Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation

A Rahman, B Saikia, CR Gogoi, A Baruah - Progress in Biophysics and …, 2022 - Elsevier
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 …

Molecular mechanism of the misfolding and oligomerization of the prion protein: current understanding and its implications

J Singh, JB Udgaonkar - Biochemistry, 2015 - ACS Publications
Prion diseases, also known as transmissible spongiform encephalopathies, make up a
group of fatal neurodegenerative disorders linked with the misfolding and aggregation of the …

Structural basis of prion inhibition by phenothiazine compounds

PK Baral, M Swayampakula, MK Rout, NNV Kav… - Structure, 2014 - cell.com
Conformational transitions of the cellular form of the prion protein, PrP C, into an infectious
isoform, PrP Sc, are considered to be central events in the progression of fatal …

Natural and synthetic derivatives of hydroxycinnamic acid modulating the pathological transformation of amyloidogenic proteins

VI Muronetz, K Barinova, S Kudryavtseva… - Molecules, 2020 - mdpi.com
This review presents the main properties of hydroxycinnamic acid (HCA) derivatives and
their potential application as agents for the prevention and treatment of neurodegenerative …

Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease

Z Zheng, M Zhang, Y Wang, R Ma, C Guo, L Feng… - Scientific reports, 2018 - nature.com
Prion diseases are caused by the propagation of misfolded cellular prion proteins (PrPs). A
completely prion disease-resistant genotype, V127M129, has been identified in Papua New …

Mechanism of unfolding of human prion protein

RK Singh, NG Chamachi, S Chakrabarty… - The Journal of …, 2017 - ACS Publications
Misfolding and aggregation of prion proteins are associated with several neurodegenerative
diseases. Therefore, understanding the mechanism of the misfolding process is of enormous …

Insights into the bidirectional properties of the sheep–deer prion transmission barrier

C Harrathi, N Fernández-Borges, H Eraña… - Molecular …, 2019 - Springer
The large chronic wasting disease (CWD)-affected cervid population in the USA and
Canada, and the risk of the disease being transmitted to humans through intermediate …

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 …

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 …

Complexes between cationic pyridylphenylene dendrimers and ovine prion protein: do hydrophobic interactions matter?

S Sorokina, P Semenyuk, Y Stroylova, V Muronetz… - RSC …, 2017 - pubs.rsc.org
Here, the interactions between cationic pyridylphenylene dendrimers of the second, third
and fourth generations and full-length ovine prion protein (PrP) were studied using …