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P2‐155: THIOREDOXIN 80 MAINTAINS INSULIN ACTIVITY BY PREVENTING ITS AGGREGATION: IMPLICATIONS FOR ALZHEIMER'S DISEASE.
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- Alzheimer's & Dementia: The Journal of the Alzheimer's Association, 2018, v. 14, p. P727, doi. 10.1016/j.jalz.2018.06.842
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- Article
The heat shock protein LarA activates the Lon protease in response to proteotoxic stress.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-43385-x
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- Article
High intracellular stability of the spidroin N‐terminal domain in spite of abundant amyloidogenic segments revealed by in‐cell hydrogen/deuterium exchange mass spectrometry.
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- FEBS Journal, 2020, v. 287, n. 13, p. 2823, doi. 10.1111/febs.15169
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- Article
Augmentation of Bri2 molecular chaperone activity against amyloid-β reduces neurotoxicity in mouse hippocampus in vitro.
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- Communications Biology, 2020, v. 3, n. 1, p. 1, doi. 10.1038/s42003-020-0757-z
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- Article
Spider Silk Protein Forms Amyloid‐Like Nanofibrils through a Non‐Nucleation‐Dependent Polymerization Mechanism (Small 46/2023).
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- Small, 2023, v. 19, n. 46, p. 1, doi. 10.1002/smll.202370388
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- Article
Spider Silk Protein Forms Amyloid‐Like Nanofibrils through a Non‐Nucleation‐Dependent Polymerization Mechanism.
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- Small, 2023, v. 19, n. 46, p. 1, doi. 10.1002/smll.202304031
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- Article
Maresin 1 attenuates pro‐inflammatory activation induced by β‐amyloid and stimulates its uptake.
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- Journal of Cellular & Molecular Medicine, 2021, v. 25, n. 1, p. 434, doi. 10.1111/jcmm.16098
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- Article
Spiders Use Structural Conversion of Globular Amyloidogenic Domains to Make Strong Silk Fibers (Adv. Funct. Mater. 23/2024).
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- Advanced Functional Materials, 2024, v. 34, n. 23, p. 1, doi. 10.1002/adfm.202470130
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- Article
Spiders Use Structural Conversion of Globular Amyloidogenic Domains to Make Strong Silk Fibers.
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- Advanced Functional Materials, 2024, v. 34, n. 23, p. 1, doi. 10.1002/adfm.202315409
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- Article
Recombinant Bri3 BRICHOS domain is a molecular chaperone with effect against amyloid formation and non-fibrillar protein aggregation.
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- Scientific Reports, 2020, v. 10, n. 1, p. 1, doi. 10.1038/s41598-020-66718-y
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- Article
Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.
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- Nature Communications, 2017, v. 8, n. 1, p. 1, doi. 10.1038/s41467-017-02056-4
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- Article
Advances in mass spectrometry to unravel the structure and function of protein condensates.
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- Nature Protocols, 2023, v. 18, n. 12, p. 3653, doi. 10.1038/s41596-023-00900-0
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- Article
Short hydrophobic loop motifs in BRICHOS domains determine chaperone activity against amorphous protein aggregation but not against amyloid formation.
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- Communications Biology, 2023, v. 6, n. 1, p. 1, doi. 10.1038/s42003-023-04883-2
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- Article
Molecular basis for different substrate‐binding sites and chaperone functions of the BRICHOS domain.
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- Protein Science: A Publication of the Protein Society, 2024, v. 33, n. 7, p. 1, doi. 10.1002/pro.5063
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- Article
A new kid in the folding funnel: Molecular chaperone activities of the BRICHOS domain.
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- Protein Science: A Publication of the Protein Society, 2023, v. 32, n. 6, p. 1, doi. 10.1002/pro.4645
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- Article
ATP‐independent molecular chaperone activity generated under reducing conditions.
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- Protein Science: A Publication of the Protein Society, 2022, v. 31, n. 8, p. 1, doi. 10.1002/pro.4378
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- Article