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Comparison of the Binding of Reversible Inhibitors to Human Butyrylcholinesterase and Acetylcholinesterase: A Crystallographic, Kinetic and Calorimetric Study

Molecules (Basel, Switzerland), 2017-11, Vol.22 (12), p.2098

2017

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Solvent Deuterium Oxide Isotope Effects on the Reactions of Organophosphorylated Acetylcholinesterase

Molecules (Basel, Switzerland), 2020-09, Vol.25 (19), p.4412

Rosenberry, Terrone L

2020

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Structures of Human Acetylcholinesterase Bound to Dihydrotanshinone I and Territrem B Show Peripheral Site Flexibility

ACS medicinal chemistry letters, 2013-11, Vol.4 (11), p.1091-1096

2013

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A Second Look at the Crystal Structures of Drosophila melanogaster Acetylcholinesterase in Complex with Tacrine Derivatives Provides Insights Concerning Catalytic Intermediates and the Design of Specific Insecticides

Molecules (Basel, Switzerland), 2020-03, Vol.25 (5), p.1198

2020

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Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer's Disease

Molecules (Basel, Switzerland), 2022-12, Vol.27 (24), p.8804

2022

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Opposing roles of the triggering receptor expressed on myeloid cells 2 and triggering receptor expressed on myeloid cells-like transcript 2 in microglia activation

Neurobiology of aging, 2016-06, Vol.42, p.132-141

2016

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Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

The Journal of neuroscience, 2007-04, Vol.27 (14), p.3650-3662

2007

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Cathepsin D regulates cerebral Aβ42/40 ratios via differential degradation of Aβ42 and Aβ40

Alzheimer's research & therapy, 2020-07, Vol.12 (1), p.1-80, Article 80

2020

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Distinct spatiotemporal accumulation of N-truncated and full-length amyloid-β42 in Alzheimer's disease

Brain (London, England : 1878), 2017-12, Vol.140 (12), p.3301-3316

2017

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Acetylcholinesterase: From 3D structure to function

Chemico-biological interactions, 2010-09, Vol.187 (1), p.10-22

2010

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A common pathway for detergent-assisted oligomerization of Aβ42

Communications biology, 2023-11, Vol.6 (1), p.1184-1184, Article 1184

2023

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The Alzheimer's Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils That Are Distinguished Structurally by Intermolecular Organization

Journal of molecular biology, 2013-07, Vol.425 (14), p.2494-2508

2013

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Rate-limiting step in the decarbamoylation of acetylcholinesterases with large carbamoyl groups

Chemico-biological interactions, 2019-08, Vol.308, p.392-395

2019

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Probing the Peripheral Site of Human Butyrylcholinesterase

Biochemistry (Easton), 2012-09, Vol.51 (36), p.7046-7053

2012

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VEGF receptor‐1 modulates amyloid β 1–42 oligomer‐induced senescence in brain endothelial cells

The FASEB journal, 2019-03, Vol.33 (3), p.4626-4637

2019

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Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa Oligomers

Journal of molecular biology, 2015-07, Vol.427 (13), p.2319-2328

2015

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Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1–42)

Journal of molecular biology, 2020-07, Vol.432 (16), p.4388-4407

2020

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Acetylthiocholine Binds to Asp74 at the Peripheral Site of Human Acetylcholinesterase as the First Step in the Catalytic Pathway

Biochemistry (Easton), 2000-07, Vol.39 (26), p.7753-7763

2000

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Decarbamoylation of acetylcholinesterases is markedly slowed as carbamoyl groups increase in size

Archives of biochemistry and biophysics, 2018-10, Vol.655, p.67-74

2018

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Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Ligand Binding to the Acylation Site

Journal of the American Chemical Society, 2008-06, Vol.130 (25), p.7856-7861

2008

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Blood-Based Oligomeric and Other Protein Variant Biomarkers to Facilitate Pre-Symptomatic Diagnosis and Staging of Alzheimer's Disease

Journal of Alzheimer's disease, 2017-01, Vol.58 (1), p.23-35

2017

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Mechanisms of altered vagal control in heart failure: influence of muscarinic receptors and acetylcholinesterase activity

American journal of physiology. Heart and circulatory physiology, 2003-10, Vol.285 (4), p.H1632-H1640

2003

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Substrate Binding to the Peripheral Site of Acetylcholinesterase Initiates Enzymatic Catalysis. Substrate Inhibition Arises as a Secondary Effect

Biochemistry (Easton), 1999-01, Vol.38 (1), p.122-133

1999

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Substrate-targeting γ-secretase modulators

Nature (London), 2008-06, Vol.453 (7197), p.925-929

2008

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Amyloid-β(1−42) Rapidly Forms Protofibrils and Oligomers by Distinct Pathways in Low Concentrations of Sodium Dodecylsulfate

Biochemistry (Easton), 2007-10, Vol.46 (43), p.12451-12462

2007

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Comparison of the Binding of Reversible Inhibitors to Human Butyrylcholinesterase and Acetylcholinesterase: A Crystallographic, Kinetic and Calorimetric Study

Solvent Deuterium Oxide Isotope Effects on the Reactions of Organophosphorylated Acetylcholinesterase

Structures of Human Acetylcholinesterase Bound to Dihydrotanshinone I and Territrem B Show Peripheral Site Flexibility

A Second Look at the Crystal Structures of Drosophila melanogaster Acetylcholinesterase in Complex with Tacrine Derivatives Provides Insights Concerning Catalytic Intermediates and the Design of Specific Insecticides

Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer's Disease

Opposing roles of the triggering receptor expressed on myeloid cells 2 and triggering receptor expressed on myeloid cells-like transcript 2 in microglia activation

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

Cathepsin D regulates cerebral Aβ42/40 ratios via differential degradation of Aβ42 and Aβ40

Distinct spatiotemporal accumulation of N-truncated and full-length amyloid-β42 in Alzheimer's disease

Acetylcholinesterase: From 3D structure to function

A common pathway for detergent-assisted oligomerization of Aβ42

The Alzheimer's Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils That Are Distinguished Structurally by Intermolecular Organization

Rate-limiting step in the decarbamoylation of acetylcholinesterases with large carbamoyl groups

Probing the Peripheral Site of Human Butyrylcholinesterase

VEGF receptor‐1 modulates amyloid β 1–42 oligomer‐induced senescence in brain endothelial cells

Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa Oligomers

Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1–42)

Acetylthiocholine Binds to Asp74 at the Peripheral Site of Human Acetylcholinesterase as the First Step in the Catalytic Pathway

Decarbamoylation of acetylcholinesterases is markedly slowed as carbamoyl groups increase in size

Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Ligand Binding to the Acylation Site

Blood-Based Oligomeric and Other Protein Variant Biomarkers to Facilitate Pre-Symptomatic Diagnosis and Staging of Alzheimer's Disease

Mechanisms of altered vagal control in heart failure: influence of muscarinic receptors and acetylcholinesterase activity

Substrate Binding to the Peripheral Site of Acetylcholinesterase Initiates Enzymatic Catalysis. Substrate Inhibition Arises as a Secondary Effect

Substrate-targeting γ-secretase modulators

Amyloid-β(1−42) Rapidly Forms Protofibrils and Oligomers by Distinct Pathways in Low Concentrations of Sodium Dodecylsulfate

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