Cargando…

Smallest Secondary Nucleation Competent Aβ Aggregates Probed by an ATP-Independent Molecular Chaperone Domain

[Image: see text] Protein oligomerization is a commonly encountered strategy by which the functional repertoire of proteins is increased. This, however, is a double-edged sword strategy because protein oligomerization is notoriously difficult to control. Living organisms have therefore developed a n...

Descripción completa

Detalles Bibliográficos
Autores principales:	Leppert, Axel, Tiiman, Ann, Kronqvist, Nina, Landreh, Michael, Abelein, Axel, Vukojević, Vladana, Johansson, Jan
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Chemical Society 2021
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8028046/ https://www.ncbi.nlm.nih.gov/pubmed/33621049 http://dx.doi.org/10.1021/acs.biochem.1c00003

Ejemplares similares

A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain
por: Leppert, Axel, et al.
Publicado: (2023)

ATP‐independent molecular chaperone activity generated under reducing conditions
por: Leppert, Axel, et al.
Publicado: (2022)

Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro
por: Chen, Gefei, et al.
Publicado: (2020)

Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation
por: Chen, Gefei, et al.
Publicado: (2023)

Amyloid inhibition by molecular chaperones in vitro can be translated to Alzheimer's pathology in vivo
por: Abelein, Axel, et al.
Publicado: (2023)

Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state
por: Chen, Gefei, et al.
Publicado: (2017)

Small Molecule Decoys of Aggregation for Elimination of Aβ-Peptide Toxicity
por: Oasa, Sho, et al.
Publicado: (2023)

High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry
por: Kaldmäe, Margit, et al.
Publicado: (2019)

High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain
por: Abelein, Axel, et al.
Publicado: (2020)

Mass Spectrometry and Machine Learning Reveal Determinants of Client Recognition by Antiamyloid Chaperones
por: Österlund, Nicklas, et al.
Publicado: (2022)

Abilities of the BRICHOS domain to prevent neurotoxicity and fibril formation are dependent on a highly conserved Asp residue
por: Chen, Gefei, et al.
Publicado: (2022)

Recombinant Bri3 BRICHOS domain is a molecular chaperone with effect against amyloid formation and non-fibrillar protein aggregation
por: Poska, Helen, et al.
Publicado: (2020)

A “grappling hook” interaction connects self-assembly and chaperone activity of Nucleophosmin 1
por: Saluri, Mihkel, et al.
Publicado: (2023)

Comparison of Cerebrospinal Fluid Amyloidogenic Nanoplaques With Core Biomarkers of Alzheimer’s Disease
por: Aksnes, Mari, et al.
Publicado: (2021)

Serum Amyloidogenic Nanoplaques and Cytokines in Alzheimer’s Disease: Pilot Study in a Small Naturalistic Memory Clinic Cohort
por: Aksnes, Mari, et al.
Publicado: (2022)

Enumeration of Smallest Intervention Strategies in Genome-Scale Metabolic Networks
por: von Kamp, Axel, et al.
Publicado: (2014)

Amyloidogenic Nanoplaques in Blood Serum of Patients with Alzheimer’s Disease Revealed by Time-Resolved Thioflavin T Fluorescence Intensity Fluctuation Analysis
por: Tiiman, Ann, et al.
Publicado: (2019)

Molecular Mechanisms of Amyloid-β Self-Assembly Seeded by In Vivo-Derived Fibrils and Inhibitory Effects of the BRICHOS Chaperone
por: Kumar, Rakesh, et al.
Publicado: (2023)

Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform
por: Arndt, Tina, et al.
Publicado: (2022)

The interwoven fibril-like structure of amyloid-beta plaques in mouse brain tissue visualized using super-resolution STED microscopy
por: Johansson, Björn, et al.
Publicado: (2023)

Independent Control of Nucleation and Layer Growth in Nanowires
por: Maliakkal, Carina B., et al.
Publicado: (2020)

Associations of cerebrospinal fluid amyloidogenic nanoplaques with cytokines in Alzheimer’s disease
por: Aksnes, Mari, et al.
Publicado: (2021)

Metal Binding of Alzheimer’s Amyloid-β and Its Effect on Peptide Self-Assembly
por: Abelein, Axel
Publicado: (2023)

Expression of the human molecular chaperone domain Bri2 BRICHOS on a gram per liter scale with an E. coli fed-batch culture
por: Schmuck, Benjamin, et al.
Publicado: (2021)

Amyloidogenic Nanoplaques in Cerebrospinal Fluid: Relationship to Amyloid Brain Uptake and Clinical Alzheimer’s Disease in a Memory Clinic Cohort
por: Aksnes, Mari, et al.
Publicado: (2020)

Protein plasticity underlines activation and function of ATP-independent chaperones
por: Suss, Ohad, et al.
Publicado: (2015)

Mechanism of the small ATP-independent chaperone Spy is substrate specific
por: Mitra, Rishav, et al.
Publicado: (2021)

Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation–inert complex
por: Wallin, Cecilia, et al.
Publicado: (2020)

Machine to smash the smallest
Publicado: (1965)

ATP-Driven Molecular Chaperone Machines
por: Clare, Daniel K, et al.
Publicado: (2013)

Protein folding occurs while bound to the ATP-independent chaperone Spy
por: Stull, Frederick, et al.
Publicado: (2015)

Insights into the client protein release mechanism of the ATP-independent chaperone Spy
por: He, Wei, et al.
Publicado: (2022)

Smallest Organism; Highest Threat
por: Pant, Amit, et al.
Publicado: (2012)

Structure of the Brain of the Smallest Coleoptera
por: Makarova, A. A., et al.
Publicado: (2022)

A Disorder-to-Order Transition Activates an ATP-Independent Membrane Protein Chaperone
por: Siegel, Alex, et al.
Publicado: (2020)

Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation
por: Nagaraj, Madhu, et al.
Publicado: (2021)

A Tetrahymena Hsp90 co-chaperone promotes siRNA loading by ATP-dependent and ATP-independent mechanisms
por: Woehrer, Sophie L, et al.
Publicado: (2015)

A prion-like domain in Hsp42 drives chaperone-facilitated aggregation of misfolded proteins
por: Grousl, Tomas, et al.
Publicado: (2018)

“Pomacytosis”—Semi-extracellular phagocytosis of cyanobacteria by the smallest marine algae
por: Kamennaya, Nina A., et al.
Publicado: (2018)

The smallest chemical reaction system with bistability
por: Wilhelm, Thomas
Publicado: (2009)

Cannot write session to /tmp/vufind_sessions/sess_vfs4774faep6lg8216soe9e4so