Cargando…

Global Proteotoxicity Caused by Human β(2) Microglobulin Variants Impairs the Unfolded Protein Response in C. elegans

Aggregation of β(2) microglobulin (β(2)m) into amyloid fibrils is associated with systemic amyloidosis, caused by the deposition of amyloid fibrils containing the wild-type protein and its truncated variant, ΔN6 β(2)m, in haemo-dialysed patients. A second form of familial systemic amyloidosis caused...

Descripción completa

Detalles Bibliográficos
Autores principales:	Good, Sarah C., Dewison, Katherine M., Radford, Sheena E., van Oosten-Hawle, Patricija
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2021
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8509642/ https://www.ncbi.nlm.nih.gov/pubmed/34639093 http://dx.doi.org/10.3390/ijms221910752

Ejemplares similares

Human wild‐type and D76N β(2)‐microglobulin variants are significant proteotoxic and metabolic stressors for transgenic C. elegans
por: Raimondi, Sara, et al.
Publicado: (2023)

Organismal Roles of Hsp90
por: van Oosten-Hawle, Patricija
Publicado: (2023)

Exploiting inter-tissue stress signaling mechanisms to preserve organismal proteostasis during aging
por: van Oosten-Hawle, Patricija
Publicado: (2023)

Single residue modulators of amyloid formation in the N-terminal P1-region of α-synuclein
por: Ulamec, Sabine M., et al.
Publicado: (2022)

Understanding the complex mechanisms of β(2)-microglobulin amyloid assembly
por: Eichner, Timo, et al.
Publicado: (2011)

Organismal proteostasis: role of cell-nonautonomous regulation and transcellular chaperone signaling
por: van Oosten-Hawle, Patricija, et al.
Publicado: (2014)

Regulation of cell-non-autonomous proteostasis in metazoans
por: O'Brien, Daniel, et al.
Publicado: (2016)

The Intestine as a Lifespan- and Proteostasis-Promoting Signaling Tissue
por: Hodge, Francesca, et al.
Publicado: (2022)

Intermolecular Alignment in β(2)-Microglobulin Amyloid Fibrils
por: Debelouchina, Galia T., et al.
Publicado: (2010)

A short motif in the N-terminal region of α-synuclein is critical for both aggregation and function
por: Doherty, Ciaran P. A., et al.
Publicado: (2020)

Comparison of the aggregation of homologous β(2)-microglobulin variants reveals protein solubility as a key determinant of amyloid formation
por: Pashley, Clare L., et al.
Publicado: (2016)

Disease-relevant β(2)-microglobulin variants share a common amyloid fold
por: Wilkinson, Martin, et al.
Publicado: (2023)

A Common β-Sheet Architecture Underlies in Vitro and in Vivo β(2)-Microglobulin Amyloid Fibrils
por: Jahn, Thomas R., et al.
Publicado: (2008)

The role of conformational flexibility in β(2)-microglobulin amyloid fibril formation at neutral pH
por: Hodkinson, John P, et al.
Publicado: (2012)

Glimpses of the molecular mechanisms of β(2)-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape
por: Platt, Geoffrey W., et al.
Publicado: (2009)

Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin
por: Fukasawa, Kanon, et al.
Publicado: (2016)

Extracellular matrix components modulate different stages in β(2)-microglobulin amyloid formation
por: Benseny-Cases, Núria, et al.
Publicado: (2019)

Globular Tetramers of β(2)-Microglobulin Assemble into Elaborate Amyloid Fibrils
por: White, Helen E., et al.
Publicado: (2009)

Fibril Growth Kinetics Reveal a Region of β(2)-microglobulin Important for Nucleation and Elongation of Aggregation
por: Platt, Geoffrey W., et al.
Publicado: (2008)

Characterization of the Response of Primary Cells Relevant to Dialysis-Related Amyloidosis to β(2)-Microglobulin Monomer and Fibrils
por: Porter, Morwenna Y., et al.
Publicado: (2011)

Increased levels of Stress-inducible phosphoprotein-1 accelerates amyloid-β deposition in a mouse model of Alzheimer’s disease
por: Lackie, Rachel E., et al.
Publicado: (2020)

Collagen I Weakly Interacts with the β-Sheets of β(2)-Microglobulin and Enhances Conformational Exchange To Induce Amyloid Formation
por: Hoop, Cody L., et al.
Publicado: (2019)

Investigation of D76N β(2)-Microglobulin Using Protein Footprinting and Structural Mass Spectrometry
por: Cornwell, Owen, et al.
Publicado: (2021)

Infliction of proteotoxic stresses by impairment of the unfolded protein response or proteasomal inhibition as a therapeutic strategy for mast cell leukemia
por: Wilhelm, Thomas, et al.
Publicado: (2017)

Frondoside A Attenuates Amyloid-β Proteotoxicity in Transgenic Caenorhabditis elegans by Suppressing Its Formation
por: Tangrodchanapong, Taweesak, et al.
Publicado: (2020)

Dimers of D76N-β(2)-microglobulin display potent antiamyloid aggregation activity
por: Maya-Martinez, Roberto, et al.
Publicado: (2022)

A PQM-1-Mediated Response Triggers Transcellular Chaperone Signaling and Regulates Organismal Proteostasis
por: O’Brien, Daniel, et al.
Publicado: (2018)

Lycium barbarum Extracts Extend Lifespan and Alleviate Proteotoxicity in Caenorhabditis elegans
por: Zhou, Haitao, et al.
Publicado: (2022)

HDX-ESI-MS Reveals Enhanced Conformational Dynamics of the Amyloidogenic Protein β(2)-Microglobulin upon Release from the MHC-1
por: Hodkinson, John P., et al.
Publicado: (2009)

Stacked Sets of Parallel, In-register β-Strands of β(2)-Microglobulin in Amyloid Fibrils Revealed by Site-directed Spin Labeling and Chemical Labeling
por: Ladner, Carol L., et al.
Publicado: (2010)

Deficient and Null Variants of SERPINA1 Are Proteotoxic in a Caenorhabditis elegans Model of α1-Antitrypsin Deficiency
por: Cummings, Erin E., et al.
Publicado: (2015)

Transcellular chaperone signaling is an intercellular stress-response distinct from the HSF-1–mediated heat shock response
por: Miles, Jay, et al.
Publicado: (2023)

Comparing Hydrogen Deuterium Exchange and Fast Photochemical Oxidation of Proteins: a Structural Characterisation of Wild-Type and ΔN6 β(2)-Microglobulin
por: Cornwell, Owen, et al.
Publicado: (2018)

Duplication of hsp-110 Is Implicated in Differential Success of Globodera Species under Climate Change
por: Jones, Laura M, et al.
Publicado: (2018)

Hyperactivation of the proteasome in Caenorhabditis elegans protects against proteotoxic stress and extends lifespan
por: Anderson, Raymond T., et al.
Publicado: (2022)

The role of the I(T)-state in D76N β(2)-microglobulin amyloid assembly: A crucial intermediate or an innocuous bystander?
por: Smith, Hugh I., et al.
Publicado: (2020)

The structure of a β(2)-microglobulin fibril suggests a molecular basis for its amyloid polymorphism
por: Iadanza, Matthew G., et al.
Publicado: (2018)

The integrated stress response remodels the microtubule-organizing center to clear unfolded proteins following proteotoxic stress
por: Hurwitz, Brian, et al.
Publicado: (2022)

β(2)-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH
por: Goodchild, Sophia C., et al.
Publicado: (2014)

β(2)-Microglobulin Amyloid Fibrils Are Nanoparticles That Disrupt Lysosomal Membrane Protein Trafficking and Inhibit Protein Degradation by Lysosomes
por: Jakhria, Toral, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_3mofnoiha34rsuhhcr386830c7