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Distinct hyperactive RAS/MAPK alleles converge on common GABAergic interneuron core programs

Development (Cambridge), 2023-05, Vol.150 (10)

2023

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Distinct hyperactive RAS/MAPK alleles converge on common GABAergic interneuron core programs

Development (Cambridge), 2023-05, Vol.150 (10)

2023

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Hyperactive MEK1 Signaling in Cortical GABAergic Neurons Promotes Embryonic Parvalbumin Neuron Loss and Defects in Behavioral Inhibition

Cerebral cortex (New York, N.Y. 1991), 2021-05, Vol.31 (6), p.3064-3081

2021

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On the lag phase in amyloid fibril formation

Physical chemistry chemical physics : PCCP, 2015-01, Vol.17 (12), p.766-7618

2015

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Molecular mechanisms of protein aggregation from global fitting of kinetic models

Nature protocols, 2016-02, Vol.11 (2), p.252-272

2016

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Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide

Nature chemistry, 2020-05, Vol.12 (5), p.445

2020

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Secondary nucleation in amyloid formation

Chemical communications (Cambridge, England), 2018, Vol.54 (63), p.8667-8684

2018

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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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Physical determinants of the self-replication of protein fibrils

Nature physics, 2016-09, Vol.12 (9), p.874-880

2016

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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

2015

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Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation

Proceedings of the National Academy of Sciences - PNAS, 2014-05, Vol.111 (21), p.7671-7676

2014

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Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

Nature communications, 2016-03, Vol.7 (1), p.10948-10948, Article 10948

2016

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Identification of on- and off-pathway oligomers in amyloid fibril formation

Chemical science (Cambridge), 2020-06, Vol.11 (24), p.6236-6247

2020

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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

Proceedings of the National Academy of Sciences - PNAS, 2013-06, Vol.110 (24), p.9758-9763

2013

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Kinetic diversity of amyloid oligomers

Proceedings of the National Academy of Sciences - PNAS, 2020-06, Vol.117 (22), p.12087-12094

2020

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Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation

Journal of the American Chemical Society, 2021-10, Vol.143 (40), p.16621-16629

2021

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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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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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Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

Proceedings of the National Academy of Sciences - PNAS, 2017-01, Vol.114 (2), p.E200-E208

2017

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Protein Microgels from Amyloid Fibril Networks

ACS nano, 2015-01, Vol.9 (1), p.43-51

2015

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Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

Nature structural & molecular biology, 2020-12, Vol.27 (12), p.1125

2020

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Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions

ACS nano, 2016-01, Vol.10 (1), p.333-341

2016

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Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils

Proceedings of the National Academy of Sciences - PNAS, 2020-05, Vol.117 (21), p.11265-11273

2020

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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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SAR by kinetics for drug discovery in protein misfolding diseases

Proceedings of the National Academy of Sciences - PNAS, 2018-10, Vol.115 (41), p.10245-10250

2018

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Distinct hyperactive RAS/MAPK alleles converge on common GABAergic interneuron core programs

Distinct hyperactive RAS/MAPK alleles converge on common GABAergic interneuron core programs

Hyperactive MEK1 Signaling in Cortical GABAergic Neurons Promotes Embryonic Parvalbumin Neuron Loss and Defects in Behavioral Inhibition

On the lag phase in amyloid fibril formation

Molecular mechanisms of protein aggregation from global fitting of kinetic models

Dynamics of oligomer populations formed during the aggregation of Alzheimer's Aβ42 peptide

Secondary nucleation in amyloid formation

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

Physical determinants of the self-replication of protein fibrils

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

Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

Identification of on- and off-pathway oligomers in amyloid fibril formation

Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

Kinetic diversity of amyloid oligomers

Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aβ42 Aggregation

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

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

Systematic development of small molecules to inhibit specific microscopic steps of Aβ42 aggregation in Alzheimer’s disease

Protein Microgels from Amyloid Fibril Networks

Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies

Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions

Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils

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

SAR by kinetics for drug discovery in protein misfolding diseases

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