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Refinado por: assunto: Amyloid - Chemistry remover assunto: Proteins remover
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1
A brief overview of amyloids and Alzheimer's disease
A brief overview of amyloids and Alzheimer's disease
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A brief overview of amyloids and Alzheimer's disease

Ow, Sian‐Yang ; Dunstan, Dave E.

Protein science, 2014-10, Vol.23 (10), p.1315-1331 [Periódico revisado por pares]

United States: Wiley Subscription Services, Inc

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2
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly
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Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly

Xue, Wei-Feng ; Homans, Steve W ; Radford, Sheena E

Proceedings of the National Academy of Sciences - PNAS, 2008-07, Vol.105 (26), p.8926-8931 [Periódico revisado por pares]

United States: National Academy of Sciences

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3
Structure and Aggregation Mechanisms in Amyloids
Structure and Aggregation Mechanisms in Amyloids
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Structure and Aggregation Mechanisms in Amyloids

Almeida, Zaida L ; Brito, Rui M M

Molecules (Basel, Switzerland), 2020-03, Vol.25 (5), p.1195 [Periódico revisado por pares]

Switzerland: MDPI AG

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4
Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers
Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers
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Amyloid formation of fish β-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers

Werner, Tony E. R. ; Bernson, David ; Esbjörner, Elin K. ; Rocha, Sandra ; Wittung-Stafshede, Pernilla

Proceedings of the National Academy of Sciences - PNAS, 2020-11, Vol.117 (45), p.27997-28004 [Periódico revisado por pares]

United States: National Academy of Sciences

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5
Physical and structural basis for polymorphism in amyloid fibrils
Physical and structural basis for polymorphism in amyloid fibrils
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Physical and structural basis for polymorphism in amyloid fibrils

Tycko, Robert

Protein science, 2014-11, Vol.23 (11), p.1528-1539 [Periódico revisado por pares]

United States: Wiley Subscription Services, Inc

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6
Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid
Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid
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Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid

Ali, Abid ; Zhaliazka, Kiryl ; Holman, Aidan P ; Kurouski, Dmitry

Proteins, structure, function, and bioinformatics, 2024-03, Vol.92 (3), p.411-417 [Periódico revisado por pares]

United States: Wiley Subscription Services, Inc

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7
Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed by Atomic Force Microscopy–Infrared Spectroscopy (AFM‐IR)
Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed by Atomic Force Microscopy–Infrared Spectroscopy (AFM‐IR)
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Nanoscale Structural Organization of Insulin Fibril Polymorphs Revealed by Atomic Force Microscopy–Infrared Spectroscopy (AFM‐IR)

Rizevsky, Stanislav ; Kurouski, Dmitry

Chembiochem : a European journal of chemical biology, 2020-02, Vol.21 (4), p.481-485 [Periódico revisado por pares]

Germany: Wiley Subscription Services, Inc

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8
Kinetic evidence for multiple aggregation pathways in antibody light chain variable domains
Kinetic evidence for multiple aggregation pathways in antibody light chain variable domains
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Kinetic evidence for multiple aggregation pathways in antibody light chain variable domains

Wong, Sherry ; West, Madeline E. ; Morgan, Gareth J.

Protein science, 2024-03, Vol.33 (3), p.e4871-n/a [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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9
Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils
Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils
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Length and saturation of fatty acids in phosphatidylserine determine the rate of lysozyme aggregation simultaneously altering the structure and toxicity of amyloid oligomers and fibrils

Frese, Addison ; Goode, Cody ; Zhaliazka, Kiryl ; Holman, Aidan P. ; Dou, Tianyi ; Kurouski, Dmitry

Protein science, 2023-08, Vol.32 (8), p.e4717-n/a [Periódico revisado por pares]

Hoboken, USA: John Wiley & Sons, Inc

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10
Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials
Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials
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Amyloid Fibrils as Building Blocks for Natural and Artificial Functional Materials

Knowles, Tuomas P. J. ; Mezzenga, Raffaele

Advanced materials (Weinheim), 2016-08, Vol.28 (31), p.6546-6561 [Periódico revisado por pares]

Germany: Blackwell Publishing Ltd

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