The route to protein aggregate superstructures: Particulates and amyloid-like spherulites

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

The route to protein aggregate superstructures : Particulates and amyloid-like spherulites. / Vetri, Valeria; Foderà, Vito.

In: FEBS Letters, Vol. 589, No. 19 Pt A, 14.09.2015, p. 2448-63.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Vetri, V & Foderà, V 2015, 'The route to protein aggregate superstructures: Particulates and amyloid-like spherulites', FEBS Letters, vol. 589, no. 19 Pt A, pp. 2448-63. https://doi.org/10.1016/j.febslet.2015.07.006

APA

Vetri, V., & Foderà, V. (2015). The route to protein aggregate superstructures: Particulates and amyloid-like spherulites. FEBS Letters, 589(19 Pt A), 2448-63. https://doi.org/10.1016/j.febslet.2015.07.006

Vancouver

Vetri V, Foderà V. The route to protein aggregate superstructures: Particulates and amyloid-like spherulites. FEBS Letters. 2015 Sep 14;589(19 Pt A):2448-63. https://doi.org/10.1016/j.febslet.2015.07.006

Author

Vetri, Valeria ; Foderà, Vito. / The route to protein aggregate superstructures : Particulates and amyloid-like spherulites. In: FEBS Letters. 2015 ; Vol. 589, No. 19 Pt A. pp. 2448-63.

Bibtex

@article{fe4665f13aef497f9a33da08f81629d2,
title = "The route to protein aggregate superstructures: Particulates and amyloid-like spherulites",
abstract = "Depending on external conditions, native proteins may change their structure and undergo different association routes leading to a large scale polymorphism of the aggregates. This feature has been widely observed but is not fully understood yet. This review focuses on morphologies, physico-chemical properties and mechanisms of formation of amyloid structures and protein superstructures. In particular, the main focus will be on protein particulates and amyloid-like spherulites, briefly summarizing possible experimental methods of analysis. Moreover, we will highlight the role of protein conformational changes and dominant forces in driving association together with their connection with the final aggregate structure. Eventually, we will discuss future perspectives in this field and we will comment what is, in our opinion, urgently needed.",
keywords = "Amyloid, Humans, Microscopy, Fluorescence, Multiphoton, Models, Chemical, Models, Molecular, Protein Aggregates, Protein Aggregation, Pathological, Protein Conformation, Thermodynamics, X-Ray Diffraction",
author = "Valeria Vetri and Vito Foder{\`a}",
note = "Copyright {\textcopyright} 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",
year = "2015",
month = sep,
day = "14",
doi = "10.1016/j.febslet.2015.07.006",
language = "English",
volume = "589",
pages = "2448--63",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "19 Pt A",

}

RIS

TY - JOUR

T1 - The route to protein aggregate superstructures

T2 - Particulates and amyloid-like spherulites

AU - Vetri, Valeria

AU - Foderà, Vito

N1 - Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

PY - 2015/9/14

Y1 - 2015/9/14

N2 - Depending on external conditions, native proteins may change their structure and undergo different association routes leading to a large scale polymorphism of the aggregates. This feature has been widely observed but is not fully understood yet. This review focuses on morphologies, physico-chemical properties and mechanisms of formation of amyloid structures and protein superstructures. In particular, the main focus will be on protein particulates and amyloid-like spherulites, briefly summarizing possible experimental methods of analysis. Moreover, we will highlight the role of protein conformational changes and dominant forces in driving association together with their connection with the final aggregate structure. Eventually, we will discuss future perspectives in this field and we will comment what is, in our opinion, urgently needed.

AB - Depending on external conditions, native proteins may change their structure and undergo different association routes leading to a large scale polymorphism of the aggregates. This feature has been widely observed but is not fully understood yet. This review focuses on morphologies, physico-chemical properties and mechanisms of formation of amyloid structures and protein superstructures. In particular, the main focus will be on protein particulates and amyloid-like spherulites, briefly summarizing possible experimental methods of analysis. Moreover, we will highlight the role of protein conformational changes and dominant forces in driving association together with their connection with the final aggregate structure. Eventually, we will discuss future perspectives in this field and we will comment what is, in our opinion, urgently needed.

KW - Amyloid

KW - Humans

KW - Microscopy, Fluorescence, Multiphoton

KW - Models, Chemical

KW - Models, Molecular

KW - Protein Aggregates

KW - Protein Aggregation, Pathological

KW - Protein Conformation

KW - Thermodynamics

KW - X-Ray Diffraction

U2 - 10.1016/j.febslet.2015.07.006

DO - 10.1016/j.febslet.2015.07.006

M3 - Journal article

C2 - 26183565

VL - 589

SP - 2448

EP - 2463

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 19 Pt A

ER -

ID: 161623467