Cargando…

Solvent Microenvironments and Copper Binding Alters the Conformation and Toxicity of a Prion Fragment

The secondary structures of amyloidogenic proteins are largely influenced by various intra and extra cellular microenvironments and metal ions that govern cytotoxicity. The secondary structure of a prion fragment, PrP(111-126), was determined using circular dichroism (CD) spectroscopy in various mic...

Descripción completa

Detalles Bibliográficos
Autores principales:	Inayathullah, Mohammed, Satheeshkumar, K. S., Malkovskiy, Andrey V., Carre, Antoine L., Sivanesan, Senthilkumar, Hardesty, Jasper O., Rajadas, Jayakumar
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2013
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3874036/ https://www.ncbi.nlm.nih.gov/pubmed/24386462 http://dx.doi.org/10.1371/journal.pone.0085160

Ejemplares similares

Effect of osmolytes on the conformation and aggregation of some amyloid peptides: CD spectroscopic data
por: Inayathullah, Mohammed, et al.
Publicado: (2016)

Repurposing Disulfiram (Tetraethylthiuram Disulfide) as a Potential Drug Candidate against Borrelia burgdorferi In Vitro and In Vivo
por: Potula, Hari-Hara S. K., et al.
Publicado: (2020)

Possible Clues for Brain Energy Translation via Endolysosomal Trafficking of APP-CTFs in Alzheimer's Disease
por: Sivanesan, Senthilkumar, et al.
Publicado: (2018)

PEG/Dextran Double Layer Influences Fe Ion Release and Colloidal Stability of Iron Oxide Nanoparticles
por: Mohammadi, M. Rezaa, et al.
Publicado: (2018)

Borreliacidal activity of Borrelia metal transporter A (BmtA) binding small molecules by manganese transport inhibition
por: Wagh, Dhananjay, et al.
Publicado: (2015)

Attenuation of synaptic toxicity and MARK4/PAR1-mediated Tau phosphorylation by methylene blue for Alzheimer’s disease treatment
por: Sun, Wenchao, et al.
Publicado: (2016)

Rationally Designed Turn Promoting Mutation in the Amyloid-β Peptide Sequence Stabilizes Oligomers in Solution
por: Rajadas, Jayakumar, et al.
Publicado: (2011)

A conformational switch controlling the toxicity of the prion protein
por: Frontzek, Karl, et al.
Publicado: (2022)

Epigenetic Dominance of Prion Conformers
por: Saijo, Eri, et al.
Publicado: (2013)

Yeast Prions: Proteins Templating Conformation and an Anti-prion System
por: Wickner, Reed B., et al.
Publicado: (2015)

Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers
por: Ma, Jiyan, et al.
Publicado: (2022)

Fidgetin-Like 2 siRNA Enhances the Wound Healing Capability of a Surfactant Polymer Dressing
por: O'Rourke, Brian P., et al.
Publicado: (2019)

Azlocillin can be the potential drug candidate against drug-tolerant Borrelia burgdorferi sensu stricto JLB31
por: Pothineni, Venkata Raveendra, et al.
Publicado: (2020)

Prion-derived copper-binding peptide fragments catalyze the generation of superoxide anion in the presence of aromatic monoamines
por: Kawano, Tomonori
Publicado: (2006)

Copper coordination modulates prion conversion and infectivity in mammalian prion proteins
por: Legname, Giuseppe
Publicado: (2023)

Expression of Single Chain Variable Fragment (scFv) Molecules in Plants: A Comprehensive Update
por: Satheeshkumar, Padikara Kutty
Publicado: (2020)

Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein
por: Srivastava, Saurabh, et al.
Publicado: (2015)

Identification of new drug candidates against Borrelia burgdorferi using high-throughput screening
por: Pothineni, Venkata Raveendra, et al.
Publicado: (2016)

In vitro and in vivo evaluation of cephalosporins for the treatment of Lyme disease
por: Pothineni, Venkata Raveendra, et al.
Publicado: (2018)

Conformational diversity in purified prions produced in vitro
por: Walsh, Daniel J., et al.
Publicado: (2023)

Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates
por: Sneideris, Tomas, et al.
Publicado: (2020)

Calcium Binding Promotes Prion Protein Fragment 90–231 Conformational Change toward a Membrane Destabilizing and Cytotoxic Structure
por: Sorrentino, Sacha, et al.
Publicado: (2012)

Structural Consequences of Copper Binding to the Prion Protein
por: Salzano, Giulia, et al.
Publicado: (2019)

Spontaneous Variants of the [RNQ+] Prion in Yeast Demonstrate the Extensive Conformational Diversity Possible with Prion Proteins
por: Huang, Vincent J., et al.
Publicado: (2013)

Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency
por: Hannaoui, Samia, et al.
Publicado: (2017)

From Seeds to Fibrils and Back: Fragmentation as an Overlooked Step in the Propagation of Prions and Prion-Like Proteins
por: Marrero-Winkens, Cristóbal, et al.
Publicado: (2020)

Defining the Conformational Features of Anchorless, Poorly Neuroinvasive Prions
por: Bett, Cyrus, et al.
Publicado: (2013)

Prion strains in mammals: Different conformations leading to disease
por: Morales, Rodrigo
Publicado: (2017)

Nanoengineered biomaterials for regenerative medicine
por: Mozafari, Masoud, et al.
Publicado: (2018)

Transient multimers modulate conformer abundances of prion protein monomer through conformational selection
por: Van der Rest, Guillaume, et al.
Publicado: (2019)

The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion
por: Giachin, Gabriele, et al.
Publicado: (2015)

Surface modification of a polyhedral oligomeric silsesquioxane poly(carbonate-urea) urethane (POSS-PCU) nanocomposite polymer as a stent coating for enhanced capture of endothelial progenitor cells
por: Tan, Aaron, et al.
Publicado: (2013)

Disulfide-crosslink scanning reveals prion–induced conformational changes and prion strain–specific structures of the pathological prion protein PrP(Sc)
por: Taguchi, Yuzuru, et al.
Publicado: (2018)

Role of ADAMs in the Ectodomain Shedding and Conformational Conversion of the Prion Protein
por: Taylor, David R., et al.
Publicado: (2009)

Characterization of spontaneously generated prion-like conformers in cultured cells
por: Zou, Roger S., et al.
Publicado: (2011)

Strain conformation, primary structure and the propagation of the yeast prion [PSI(+)]
por: Verges, Katherine J., et al.
Publicado: (2011)

Detecting Differences in Prion Protein Conformation by Quantifying Methionine Oxidation
por: Silva, Christopher J., et al.
Publicado: (2022)

Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments
por: Michiels, Emiel, et al.
Publicado: (2020)

The protease-sensitive N-terminal polybasic region of prion protein modulates its conversion to the pathogenic prion conformer
por: Zhang, Xiangyi, et al.
Publicado: (2021)

Low Copper and High Manganese Levels in Prion Protein Plaques
por: Johnson, Christopher J., et al.
Publicado: (2013)

Cannot write session to /tmp/vufind_sessions/sess_8v61c4cu58cjt9e9261fm39neu