Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation
Aberrant protein folding known as protein misfolding is counted as one of the striking factors
of neurodegenerative diseases. The extensive range of pathologies caused by protein …
of neurodegenerative diseases. The extensive range of pathologies caused by protein …
[HTML][HTML] Intrinsic determinants of prion protein neurotoxicity in Drosophila: from sequence to (dys)function
A Cembran, P Fernandez-Funez - Frontiers in Molecular …, 2023 - frontiersin.org
Prion diseases are fatal brain disorders characterized by deposition of insoluble isoforms of
the prion protein (PrP). The normal and pathogenic structures of PrP are relatively well …
the prion protein (PrP). The normal and pathogenic structures of PrP are relatively well …
Pyrazinamide drug resistance in RpsA mutant (∆438A) of Mycobacterium tuberculosis: Dynamics of essential motions and free‐energy landscape analysis
Pyrazinamide is an essential first‐line antitubercular drug which plays pivotal role in
tuberculosis treatment. It is a prodrug that requires amide hydrolysis by mycobacterial …
tuberculosis treatment. It is a prodrug that requires amide hydrolysis by mycobacterial …
Conformational fluctuations and induced orientation of a protein, its solvation shell, and bulk water in weak non-unfolding external electric fields
Y Shuto, E Walinda, D Morimoto… - The Journal of Physical …, 2023 - ACS Publications
Extreme external electric fields have been reported to disrupt the tertiary structure of stably
folded proteins; however, the effects of weaker electric fields on many biomolecules …
folded proteins; however, the effects of weaker electric fields on many biomolecules …
Drug repurposing against arabinosyl transferase (EmbC) of Mycobacterium tuberculosis: Essential dynamics and free energy minima based binding mechanics …
Arabinosyl tranferases (embA, embB, embC) are the key enzymes responsible for
biogenesis of arabinan domain of arabinogalactan (AG) and lipoarabinomannan (LAM), two …
biogenesis of arabinan domain of arabinogalactan (AG) and lipoarabinomannan (LAM), two …
Temperature-induced misfolding in prion protein: evidence of multiple partially disordered states stabilized by non-native hydrogen bonds
NG Chamachi, S Chakrabarty - Biochemistry, 2017 - ACS Publications
The structural basis of pathways of misfolding of a cellular prion (PrPC) into the toxic scrapie
form (PrPSC) and identification of possible intermediates (eg, PrP*) still eludes us. In this …
form (PrPSC) and identification of possible intermediates (eg, PrP*) still eludes us. In this …
Thermostabilizing mechanisms of canonical single amino acid substitutions at a GH1 β‐glucosidase probed by multiple MD and computational approaches
REO Rocha, DCB Mariano, TS Almeida… - Proteins: Structure …, 2023 - Wiley Online Library
Abstract β‐glucosidases play a pivotal role in second‐generation biofuel (2G‐biofuel)
production. For this application, thermostable enzymes are essential due to the denaturing …
production. For this application, thermostable enzymes are essential due to the denaturing …
Molecular insights into the critical role of gallate moiety of green tea catechins in modulating prion fibrillation, cellular internalization, and neuronal toxicity
N Admane, A Srivastava, S Jamal, R Sharma… - International Journal of …, 2022 - Elsevier
Transmissible spongiform encephalopathies (TSEs) or prion diseases are fatal
neurodegenerative diseases with no approved therapeutics. TSE pathology is characterized …
neurodegenerative diseases with no approved therapeutics. TSE pathology is characterized …
[HTML][HTML] Insight from animals resistant to prion diseases: Deciphering the genotype–morphotype–phenotype code for the prion protein
Prion diseases are a group of neurodegenerative diseases endemic in humans and several
ruminants caused by the misfolding of native prion protein (PrP) into pathological …
ruminants caused by the misfolding of native prion protein (PrP) into pathological …
[HTML][HTML] Structural and dynamical determinants of a β-sheet-enriched intermediate involved in amyloid fibrillar assembly of human prion protein
L Russo, G Salzano, A Corvino, E Bistaffa, F Moda… - Chemical …, 2022 - pubs.rsc.org
The conformational conversion of the cellular prion protein (PrPC) into a misfolded,
aggregated and infectious scrapie isoform is associated with prion disease pathology and …
aggregated and infectious scrapie isoform is associated with prion disease pathology and …