Výsledky vyhledávání - "70-KILODALTON HEAT SHOCK PROTEIN (HSP70)"

Disassembly of Tau fibrils by the human Hsp70 disaggregation machinery generates small seeding-competent species

Autor: Karine Madiona, Axel Mogk, Taxiarchis Katsinelos, Eliana Nachman, Bernd Bukau, Harm H. Kampinga, Luc Bousset, Anne S. Wentink, Kieren Allinson, Ronald Melki, William A. McEwan, Thomas R. Jahn, Carmen Nussbaum-Krammer

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2020, pp.jbc.RA120.013478. ⟨10.1074/jbc.RA120.013478⟩
The Journal of Biological Chemistry
Journal of Biological Chemistry, 2020, 295, pp.9676-9690. ⟨10.1074/jbc.ra120.013478⟩
Journal of Biological Chemistry, 295(28), 9676-9690. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Journal of Biological Chemistry, 2020, pp.jbc.RA120.013478. ⟨10.1074/jbc.RA120.013478⟩

International audience; The accumulation of amyloid Tau aggregates is implicated in Alzheimer’s disease (AD) and other tauopathies. Molecular chaperones are known to maintain protein homeostasis. Here, we show that an ATP-dependent human chaperone

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7af836307ca07fe8d853086203e2ea9b
https://hal-cea.archives-ouvertes.fr/cea-02733373

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Pharmacological induction of heat shock proteins ameliorates toxicity of mutant PKCγ in spinocerebellar ataxia type 14

Autor: Naoko Adachi, Hideyuki Takahashi, Naoaki Saito, Takehiko Ueyama, Takahiro Seki, Norio Sakai, Aoi Nakazono, Daizo Hamada

Publikováno v: The Journal of biological chemistry. 293(38)

Amyloid and amyloid-like protein aggregations are hallmarks of multiple, varied neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. We previously reported that spinocerebellar ataxia type 14 (SCA14), a dominant-inherited neur

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283489869005571b2ef9a445dcfa6b6c
https://pubmed.ncbi.nlm.nih.gov/30093405

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Failed mitochondrial import and impaired proteostasis trigger SUMOylation of mitochondrial proteins

Autor: Florian Paasch, Stefan Jentsch, Fabian den Brave, Boris Pfander, Ivan Psakhye

Publikováno v: The Journal of Biological Chemistry
Journal of Biological Chemistry

Modification by the ubiquitin-like protein SUMO affects hundreds of cellular substrate proteins and regulates a wide variety of physiological processes. While the SUMO system appears to predominantly target nuclear proteins and, to a lesser extent, c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::265b15a85d568837beed22030409fda0
https://pubmed.ncbi.nlm.nih.gov/29183993

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Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance

Autor: Alex L, Lai, Eugenia M, Clerico, Mandy E, Blackburn, Nisha A, Patel, Carol V, Robinson, Peter P, Borbat, Jack H, Freed, Lila M, Gierasch

Publikováno v: The Journal of Biological Chemistry

Proteins are dynamic entities that populate conformational ensembles, and most functions of proteins depend on their dynamic character. Allostery, in particular, relies on ligand-modulated shifts in these conformational ensembles. Hsp70s are alloster

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1a2ad0ea5b6cb6d084f312557ffea4c1
https://pubmed.ncbi.nlm.nih.gov/28428246

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Modulation of the Chaperone DnaK Allosterism by the Nucleotide Exchange Factor GrpE*

Autor: Judit Perales-Calvo, Roberto Melero, María Ángeles Pérez-Calvo, Arturo Muga, Oscar Llorca, Lucía Quintana-Gallardo, Fernando Moro, José M. Valpuesta

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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10 p.-6 fig.
Hsp70 chaperones comprise two domains, the nucleotide-binding domain (Hsp70NBD), responsible for structural and functional changes in the chaperone, and the substrate-binding domain (Hsp70SBD), involved in substrate interaction. Sub

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13c134ffb4e32f431c56fb9cd4f77803
https://europepmc.org/articles/PMC4400324/

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NF-κB Transcriptional Activity Is Modulated by FK506-binding Proteins FKBP51 and FKBP52: A ROLE FOR PEPTIDYL-PROLYL ISOMERASE ACTIVITY*

Autor: Erlejman, Alejandra Giselle, de Leo, Sonia Alejandra, Mazaira, Gisela Ileana, Molinari, Alejandro Martín, Camisay, Maria Fernanda, Fontana, Vanina Andrea, Cox, Mark, Piwien Pilipuk, Graciela, Galigniana, Mario Daniel

Publikováno v: CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET

Hsp90 binding immunophilins FKBP51 and FKBP52 modulate steroid receptor trafficking and hormone-dependent biological responses. With the purpose to expand this model to other nuclear factors that are also subject to nuclear-cytoplasmic shuttling, we

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::03ee8912e2b194847d799d80b546a60d
https://europepmc.org/articles/PMC4176250/

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