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Corrigendum to “Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly” [FEBS Lett. 586 (2012) 3991–3995].
- Published in:
- 2013
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- Publication type:
- Correction notice
Transient small molecule interactions kinetically modulate amyloid β peptide self-assembly
- Published in:
- FEBS Letters, 2012, v. 586, n. 22, p. 3991, doi. 10.1016/j.febslet.2012.09.035
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- Publication type:
- Article
Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS.
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- Protein Science: A Publication of the Protein Society, 2024, v. 33, n. 8, p. 1, doi. 10.1002/pro.5091
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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
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
The hairpin conformation of the amyloid β peptide is an important structural motif along the aggregation pathway.
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- Journal of Biological Inorganic Chemistry (JBIC), 2014, v. 19, n. 4/5, p. 623, doi. 10.1007/s00775-014-1131-8
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- Article
Dementia-related Bri2 BRICHOS is a versatile molecular chaperone that efficiently inhibits Aβ42 toxicity in Drosophila.
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- Biochemical Journal, 2016, v. 473, n. 20, p. 3683, doi. 10.1042/BCJ20160277
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- Article
Increased CSF-decorin predicts brain pathological changes driven by Alzheimer's Aβ amyloidosis.
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- Acta Neuropathologica Communications, 2022, v. 10, n. 1, p. 1, doi. 10.1186/s40478-022-01398-5
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- Publication type:
- Article
Spidroin N-terminal domain forms amyloid-like fibril based hydrogels and provides a protein immobilization platform.
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- Nature Communications, 2022, v. 13, n. 1, p. 1, doi. 10.1038/s41467-022-32093-7
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- Article
Autophagy Impairment in App Knock-in Alzheimer's Model Mice.
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- Frontiers in Aging Neuroscience, 2022, v. 14, p. 1, doi. 10.3389/fnagi.2022.878303
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- Article
Isotope‐labeled amyloid‐β does not transmit to the brain in a prion‐like manner after peripheral administration.
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- EMBO Reports, 2022, v. 23, n. 7, p. 1, doi. 10.15252/embr.202154405
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- Article
Functionalization of amyloid fibrils via the Bri2 BRICHOS domain.
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- Scientific Reports, 2020, v. 10, n. 1, p. 1, doi. 10.1038/s41598-020-78732-1
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- Article
High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain.
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- Scientific Reports, 2020, v. 10, n. 1, p. 1, doi. 10.1038/s41598-019-57143-x
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- Article
Identification of potential aggregation hotspots on Aβ42 fibrils blocked by the anti-amyloid chaperone-like BRICHOS domain.
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- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-45192-4
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- Publication type:
- Article
Biophysical Studies of the Amyloid β-Peptide: Interactions with Metal Ions and Small Molecules.
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- ChemBioChem, 2013, v. 14, n. 14, p. 1692, doi. 10.1002/cbic.201300262
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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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- Publication type:
- 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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- Publication type:
- Article
Decorin is an early CSF biomarker of Alzheimer's Aβ amyloidosis.
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- Alzheimer's & Dementia: The Journal of the Alzheimer's Association, 2021, v. 17, p. 1, doi. 10.1002/alz.054474
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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