Cargando…

Q-Rich Yeast Prion [PSI(+)] Accelerates Aggregation of Transthyretin, a Non-Q-Rich Human Protein

Interactions amongst different amyloid proteins have been proposed as a probable mechanism of aggregation and thus an important risk factor for the onset as well as progression of various neurodegenerative disorders including Alzheimer's, Parkinson's, Huntington's, and Amyotrophic Lat...

Descripción completa

Detalles Bibliográficos
Autores principales:	Verma, Meenakshi, Girdhar, Amandeep, Patel, Basant, Ganguly, Nirmal K., Kukreti, Ritushree, Taneja, Vibha
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Frontiers Media S.A. 2018
Materias:	Neuroscience
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5859028/ https://www.ncbi.nlm.nih.gov/pubmed/29593496 http://dx.doi.org/10.3389/fnmol.2018.00075

Ejemplares similares

Curcumin Prevents Formation of Polyglutamine Aggregates by Inhibiting Vps36, a Component of the ESCRT-II Complex
por: Verma, Meenakshi, et al.
Publicado: (2012)

Analyzing the Birth and Propagation of Two Distinct Prions, [PSI(+)] and [Het-s](y), in Yeast
por: Mathur, Vidhu, et al.
Publicado: (2010)

An acridine derivative, [4,5-bis{(N-carboxy methyl imidazolium)methyl}acridine] dibromide, shows anti-TDP-43 aggregation effect in ALS disease models
por: Prasad, Archana, et al.
Publicado: (2016)

Implications of oxidative stress in chronic kidney disease: a review on current concepts and therapies
por: Verma, Sagar, et al.
Publicado: (2021)

A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions
por: Oishi, Keita, et al.
Publicado: (2013)

Methionine Sulfoxide Reductases Suppress the Formation of the [PSI(+)] Prion and Protein Aggregation in Yeast
por: Schepers, Jana, et al.
Publicado: (2023)

Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains
por: Espinosa Angarica, Vladimir, et al.
Publicado: (2013)

Structural Definition Is Important for the Propagation of the Yeast [PSI(+)] Prion
por: Marchante, Ricardo, et al.
Publicado: (2013)

A unifying model for the propagation of prion proteins in yeast brings insight into the [PSI(+)] prion
por: Lemarre, Paul, et al.
Publicado: (2020)

Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [PSI(+)] Prion
por: Stanford, Katherine E., et al.
Publicado: (2023)

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

Could yeast prion domains originate from polyQ/N tracts?
por: Alexandrov, Alexander I., et al.
Publicado: (2013)

Yeast Prions: Protein Aggregation Is Not Enough
por: Sherman, Michael Y
Publicado: (2004)

The Number and Transmission of [PSI (+)] Prion Seeds (Propagons) in the Yeast Saccharomyces cerevisiae
por: Byrne, Lee J., et al.
Publicado: (2009)

Autophagy protects against de novo formation of the [PSI(+)] prion in yeast
por: Speldewinde, Shaun H., et al.
Publicado: (2015)

The frequency of yeast [PSI(+)] prion formation is increased during chronological ageing
por: Speldewinde, Shaun H., et al.
Publicado: (2017)

A prolonged chronological lifespan is an unexpected benefit of the [PSI(+)] prion in yeast
por: Wang, Kai, et al.
Publicado: (2017)

The story of stolen chaperones: How overexpression of Q/N proteins cures yeast prions
por: Derkatch, Irina L, et al.
Publicado: (2013)

Q-values of some nuclides on the neutron-rich side of stability
por: Rudstam,G, et al.
Publicado: (1970)

Heterologous Gln/Asn-Rich Proteins Impede the Propagation of Yeast Prions by Altering Chaperone Availability
por: Yang, Zi, et al.
Publicado: (2013)

The yeast molecular chaperone, Hsp104, influences transthyretin aggregate formation
por: Knier, Adam S., et al.
Publicado: (2022)

Nonsense Mutations in the Yeast SUP35 Gene Affect the [PSI(+)] Prion Propagation
por: Trubitsina, Nina P., et al.
Publicado: (2020)

Precision Q-value determinations for neutron-rich rubidium isotopes at TRISTAN
por: Brenner, D S, et al.
Publicado: (1981)

Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI (+)] prion
por: Doronina, Victoria A., et al.
Publicado: (2015)

Engineered bacterial hydrophobic oligopeptide repeats in a synthetic yeast prion, [REP-PSI(+)]
por: Gasset-Rosa, Fátima, et al.
Publicado: (2015)

Controlling the prion propensity of glutamine/asparagine-rich proteins
por: Paul, Kacy R, et al.
Publicado: (2015)

EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates
por: Zou, Huizhen, et al.
Publicado: (2023)

Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI(+)] prion formation
por: Speldewinde, Shaun H., et al.
Publicado: (2017)

The [PSI(+)] yeast prion does not wildly affect proteome composition whereas selective pressure exerted on [PSI(+)] cells can promote aneuploidy
por: Chan, Patrick H. W., et al.
Publicado: (2017)

Importance of the Q/N-rich segment for protein stability of endogenous mouse TDP-43
por: Sato, Toshiya, et al.
Publicado: (2022)

Methionine Oxidation of Sup35 Protein Induces Formation of the [PSI(+)] Prion in a Yeast Peroxiredoxin Mutant
por: Sideri, Theodora C., et al.
Publicado: (2011)

The Pub1 and Upf1 Proteins Act in Concert to Protect Yeast from Toxicity of the [PSI(+)] Prion
por: Urakov, Valery N., et al.
Publicado: (2018)

Antiprion systems in yeast cooperate to cure or prevent the generation of nearly all [PSI(+)] and [URE3] prions
por: Son, Moonil, et al.
Publicado: (2022)

Human J-Domain Protein DnaJB6 Protects Yeast from [PSI(+)] Prion Toxicity
por: Dolder, Richard E., et al.
Publicado: (2022)

Sequestration of Sup35 by Aggregates of huntingtin Fragments Causes Toxicity of [PSI(+)] Yeast
por: Zhao, Xiaohong, et al.
Publicado: (2012)

Structural and dynamic studies reveal that the Ala-rich region of ataxin-7 initiates α-helix formation of the polyQ tract but suppresses its aggregation
por: Hong, Jun-Ye, et al.
Publicado: (2019)

Uncovering the Mechanism of Aggregation of Human Transthyretin
por: Saelices, Lorena, et al.
Publicado: (2015)

The Importance of a Gatekeeper Residue on the Aggregation of Transthyretin: IMPLICATIONS FOR TRANSTHYRETIN-RELATED AMYLOIDOSES
por: Sant'Anna, Ricardo, et al.
Publicado: (2014)

Oxidative Stress: A Key Modulator in Neurodegenerative Diseases
por: Singh, Anju, et al.
Publicado: (2019)

Oxidative Stress: Role and Response of Short Guanine Tracts at Genomic Locations
por: Singh, Anju, et al.
Publicado: (2019)

Cannot write session to /tmp/vufind_sessions/sess_4hr9k97rdr5ktfnef9jam990n2