLES IN VITRO AND IN VIVO

Alzheimer's & dementia, 2014-07, Vol.10 (4S_Part_12), p.P494-P494

2014

Volltextzugriff (PDF)

P4‐412: NPT001: A candidate therapeutic for clearance of beta‐amyloid and tau aggregates in Alzheimer's disease

Alzheimer's & dementia, 2011-07, Vol.7 (4S_Part_25), p.e56-e56

2011

Volltextzugriff (PDF)

NPT001: A candidate therapeutic for clearance of beta-amyloid and tau aggregates in Alzheimer's disease

Alzheimer's & dementia, 2011-07, Vol.7 (4), p.e56-e56

2011

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Structural insights into a yeast prion illuminate nucleation and strain diversity

natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures

Conserved features of intermediates in amyloid assembly determine their benign or toxic states

Conformation as the Therapeutic Target for Neurodegenerative Diseases

Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI⁺] prion in yeast and aggregation of Sup35 in vitro

477 Deep learning to drive COVID-19 rapid drug repurposing

Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs

Stability and Inter-domain Interactions Modulate Amyloid Binding Activity of a General Amyloid Interaction Motif

The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication

Opposing Effects of Glutamine and Asparagine Govern Prion Formation by Intrinsically Disordered Proteins

A Bacteriophage Capsid Protein Provides a General Amyloid Interaction Motif (GAIM) That Binds and Remodels Misfolded Protein Assemblies

GAIM fusions are therapeutic candidates for peripheral amyloidosis

MUTAGENESIS OF THE GENERAL AMYLOID INTERACTION MOTIF (GAIM) REVEALS A STRUCTURE-ACTIVITY RELATIONSHIP FOR MISFOLDED BETA-AMYLOID AND TAU AGGREGATES

NPT088 reduces both amyloid-β and tau pathologies in transgenic mice

P4‐213: REDUCTION OF β‐AMYLOID AND PHOSPHO‐TAU IN TRANSGENIC MICE BY A NOVEL FUSION PROTEIN BIVALENT FOR A GENERAL AMYLOID INTERACTION MOTIF (GAIM)

REDUCTION OF β-AMYLOID AND PHOSPHO-TAU IN TRANSGENIC MICE BY A NOVEL FUSION PROTEIN BIVALENT FOR A GENERAL AMYLOID INTERACTION MOTIF (GAIM)

P2–050: A novel mechanism that targets misfolded protein assemblies

P4–290: Novel fusion protein bivalent for a general amyloid interaction motif reduces beta‐amyloid aggregates in transgenic mice

Novel fusion protein bivalent for a general amyloid interaction motif reduces beta-amyloid aggregates in transgenic mice

O1‐05‐01: Discovery, preclinical development, and clinical trial approach for npt088, a general amyloid interaction motif (GAIM)‐immunoglobulin fusion

Discovery, preclinical development, and clinical trial approach for npt088, a general amyloid interaction motif (GAIM)-immunoglobulin fusion

IMMUNOGLOBULIN-GENERAL AMYLOID INTERACTION MOTIF (IG-GAIM) MOLECULES TARGET BETA AMYLOID AND NEUROFIBRILLARY TANGLES IN VITRO AND IN VIVO

P2‐067: IMMUNOGLOBULIN‐GENERAL AMYLOID INTERACTION MOTIF (IG‐GAIM) MOLECULES TARGET BETA AMYLOID AND NEUROFIBRILLARY TANGLES IN VITRO AND IN VIVO

P4‐412: NPT001: A candidate therapeutic for clearance of beta‐amyloid and tau aggregates in Alzheimer's disease

NPT001: A candidate therapeutic for clearance of beta-amyloid and tau aggregates in Alzheimer's disease

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