Self-Assembly of Ovalbumin Amyloid Pores: Effects on Membrane Permeabilization, Dipole Potential, and Bilayer Fluidity-Reference-Cited by-同舟云学术

Self-Assembly of Ovalbumin Amyloid Pores: Effects on Membrane Permeabilization, Dipole Potential, and Bilayer Fluidity

Published:2015-08-05 Issue:32 Volume:31 Page:8911-8922
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Bhattacharya Mily¹,Dogra Priyanka¹

Affiliation:

1. Department of Chemical Sciences, Indian Institute of Science Education and Research (IISER), Mohali, Knowledge City, Sector 81, S.A.S. Nagar, Mohali-140306, India

Funder

National Science Foundation

European Cooperation in Science and Technology

Department of Science and Technology, Ministry of Science and Technology

U.S. Department of Energy

Technion-Israel Institute of Technology

Engineering and Physical Sciences Research Council

University Of Edinburgh

Israel Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.langmuir.5b02074

Reference84 articles.

1. Amyloid Polymorphism: Structural Basis and Neurobiological Relevance

2. Energy landscapes of functional proteins are inherently risky

3. The amyloid state and its association with protein misfolding diseases

4. Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function

5. Amyloid Fibrils: the Eighth Wonder of the World in Protein Folding and Aggregation

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