Molecular simulation unravels the amyloidogenic misfolding of nascent ApoA1 protein, driven by deleterious point mutations occurring in between 170–178 hotspot region-Reference-Cited by-同舟云学术

Molecular simulation unravels the amyloidogenic misfolding of nascent ApoA1 protein, driven by deleterious point mutations occurring in between 170–178 hotspot region

Published:2021-10-06 Issue: Volume: Page:1-13
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Chandrasekhar G.¹,Chandra Sekar P.¹,Srinivasan E.¹,Amarnath A.¹,Pengyong H.²,Rajasekaran R.¹

Affiliation:

1. Bioinformatics Lab, Department of Biotechnology, School of Bio Sciences and Technology, Vellore Institute of Technology (Deemed to be University), Vellore, Tamil Nadu, India

2. Central Lab, Changzhi Medical College, Changzhi, China

Funder

VIT

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2021.1986134

Reference76 articles.

1. Expert consensus recommendations to improve diagnosis of ATTR amyloidosis with polyneuropathy

2. Normal modes for predicting protein motions: A comprehensive database assessment and associated Web tool

3. Apolipoprotein A-I: the dual face of a protein

4. Assignment of the apolipoprotein A-I gene to 11q23 based on RFLP in a case with a partial deletion of chromosome 11, del(11)(q23.3?qter)

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