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Amyloids

Amyloids is a collective term to describe misfolded proteins that self-assemble into insoluble fibrils both in vitro and in vivo. These protein aggregates are involved in a wide variety of human diseases, from Alzheimer's Disease to Type 2 Diabetes and Rheumatoid Arthritis to Artherosclerosis. Given the importance of amyloids in a disease context, intense study of their biophysical properties has given plenty of new information on ways to inhibit their formation.

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Identification of Transthyretin Fibril Formation Inhibitors Using Structure-Based Virtual Screening

Identification of Transthyretin Fibril Formation Inhibitors Using Structure‐Based Virtual Screening

Rapid and accurate! Inhibitors of transthyretin (TTR) fibril deposition were identified thanks to a structure-based virtual screening of the entire Aldrich Market Select database. The first results of this protocol, despite the unique peculiarity of the TTR site with its symmetry and multi-binding mode, allowed the detection of two very active inhibitors and one scaffold for optimization. Much information, however, is still stored in the outputs.

[Full Paper]
Gabriella Ortore, Adriano Martinelli
ChemMedChem, May 11, 2017, https://doi.org/10.1002/cmdc.201700051 Read article

Flexible N-Termini of Amyloid β-Protein Oligomers: A Link between Structure and Activity?

Flexible N‐Termini of Amyloid β‐Protein Oligomers: A Link between Structure and Activity?

[Review]
Brigita Urbanc
Isr. J. Chem., February 03, 2017, https://doi.org/10.1002/ijch.201600097 Read article

Theory of Amyloid Fibril Nucleation from Folded Proteins

Theory of Amyloid Fibril Nucleation from Folded Proteins

[Full Paper]
Lingyun Zhang, Jeremy D. Schmit
Isr. J. Chem., January 30, 2017, https://doi.org/10.1002/ijch.201600079 Read article

Conformational Transitions of the Amyloid-β Peptide Upon Copper(II) Binding and pH Changes

Conformational Transitions of the Amyloid‐β Peptide Upon Copper(II) Binding and pH Changes

[Full Paper]
Qinghua Liao, Michael C. Owen, Olujide O. Olubiyi, Bogdan Barz, Birgit Strodel
Isr. J. Chem., January 20, 2017, https://doi.org/10.1002/ijch.201600108 Read article

Cerebrospinal Fluid Proteins as Regulators of Beta-amyloid Aggregation and Toxicity

Cerebrospinal Fluid Proteins as Regulators of Beta‐amyloid Aggregation and Toxicity

[Review]
Kayla M. Pate, Regina M. Murphy
Isr. J. Chem., January 18, 2017, https://doi.org/10.1002/ijch.201600078 Read article

The Amyloid-β Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal Ions

The Amyloid‐β Peptide in Amyloid Formation Processes: Interactions with Blood Proteins and Naturally Occurring Metal Ions

[Review]
Cecilia Wallin, Jinghui Luo, Jüri Jarvet, Sebastian K. T. S. Wärmländer, Astrid Gräslund
Isr. J. Chem., December 28, 2016, https://doi.org/10.1002/ijch.201600105 Read article

Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?

Evolutionary Adaptation and Amyloid Formation: Does the Reduced Amyloidogenicity and Cytotoxicity of Ursine Amylin Contribute to the Metabolic Adaption of Bears and Polar Bears?

[Full Paper]
Rehana Akter, Andisheh Abedini, Zachary Ridgway, Xiaoxue Zhang, Joel Kleinberg, Ann Marie Schmidt, Daniel P. Raleigh
Isr. J. Chem., December 19, 2016, https://doi.org/10.1002/ijch.201600081 Read article

Fluorescent Markers for Amyloid-β Detection: Computational Insights

Fluorescent Markers for Amyloid‐β Detection: Computational Insights

[Review]
Francesca Peccati, Stefano Pantaleone, Xavier Solans-Monfort, Mariona Sodupe
Isr. J. Chem., December 01, 2016, https://doi.org/10.1002/ijch.201600114 Read article

Generation of Amyloid-β Peptides by γ-Secretase

Generation of Amyloid‐β Peptides by γ‐Secretase

[Review]
Rodrigo Aguayo-Ortiz, Laura Dominguez
Isr. J. Chem., November 25, 2016, https://doi.org/10.1002/ijch.201600073 Read article

Formation of Apoptosis-Inducing Amyloid Fibrils by Tryptophan

Formation of Apoptosis‐Inducing Amyloid Fibrils by Tryptophan

[Full Paper]
Shira Shaham-Niv, Pavel Rehak, Lela Vuković, Lihi Adler-Abramovich, Petr Král, Ehud Gazit
Isr. J. Chem., November 16, 2016, https://doi.org/10.1002/ijch.201600076 Read article

Molecular Simulations of Amyloid Structures, Toxicity, and Inhibition

Molecular Simulations of Amyloid Structures, Toxicity, and Inhibition

[Review]
Mingzhen Zhang, Baiping Ren, Hong Chen, Yan Sun, Jie Ma, Binbo Jiang, Jie Zheng
Isr. J. Chem., November 16, 2016, https://doi.org/10.1002/ijch.201600075 Read article

Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

Structural Biology of Calcitonin: From Aqueous Therapeutic Properties to Amyloid Aggregation

[Review]
Kian Kamgar-Parsi, James Tolchard, Birgit Habenstein, Antoine Loquet, Akira Naito, Ayyalusamy Ramamoorthy
Isr. J. Chem., November 15, 2016, https://doi.org/10.1002/ijch.201600096 Read article

Compilation and Analysis of Enzymes, Engineered Antibodies, and Nanoparticles Designed to Interfere with Amyloid-β Aggregation

Compilation and Analysis of Enzymes, Engineered Antibodies, and Nanoparticles Designed to Interfere with Amyloid‐β Aggregation

[Review]
Jun Zhao, Buyong Ma, Ruth Nussinov
Isr. J. Chem., October 25, 2016, https://doi.org/10.1002/ijch.201600093 Read article

Coarse-grained and All-atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation

Coarse‐grained and All‐atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation

[Review]
Mara Chiricotto, Thanh Thuy Tran, Phuong H. Nguyen, Simone Melchionna, Fabio Sterpone, Philippe Derreumaux
Isr. J. Chem., August 01, 2016, https://doi.org/10.1002/ijch.201600048 Read article

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