Cargando…

Computational Analysis of the Interactions between the S100B Extracellular Chaperone and Its Amyloid β Peptide Client

S100B is an astrocytic extracellular Ca(2+)-binding protein implicated in Alzheimer’s disease, whose role as a holdase-type chaperone delaying Aβ(42) aggregation and toxicity was recently uncovered. Here, we employ computational biology approaches to dissect the structural details and dynamics of th...

Descripción completa

Detalles Bibliográficos
Autores principales:	Rodrigues, Filipe E. P., Figueira, António J., Gomes, Cláudio M., Machuqueiro, Miguel
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	MDPI 2021
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8037576/ https://www.ncbi.nlm.nih.gov/pubmed/33807304 http://dx.doi.org/10.3390/ijms22073629

Ejemplares similares

S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation
por: Figueira, António J., et al.
Publicado: (2023)

The mouse nicotinamide mononucleotide adenylyltransferase chaperones diverse pathological amyloid client proteins
por: Huang, Chengan, et al.
Publicado: (2022)

The interactions of molecular chaperones with client proteins: why are they so weak?
por: Arhar, Taylor, et al.
Publicado: (2021)

The chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogaster
por: Hermansson, Erik, et al.
Publicado: (2014)

Editorial: A focus on chaperone clients
por: Horovitz, Amnon, et al.
Publicado: (2023)

Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation
por: West, Jennifer, et al.
Publicado: (2021)

Amyloid-β peptide-induced extracellular S100A9 depletion is associated with decrease of antimicrobial peptide activity in human THP-1 monocytes
por: Lee, Eun Ok, et al.
Publicado: (2013)

The Collagen Chaperone HSP47 Is a New Interactor of APP that Affects the Levels of Extracellular Beta-Amyloid Peptides
por: Bianchi, Federico T., et al.
Publicado: (2011)

A molecular mechanism of chaperone-client recognition
por: He, Lichun, et al.
Publicado: (2016)

Molecular chaperones and their denaturing effect on client proteins
por: Hiller, Sebastian
Publicado: (2020)

A switch point in the molecular chaperone Hsp90 responding to client interaction
por: Rutz, Daniel Andreas, et al.
Publicado: (2018)

Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast
por: Killian, Andrea N., et al.
Publicado: (2019)

The Amyloid Forming Peptides Islet Amyloid Polypeptide and Amyloid β Interact at the Molecular Level
por: Wang, Ye, et al.
Publicado: (2021)

The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ
por: Williams, Danielle M., et al.
Publicado: (2021)

Anticholinergic Drugs Interact With Neuroprotective Chaperone L-PGDS and Modulate Cytotoxicity of Aβ Amyloids
por: Low, Kimberly Jia Yi, et al.
Publicado: (2020)

Ecological network analysis reveals cancer-dependent chaperone-client interaction structure and robustness
por: Galai, Geut, et al.
Publicado: (2023)

Molecular Chaperones Accelerate the Evolution of Their Protein Clients in Yeast
por: Alvarez-Ponce, David, et al.
Publicado: (2019)

Dealing with difficult clients via personalized chaperone inhibitors
por: Truman, Andrew W.
Publicado: (2021)

Intramembrane client recognition potentiates the chaperone functions of calnexin
por: Bloemeke, Nicolas, et al.
Publicado: (2022)

Pan-Cancer Analysis of Mitochondria Chaperone-Client Co-Expression Reveals Chaperone Functional Partitioning
por: Galai, Geut, et al.
Publicado: (2020)

Computational modeling of the effects of autophagy on amyloid-β peptide levels
por: Han, Kyungreem, et al.
Publicado: (2020)

Dynamic interactions and Ca(2+)-binding modulate the holdase-type chaperone activity of S100B preventing tau aggregation and seeding
por: Moreira, Guilherme G., et al.
Publicado: (2021)

The C-terminal domain of the antiamyloid chaperone DNAJB6 binds to amyloid-β peptide fibrils and inhibits secondary nucleation
por: Österlund, Nicklas, et al.
Publicado: (2023)

Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins
por: Smith, Jennifer R., et al.
Publicado: (2013)

Tailoring Hydrophobic Interactions between Probes and Amyloid-β Peptides for Fluorescent Monitoring of Amyloid-β Aggregation
por: Kim, Sonam, et al.
Publicado: (2018)

Preventing β-amyloid fibrillization and deposition: β-sheet breakers and pathological chaperone inhibitors
por: Wisniewski, Thomas, et al.
Publicado: (2008)

The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation
por: Cristóvão, Joana S., et al.
Publicado: (2018)

Chaperone activation and client binding of a 2-cysteine peroxiredoxin
por: Teixeira, Filipa, et al.
Publicado: (2019)

How do Chaperones Bind (Partly) Unfolded Client Proteins?
por: Sučec, Iva, et al.
Publicado: (2021)

Hsp110 Chaperones Control Client Fate Determination in the Hsp70–Hsp90 Chaperone System
por: Mandal, Atin K., et al.
Publicado: (2010)

Amyloid-β oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation
por: Österlund, Nicklas, et al.
Publicado: (2020)

On the Conformational Dynamics of β-Amyloid Forming Peptides: A Computational Perspective
por: Saravanan, Konda Mani, et al.
Publicado: (2020)

Amyloid-β Processing in Aged S100B Transgenic Mice Is Sex Dependent
por: Wartchow, Krista Minéia, et al.
Publicado: (2021)

Interfacial Dynamics and Growth Modes of β(2)-Microglobulin Dimers
por: Oliveira, Nuno F. B., et al.
Publicado: (2023)

Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
por: Li, Ting, et al.
Publicado: (2018)

Interaction Mechanism Between the HSV-1 Glycoprotein B and the Antimicrobial Peptide Amyloid-β
por: Bourgade, Karine, et al.
Publicado: (2022)

Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides
por: Silva, Tomás F. D., et al.
Publicado: (2023)

Interaction of the Molecular Chaperone DNAJB6 with Growing Amyloid-beta 42 (Aβ42) Aggregates Leads to Sub-stoichiometric Inhibition of Amyloid Formation
por: Månsson, Cecilia, et al.
Publicado: (2014)

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

Hypocretin and brain β-amyloid peptide interactions in cognitive disorders and narcolepsy
por: Dauvilliers, Yves A., et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_ajp9b24e473nfjv20u6jgnprm6