(2023). Advanced Big Data Analysis for Deciphering the Role of Protein Misfolding and Interactions in the Pathogenesis of Alzheimer’s Disease. In 2023 IEEE International Conference on Big Data (BigData) (pp. 4614–4617). IEEE. https://doi.org/10.1109/bigdata59044.2023.10386706
Περίληψη
Predicting the three-dimensional structure of proteins directly from their sequence of amino acids remains a challenge in biomedical research. Protein functionality depends not only on its sequence but also on the precise folding that occurs during the process of developing their tertiary structure. Misfolded proteins may lead to the generation of entities that are inherently toxic to the organism, such as the formation of amyloid fibrils in the context of Alzheimer’s disease. Herein, the structural conformation of specific missense mutations in proteins involved in Alzheimer’s disease was performed through computational analysis and prediction of the binding mode and multiplicity of them was further assessed. Our findings reveal direct sequence-to-structure motifs from single polypeptides and the received domains with the proper fold. Nevertheless, the positions with the particular deviations are most commonly accompanied by limited downward spikes in pLDDT value, suggesting lower prediction confidence and potential disorder.
- DOI
- 10.1109/bigdata59044.2023.10386706
- Τύπος
- Άρθρο σε Πρακτικά Συνεδρίου
- Έτος
- 2023
Σύνδεσμοι
BibTeX
@inproceedings{krokidis2023advanced,
title = {Advanced Big Data Analysis for Deciphering the Role of Protein Misfolding and Interactions in the Pathogenesis of Alzheimer’s Disease},
author = {Marios G. Krokidis and Georgios N. Dimitrakopoulos and Themis P. Exarchos and Aristidis G. Vrahatis and Panagiotis Vlamos},
url = {https://doi.org/10.1109/bigdata59044.2023.10386706},
doi = {10.1109/bigdata59044.2023.10386706},
year = {2023},
date = {2023-01-01},
booktitle = {2023 IEEE International Conference on Big Data (BigData)},
pages = {4614–4617},
publisher = {IEEE},
abstract = {Predicting the three-dimensional structure of proteins directly from their sequence of amino acids remains a challenge in biomedical research. Protein functionality depends not only on its sequence but also on the precise folding that occurs during the process of developing their tertiary structure. Misfolded proteins may lead to the generation of entities that are inherently toxic to the organism, such as the formation of amyloid fibrils in the context of Alzheimer’s disease. Herein, the structural conformation of specific missense mutations in proteins involved in Alzheimer’s disease was performed through computational analysis and prediction of the binding mode and multiplicity of them was further assessed. Our findings reveal direct sequence-to-structure motifs from single polypeptides and the received domains with the proper fold. Nevertheless, the positions with the particular deviations are most commonly accompanied by limited downward spikes in pLDDT value, suggesting lower prediction confidence and potential disorder.},
keywords = {},
pubstate = {published},
tppubtype = {inproceedings}
}