Hydration Thermodynamics of the N-Terminal FAD Mutants of Amyloid-β-Reference-Cited by-同舟云学术

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Hydration Thermodynamics of the N-Terminal FAD Mutants of Amyloid-β

Published:2021-01-14 Issue:1 Volume:61 Page:298-310
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Aggarwal Leena¹,Biswas Parbati¹^ORCID

Affiliation:

1. Department of Chemistry, University of Delhi, Delhi 110007, India

Funder

University of Delhi

Council of Scientific and Industrial Research

Science and Engineering Research Board

Department of Science and Technology, Ministry of Science and Technology

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jcim.0c01286

Reference87 articles.

1. Cellular Regulation of Amyloid Formation in Aging and Disease

2. Proteostasis Failure in Neurodegenerative Diseases: Focus on Oxidative Stress

3. A? Oligomers ? a decade of discovery

4. Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β–amyloid precursor protein gene

5. Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type

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1. Effect of caffeine on the aggregation of amyloid-β–A 3D RISM study;The Journal of Chemical Physics;2024-03-22

2. Aggregation propensities of proteins with varying degrees of disorder;Journal of Computational Chemistry;2022-12-05

3. Impact of A2T and D23N mutations on C99 homodimer conformations;The Journal of Chemical Physics;2022-08-28

4. Virtual Quasi-2D Intermediates as Building Blocks for Plausible Structural Models of Amyloid Fibrils from Proteins with Complex Topologies: A Case Study of Insulin;Langmuir;2022-05-26

5. Effect of Cholesterol Molecules on Aβ1-42 Wild-Type and Mutants Trimers;Molecules;2022-02-18

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