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Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study

Journal of the American Chemical Society, 2010-03, Vol.132 (12), p.4266-4280

2010

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Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer’s disease

Neurobiology of aging, 2004-05, Vol.25 (5), p.569-580

2004

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Dynamics of Metastable β-Hairpin Structures in the Folding Nucleus of Amyloid β-Protein

The journal of physical chemistry. B, 2012-06, Vol.116 (22), p.6311-6325

2012

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Effects of the Arctic (E22-->G) mutation on amyloid beta-protein folding: discrete molecular dynamics study

Journal of the American Chemical Society, 2008-12, Vol.130 (51), p.17413-17422

2008

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Cryptocandin, a potent antimycotic from the endophytic fungus Cryptosporiopsis cf. quercina

Microbiology (Society for General Microbiology), 1999-08, Vol.145 ( Pt 8) (8), p.1919-1926

1999

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Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis

Journal of molecular biology, 2001-10, Vol.312 (5), p.1103-1119

2001

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Amyloid β-peptide is produced by cultured cells during normal metabolism

Nature (London), 1992-09, Vol.359 (6393), p.322-325

1992

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Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing

Biochemistry (Easton), 1993-03, Vol.32 (8), p.1991-2002

1993

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An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments

Amyloid, 2000, Vol.7 (3), p.166-178

2000

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The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

Nature neuroscience, 2001-09, Vol.4 (9), p.887-893

2001

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Munumbicins, wide-spectrum antibiotics produced by Streptomyces NRRL 30562, endophytic on Kennedia nigriscans

Microbiology (Society for General Microbiology), 2002-09, Vol.148 (Pt 9), p.2675

2002

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Coronamycins, peptide antibiotics produced by a verticillate Streptomyces sp. (MSU-2110) endophytic on Monstera sp

Microbiology (Society for General Microbiology), 2004-04, Vol.150 (Pt 4), p.785-793

2004

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Structural and kinetic features of amyloid β-protein fibrillogenesis

Amyloid, 1998-06, Vol.5 (2), p.121-142

Teplow, David B.

1998

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Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences

Journal of molecular biology, 2008-12, Vol.384 (2), p.450-464

2008

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Effects of the Arctic (E22→G) Mutation on Amyloid β-Protein Folding: Discrete Molecular Dynamics Study

Journal of the American Chemical Society, 2011-03, Vol.133 (8), p.2789-2789

2011

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Conformational Dynamics of Amyloid β-Protein Assembly Probed Using Intrinsic Fluorescence

Biochemistry (Easton), 2005-10, Vol.44 (40), p.13365-13376

2005

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A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils

Nature structural & molecular biology, 2000-12, Vol.7 (12), p.1095-1099

2000

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Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies

Journal of neuroscience research, 2002-09, Vol.69 (5), p.567-577

2002

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Oligomerization of Endogenous and Synthetic Amyloid β-Protein at Nanomolar Levels in Cell Culture and Stabilization of Monomer by Congo Red

Biochemistry (Easton), 1998-03, Vol.37 (11), p.3602-3611

1998

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Cogitations on a proteocentric lexicon

Neurobiology of aging, 2000-07, Vol.21 (4), p.563-564

Teplow, David B

2000

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Identification of cellular proteins binding to the scrapie prion protein

Biochemistry (Easton), 1990-06, Vol.29 (24), p.5848-5855

1990

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Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer

Nature (London), 1989-04, Vol.338 (6217), p.656-658

1989

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Identity of PSA purified from seminal fluid by different methods: Comparison by amino acid analysis and assigned extinction coefficients

The Prostate, 1995-10, Vol.27 (4), p.198-203

1995

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[27] Monitoring protein assembly using quasielastic light scattering spectroscopy

Methods in Enzymology, 1999, Vol.309, p.429-459

1999

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Effects of Familial Alzheimer’s Disease Mutations on the Folding Nucleation of the Amyloid β-Protein

Journal of molecular biology, 2008-08, Vol.381 (1), p.221-228

2008

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Elucidation of Amyloid β-Protein Oligomerization Mechanisms: Discrete Molecular Dynamics Study

Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer’s disease

Dynamics of Metastable β-Hairpin Structures in the Folding Nucleus of Amyloid β-Protein

Effects of the Arctic (E22-->G) mutation on amyloid beta-protein folding: discrete molecular dynamics study

Cryptocandin, a potent antimycotic from the endophytic fungus Cryptosporiopsis cf. quercina

Identification and characterization of key kinetic intermediates in amyloid β-protein fibrillogenesis

Amyloid β-peptide is produced by cultured cells during normal metabolism

Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing

An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

Munumbicins, wide-spectrum antibiotics produced by Streptomyces NRRL 30562, endophytic on Kennedia nigriscans

Coronamycins, peptide antibiotics produced by a verticillate Streptomyces sp. (MSU-2110) endophytic on Monstera sp

Structural and kinetic features of amyloid β-protein fibrillogenesis

Amyloid β-Protein Monomer Folding: Free-Energy Surfaces Reveal Alloform-Specific Differences

Effects of the Arctic (E22→G) Mutation on Amyloid β-Protein Folding: Discrete Molecular Dynamics Study

Conformational Dynamics of Amyloid β-Protein Assembly Probed Using Intrinsic Fluorescence

A de novo designed helix-turn-helix peptide forms nontoxic amyloid fibrils

Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: The emerging role of oligomeric assemblies

Oligomerization of Endogenous and Synthetic Amyloid β-Protein at Nanomolar Levels in Cell Culture and Stabilization of Monomer by Congo Red

Cogitations on a proteocentric lexicon

Identification of cellular proteins binding to the scrapie prion protein

Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer

Identity of PSA purified from seminal fluid by different methods: Comparison by amino acid analysis and assigned extinction coefficients

[27] Monitoring protein assembly using quasielastic light scattering spectroscopy

Effects of Familial Alzheimer’s Disease Mutations on the Folding Nucleation of the Amyloid β-Protein

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