Rita P-Y Chen
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Explore the profile of Rita P-Y Chen including associated specialties, affiliations and a list of published articles.
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46
Citations
387
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Recent Articles
1.
Allahyartorkaman M, Chan T, Chen E, Ng S, Chen Y, Wen J, et al.
J Am Chem Soc
. 2025 Mar;
PMID: 40074668
In this study, the role of phosphorylation in the liquid-liquid phase separation (LLPS) of tau, the underlying driving forces, and the potential implications of this separation on protein conformation and...
2.
Lee C, Saw J, Chen E, Wang C, Uchihashi T, Chen R
J Mol Biol
. 2024 Apr;
436(11):168576.
PMID: 38641239
Prions, the misfolding form of prion proteins, are contagious proteinaceous macromolecules. Recent studies have shown that infectious prion fibrils formed in the brain and non-infectious fibrils formed from recombinant prion...
3.
Chen E, Wang C, Liao Y, Chan F, Kanaoka Y, Uchihashi T, et al.
Nat Commun
. 2023 Sep;
14(1):5464.
PMID: 37673860
The abuse of antibiotics has led to the emergence of multidrug-resistant microbial pathogens, presenting a pressing challenge in global healthcare. Membrane-disrupting antimicrobial peptides (AMPs) combat so-called superbugs via mechanisms different...
4.
Chu B, Lin Y, Shen H, Chen R
Methods Mol Biol
. 2022 Oct;
2551:633-647.
PMID: 36310229
Amyloidogenesis, self-propagation of protein or peptide monomers to amyloid fibrils, has been linked to incurable pathogenesis of neurodegenerative diseases such as Alzheimer's disease and prion diseases. Investigations of amyloid structures...
5.
Chen E, Kao H, Lee C, Huang J, Wu K, Chen R
J Am Chem Soc
. 2022 Jul;
144(30):13888-13894.
PMID: 35857020
Fibrils of the hamster prion peptide (sHaPrP, sequence 108-144) were prepared in an acidic solution, and their structure was solved by cryogenic electron microscopy with a resolution of 2.23 Å...
6.
Chu B, Tsai R, Hung C, Kuo Y, Chen E, Chiang Y, et al.
Protein Sci
. 2022 May;
31(6):e4326.
PMID: 35634767
Prion diseases are transmissible fatal neurodegenerative disorders spreading between humans and other mammals. The pathogenic agent, prion, is a protease-resistant, β-sheet-rich protein aggregate, converted from a membrane protein called PrP...
7.
Chen S, Chen E, Yang S, Kuo P, Jan H, Yang T, et al.
Front Microbiol
. 2022 Jan;
12:821347.
PMID: 35095824
[This corrects the article DOI: 10.3389/fmicb.2021.678330.].
8.
Chen E, Weng C, Li Y, Wu M, Yang C, Lee K, et al.
Front Plant Sci
. 2021 Oct;
12:753217.
PMID: 34659322
Plant diseases are important issues in agriculture, and the development of effective and environment-friendly means of disease control is crucial and highly desired. Antimicrobial peptides (AMPs) are known as potential...
9.
Matiadis D, Ng S, Chen E, Nigianni G, Vidali V, Canko A, et al.
Biomedicines
. 2021 Aug;
9(8).
PMID: 34440159
Background: Alzheimer's disease (AD) involves impairment of Aβ clearance. Neprilysin (NEP) is the most efficient Aβ peptidase. Enhancement of the activity or expression of NEP may provide a prominent therapeutic...
10.
Chen E, Lin K, Sang J, Ho M, Lee C, Shih O, et al.
IUBMB Life
. 2021 Jul;
74(8):780-793.
PMID: 34288372
Prion protein is composed of a structure-unsolved N-terminal domain and a globular C-terminal domain. Under limited trypsin digestion, mouse recombinant prion protein can be cleaved into two parts at residue...